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Ingredients Technical Write To Karl Loren Table Of Contents

Arginine

Both Life Glow Plus and Super Life Glow contain a large quantity of the amino acid, Arginine.  Here are 50 scientific studies about that substance.

 

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Click On The Link/Number To Review The Study
Number Title Comment
...1...
Hyperargininemia, epilepsy and the metabolism of guanidino compounds.

 

...2...
Conditional deficiencies of ornithine or arginine.
...3...
Orotic acid, arginine, and hepatotoxicity.
...4...
Prostaglandins and the alpha-cell.
...5...
Regulation of polyamine biosynthesis by antizyme and some recent developments relating the induction of polyamine biosynthesis to cell growth. Review.

 

...6...
Arginine vasotocin as a pineal hormone.
...7...
Treating severe metabolic alkalosis.
...8... Immunonutrition: the role of arginine.
...9...
The development and function of the endocrine pancreas of fetuses and infants born to normal and diabetic mothers.

 

...10...
Drug-induced hyperkalemia.
Menu Position #10
...11...
Glucose regulation in non-insulin-dependent diabetes mellitus. Interaction between pancreatic islets and the liver.
...12...
Treatment strategies for patients with non-insulin-dependent diabetes mellitus.

 

...13...
Conversion factors of high- to low-molecular-weight forms of atrial natriuretic factor.
...14...
Dietary protein effects on cholesterol and lipoprotein concentrations: a review.

 

...15...
Effect of ethanol on spontaneous and stimulated growth hormone secretion.
...16...
Design of nitric oxide synthase inhibitors and their use to reverse hypotension associated with cancer immunotherapy.

 

...17...
Recent advances: parenteral nutrition support.
...18...
Use of nitric oxide synthase inhibitors as a novel treatment for septic shock.
...19...
Characterization of mammalian ADP-ribosylation cycles.

 

...20...
Disorders of prolactin and growth hormone secretion.

 

Menu Position #20
...21...
Islet-cell abnormalities in non-insulin-dependent diabetes mellitus.
...22...
Selective pharmacological inhibition of distinct nitric oxide synthase isoforms.

 

...23...
Vascular biology: relevance of nitric oxide in vascular and nonvascular tissue with normal and decreased renal function.

 

...24...
Recent progress in pharmacological therapy of male subfertility--a review.

 

...25...
Endothelial dysfunction in chronic heart failure. Experimental and clinical studies.

 

...26...
Beneficial circulatory effect of L-arginine.
...27...
Nitric oxide in essential and renal hypertension [editorial]
...28...
Protein metabolism in the cancer patient.

 

...29...
Arginine: new and exciting developments for an "old" amino acid.
...30...
Endothelial function in hypertension.
Menu Position #30
...31...
Role of arginine in health and in renal disease [editorial]
...32...
ADP-ribosylarginine hydrolases and ADP-ribosyltransferases. Partners in ADP-ribosylation cycles.
...33...
Alternative pathway therapy for urea cycle disorders.

 

...34...
Invited opinion: role of nitric oxide in hemorrhagic, traumatic, and anaphylactic shock and thermal injury.
...35...
Mono(ADP-ribosyl)transferases and related enzymes in animal tissues. Emerging gene families.
...36...
Apparent affinity and potency of BIBP3226, a non-peptide neuropeptide Y receptor antagonist, on purported neuropeptide Y Y1, Y2 and Y3 receptors.

 

...37...
Nitric oxide as a neurotransmitter in human airways.
...38...
New biomarkers of Maillard reaction damage to proteins.
...39...
Modulation of coronary autoregulatory responses by endothelium-derived nitric oxide.

 

...40...
BIBP 3226, the first selective neuropeptide Y1 receptor antagonist: a review of its pharmacological properties.
Menu Position #40
...41...
The role of orthotopic liver transplantation in the treatment of ornithine transcarbamylase deficiency.

 

...42...
Renal endothelial function in humans.
...43...
Cardiovascular effects of L-arginine.

 

Regardless of the mechanism, a wide array of cardiovascular disorders characterized by endothelial dysfunction are reversible by L-arginine.
...44...
Enhancement of nitric oxide synthesis by L-arginine supplementation in renal disease: is it good or bad?
...45...
Cytokines and L-arginine in renal injury and repair [editorial]
...46...
L-arginine and malignant disease: a potential therapeutic role?
The beneficial effects of L-arginine on nitrogen metabolism, wound healing and host defences demonstrated in animal studies have been shown to be significant in patient studies as well.
...47...
Can arginine and ornithine support gut functions?

 

...48...
Impact of the L-arginine/nitric oxide system in pregnancy.
...49...
Nitric oxide in the regulation of renal blood flow.
...50...
Advanced glycation end-products in diabetic nephropathy.

 


HealthGate Document


Record 1 from database: MEDLINE
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Title
Hyperargininemia, epilepsy and the metabolism of guanidino compounds.
Author
Wiechert P; Marescau B; De Deyn PP; Lowenthal A
Address
Source
Padiatr Grenzgeb, 1989, 28:2, 101-6
Abstract
Patients with hyperargininemia have an arginase deficiency which leads to blockade of the urea cycle in the last step with several clinical symptoms. Owing to the arginase deficiency this patients accumulate arginine which leads to eventual alternative yet unknown pathways of arginine metabolism. These clinical and biochemical findings intensified the research on guanidino compounds. It has been shown that most of the guanidino compounds are epileptogenic. Therefore we investigated the levels of 12 guanidino compounds in serum and brain of audiogenic sensitive rats. The changes of some guanidino compounds in serum and brain will be discussed.
Language of Publication
English
Unique Identifier
89263307

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MeSH Heading (Major)
Amino Acid Metabolism, Inborn Errors|BL/*GE; Arginase|*DF; Arginine|*BL; Epilepsy|BL/*GE; Guanidines|*BL
MeSH Heading
Brain|ME; Child; Human; Support, Non-U.S. Gov't

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0030-932X
Country of Publication
GERMANY, EAST
CAS Registry/EC Number
EC 3.5.3.1 (Arginase); 0 (Guanidines); 7004-12-8 (Arginine)


Record 2 from database: MEDLINE
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Title
Conditional deficiencies of ornithine or arginine.
Author
Zieve L
Address
Source
J Am Coll Nutr, 1986, 5:2, 167-76
Abstract
Relative deficiencies of ornithine or arginine occur in the presence of excessive ammonia, excessive lysine, growth, pregnancy, trauma, or protein deficiency and malnutrition. Ammonia excess may occur in the presence of a normal liver when amino acid mixtures lacking ornithine, arginine, or citrulline are infused; when specific amino acids such as glycine are injected; when ammonium salts, urea, or urease are injected; or when the gastrointestinal tract contains an excess of protein, urea, or NH4+, as occurs after a gastrointestinal hemorrhage. In these states, ornithine is often rate-limiting for urea cycle function. Ornithine is also rate-limiting when ammonia excess occurs in the presence of hepatic failure. In three of the inherited urea cycle disorders, ornithine insufficiency and ammonia excess also occur. These disorders are citrullinemia, argininosuccinic aciduria, and argininemia. In the presence of excessive lysine the availability of arginine is reduced and the formation of ornithine is decreased in the liver; urea synthesis is reduced, but orotic acid synthesis is increased, and orotic aciduria results as carbamyl phosphate is directed toward the pyrimidine pathway. Hereditary lysinuric protein intolerance results in ornithine depletion, hyperammonemia, and orotic acid uria. Optimal growth in several species of animals requires 0.4-1.0% arginine in the diet. Diets deficient in arginine are associated with poor wound healing as well as stunted growth. The measurement of orotic acid excretion has been a convenient indicator of insufficiency of ornithine or arginine during growth or pregnancy in animals and should prove useful in assessing the requirement for arginine after trauma. Normal human pregnancy is associated with low-grade orotic aciduria. Protein deficiency and malnutrition increase the vulnerability of the animal or child to ammonia toxicity. This is presumably due to insufficient ornithine for normal urea cycle responsiveness.
Language of Publication
English
Unique Identifier
86251831

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MeSH Heading (Major)
Arginine|*DF; Ornithine|*DF
MeSH Heading
Amino Acids|AD; Amino Acids, Branched-Chain|AN; Ammonia|TO; Animal; Citrulline|PH; Female; Glycine|TO; Hepatic Encephalopathy|BL; Human; Liver Cirrhosis|BL; Lysine|TO; Models, Biological; Orotic Acid|UR; Pregnancy; Protein Deficiency|CO; Urease|ME

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0731-5724
Country of Publication
UNITED STATES
CAS Registry/EC Number
EC 3.5.1.5 (Urease); 0 (Amino Acids); 0 (Amino Acids, Branched-Chain); 372-75-8 (Citrulline); 56-40-6 (Glycine); 56-87-1 (Lysine); 65-86-1 (Orotic Acid); 7004-12-8 (Arginine); 7006-33-9 (Ornithine); 7664-41-7 (Ammonia)


Record 3 from database: MEDLINE
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Title
Orotic acid, arginine, and hepatotoxicity.
Author
Visek WJ; Shoemaker JD
Address
Source
J Am Coll Nutr, 1986, 5:2, 153-66
Abstract
This communication presents evidence from the literature and recent experiments that describe circumstances wherein arginine may be a conditional dietary essential. Previous work has established that the synthesis of orotic acid (OA), the first pyrimidine formed in the de novo pathway of nucleic acid synthesis, becomes elevated whenever the ammonia load exceeds the capacity of the urea cycle. Under these circumstances, the common intermediate, carbamyl phosphate, leaks from the mitochondria and induces OA synthesis in the cytoplasm. This leads to increased OA excretion in the urine as pyrimidine synthesis escapes feedback control. A deficiency of urea cycle substrates such as arginine, and administration of certain drugs, ammonium salts, urease, or excess amino acids raises orotic acid excretion. Our recent experiments in rats show that OA excretion is also elevated after partial hepatectomy following galactosamine administration, exposure to carbon tetrachloride, or feeding 36% of calories as ethanol. The elevation in OA excretion was suppressed by dietary supplementation with arginine, implying that arginine is conditionally essential. Adult human male alcoholics showed elevated urinary orotic acid-to-creatinine ratios early after drinking episodes, which declined with time following abstinence. Such evidence shows that well studied hepatotoxins and surgical liver injury affect pathways of ammonia metabolism and suggests that urinary orotic acid can be an indicator of hepatotoxicity and increased needs for arginine. Arginine-deficient diets and alcohol feeding both enhance fatty deposition in the liver, which can be worsened by high fat intakes in rats. Alcoholism, various other diseases, and fasting and realimentation change orotic acid excretion. Such responses will have to be taken into account in establishing "normal values" for OA excretion.
Language of Publication
English
Unique Identifier
86251830

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MeSH Heading (Major)
Arginine|*PH; Liver|*DE/IN; Orotic Acid|*UR
MeSH Heading
Adult; Alcohol, Ethyl|ME; Alcoholism|UR; Ammonia|ME; Animal; Dietary Fats|PD; Dietary Proteins|PD; Fasting; Ferrets; Food; Human; Liver Diseases, Alcoholic|DI/UR; Liver Regeneration; Male; Models, Biological; Rats; Reye's Syndrome|PP; Urea|BL

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0731-5724
Country of Publication
UNITED STATES
CAS Registry/EC Number
0 (Dietary Fats); 0 (Dietary Proteins); 57-13-6 (Urea); 64-17-5 (Alcohol, Ethyl); 65-86-1 (Orotic Acid); 7004-12-8 (Arginine); 7664-41-7 (Ammonia)


Record 4 from database: MEDLINE
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Title
Prostaglandins and the alpha-cell.
Author
Giugliano D; Torella R; D'Onofrio F
Address
Source
Prostaglandins Med, 1981 Mar, 6:3, 283-97
Abstract
Experimental evidence has recently accumulated indicating that administration of some prostaglandins (PGs), particularly those of the E series, can evoke release of glucagon by the pancreatic alpha-cells. Virtually, all the in vitro studies (isolated perfused rat pancreas, isolated guinea-pig islets) agree that PGs can increase both basal and stimulated glucagon release. On the other hand, inhibition of PG synthesis with indomethacin blocks glucagon release. In rats and in normal humans, PGE1, but not PGA2 or PGF2a, causes a progressive rise of plasma glucagon levels. While in the rat this response seems independent of the adrenergic nervous system, in man the hyperglucagonemia induced by PGE1 is easily suppressed by propranolol, suggesting an interaction between the prostaglandin and the beta-receptors of the alpha-cell. Studies with inhibitors of PG synthesis in vivo have yielded conflicting results, depending on the particular experimental protocol used and on the type of inhibitor tested. In normal humans, it seems that acetylsalicylic acid (ASA) has no effect on glucagon response to arginine, tolbutamide and insulin-induced hypoglycemia. Conversely, a stimulator of PG synthesis, such as furosemide, increases glucagon response to an arginine pulse in man. In insulin-dependent diabetics, who present an exaggerated glucagon response to stimulants, ASA fails to alter glucagon response to arginine, but completely blunts the glucagon response to salbutamol, a weak beta-2 receptor agonist. In conclusion, these observations provide evidence in support to a role for PGs, at least PGE, in the contro of glucagon release.
Language of Publication
English
Unique Identifier
81175420

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MeSH Heading (Major)
Glucagon|*SE; Islets of Langerhans|DE/*SE; Prostaglandins|*PH
MeSH Heading
Albuterol|DU; Animal; Arginine|DU; Aspirin|DU; Blood Glucose|ME; Diabetes Mellitus|ME; Furosemide|DU; Guinea Pigs; Human; Indomethacin|PD; Kinetics; Propranolol|DU; Prostaglandins E|DU; Rats

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0161-4630
Country of Publication
UNITED STATES
CAS Registry/EC Number
0 (Blood Glucose); 0 (Prostaglandins E); 0 (Prostaglandins); 18559-94-9 (Albuterol); 50-78-2 (Aspirin); 525-66-6 (Propranolol); 53-86-1 (Indomethacin); 54-31-9 (Furosemide); 7004-12-8 (Arginine); 9007-92-5 (Glucagon)


Record 5 from database: MEDLINE
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Title
Regulation of polyamine biosynthesis by antizyme and some recent developments relating the induction of polyamine biosynthesis to cell growth. Review.
Author
Canellakis ES; Kyriakidis DA; Rinehart CA Jr; Huang SC; Panagiotidis C; Fong WF
Address
Source
Biosci Rep, 1985 Mar, 5:3, 189-204
Abstract
This review considers the role of antizyme, of amino acids and of protein synthesis in the regulation of polyamine biosynthesis. The ornithine decarboxylase of eukaryotic cells and of Escherichia coli can be non-competitively inhibited by proteins, termed antizymes, which are induced by di- and poly- amines. Some antizymes have been purified to homogeneity and have been shown to be structurally unique to the cell of origin. Yet, the E. coli antizyme and the rat liver antizyme cross react and inhibit each other's biosynthetic decarboxylases. These results indicate that aspects of the control of polyamine biosynthesis have been highly conserved throughout evolution. Evidence for the physiological role of the antizyme in mammalian cells rests upon its identification in normal uninduced cells, upon the inverse relationship that exists between antizyme and ornithine decarboxylase as well as upon the existence of the complex of ornithine decarboxylase and antizyme in vivo. Furthermore, the antizyme has been shown to be highly specific; its Keq for ornithine decarboxylase is 1.4 X 10(11) M-1. In addition, mammalian cells contain an anti-antizyme, a protein that specifically binds to the antizyme of an ornithine decarboxylase-antizyme complex and liberates free ornithine decarboxylase from the complex. In E. coli, in which polyamine biosynthesis is mediated both by ornithine decarboxylase and by arginine decarboxylase, three proteins (one acidic and two basic) have been purified, each of which inhibits both these enzymes. They do not inhibit the biodegradative ornithine and arginine decarboxylases nor lysine decarboxylase. The two basic inhibitors have been shown to correspond to the ribosomal proteins S20/L26 and L34, respectively. The relationship of the acidic antizyme to other known E. coli proteins remains to be determined. In mammalian cells, ornithine decarboxylase can be induced by a broad spectrum of compounds. These range from hormones and growth factors to natural amino acids such as asparagine and to non-metabolizable amino acid analogues such as alpha-amino-isobutyric acid. The amino acids that induce ornithine decarboxylase as well as those that promote polyamine uptake utilize the sodium dependent A and N transport systems. Consequently, they act in concert and increase intracellular polyamine levels by both mechanisms. The induction of ornithine decarboxylase by growth factors, such as NGF, EGF, and PDGF as well as by insulin requires the presence of these same amino acids and does not occur in their absence. However, the inducing amino acid need not be incorporated into protein nor covalently modified.(ABSTRACT TRUNCATED AT 400 WORDS)
Language of Publication
English
Unique Identifier
85253067

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MeSH Heading (Major)
Ornithine Decarboxylase|*AI/ME; Polyamines|*BI; Proteins|*PH
MeSH Heading
Amino Acids|ME/PH; Animal; Arginine|ME; Bacterial Proteins|PH; Biological Transport, Active; Carboxy-Lyases|AI; Enzyme Activation; Escherichia coli|ME; Human; Liver|EN; Ornithine|ME; Rats; Ribosomal Proteins|PH; Species Specificity; Substrate Specificity; Support, U.S. Gov't, P.H.S.

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0144-8463
Country of Publication
ENGLAND
CAS Registry/EC Number
EC 4.1.1. (Carboxy-Lyases); EC 4.1.1.17 (Ornithine Decarboxylase); EC 4.1.1.18 (lysine decarboxylase); EC 4.1.1.19 (arginine decarboxylase); 0 (ornithine decarboxylase antizyme inhibitor); 0 (ornithine decarboxylase antizyme); 0 (ribosomal protein L34); 0 (ribosomal protein S20-L26); 0 (Amino Acids); 0 (Bacterial Proteins); 0 (Polyamines); 0 (Ribosomal Proteins); 7004-12-8 (Arginine); 7006-33-9 (Ornithine)


Record 6 from database: MEDLINE
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Title
Arginine vasotocin as a pineal hormone.
Author
Pavel S
Address
Source
J Neural Transm Suppl, 1978, :13, 135-55
Abstract
The pineal nonapeptide hormone arginine vasotocin (AVT) is synthesized by the ependymal cells of the pineal recess and subcommissural organ and stored in so far undefined cells of the pineal gland proper. AVT is first released into the cerebrospinal fluid (CSF) and reaches the blood only secondarily after its absorption from CSF. It displays a diurnal rhythm in the pineal and CSF, suggesting its release into the CSF during the night in the dark. Melatonin represents its releasing hormone. AVT exerts both its endocrine and non-endocrine effects by a unique mechanism involving the activation of serotonin neurotransmission in the brain with resultant inhibition of release of hypothalamic releasing and inhibiting hormones and induction of sleep. It produces both its endocrine effects and sleep at concentrations equivalent to only several hundreds of molecules, being thus by far the most active hormone so far known. Midbrain raphe nuclei or some structures intimately correlated with these cell bodies, most contain the extremely sensitive and specific AVT receptors in the mammalian brain. In contrast with its natural analogues arginine vasopressin and oxytocin which are mainly blood hormones, AVT is a CSF hormone whose major if not the sole site of action is the brain itself.
Language of Publication
English
Unique Identifier
79241098

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MeSH Heading (Major)
Hypothalamus|*PH; Pineal Body|*PH; Prolactin|*SE; Vasotocin|CF/PD/*PH
MeSH Heading
Animal; Arginine; Corticotropin|SE; Gonadotropins|SE; Human; MSH|SE; Serotonin|ME; Sleep

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0303-6995
Country of Publication
AUSTRIA


Record 7 from database: MEDLINE
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Title
Treating severe metabolic alkalosis.
Author
Martin WJ; Matzke GR
Address
Source
Clin Pharm, 1982 Jan-Feb, 1:1, 42-8
Abstract
The pathophysiology, symptomatology, and treatment of metabolic alkalosis are reviewed, with emphasis on treatment with intravenous hydrochloric acid. Three buffering systems are used by the body to correct an arterial pH above 7.45--tissue, respiratory, and renal systems. The kidneys have the primary responsibility for correcting a severe metabolic alkalosis, but several conditions (e.g., severe volume contraction) can interfere with the renal mechanisms. No unique symptoms are associated with metabolic alkalosis. Conventional conservative treatment of metabolic alkalosis involves meeting the patient's fluid and electrolyte needs and allowing the body to correct the alkalosis through its own mechanisms. However, when more rapid resolution of the alkalosis is needed or the patient cannot tolerate fluid and electrolyte therapy, mineral acids may be administered. Ammonium chloride and arginine monohydrochloride infusions may both be used; since both require hepatic conversion for full activity, patients with hepatic dysfunction may require alternative therapy. Dilute hydrochloric acid (0.1-0.2 N) may be given intravenously to these patients through a central-venous catheter. Dosage guidelines and formulation procedures are described in the paper, as are other possible therapeutic alternatives (dialysis, acetazolamide, cimetidine). Most cases of metabolic alkalosis can be managed with fluid and electrolyte therapy. When metabolic alkalosis needs to be resolved quickly or when conventional therapy cannot be tolerated, mineral acid administration should be instituted. The primary drug of choice for these patients is intravenous ammonium chloride; patients with hepatic or severe renal dysfunction should receive dilute hydrochloric acid via a central-venous catheter.
Language of Publication
English
Unique Identifier
83260265

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MeSH Heading (Major)
Alkalosis|*DT/PP
MeSH Heading
Acetazolamide|TU; Ammonium Chloride|TU; Arginine|TU; Case Report; Cimetidine|TU; Human; Hydrochloric Acid|AD/TU; Male; Middle Age

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0278-2677
Country of Publication
UNITED STATES
CAS Registry/EC Number
12125-02-9 (Ammonium Chloride); 51481-61-9 (Cimetidine); 59-66-5 (Acetazolamide); 7004-12-8 (Arginine); 7647-01-0 (Hydrochloric Acid)


Record 8 from database: MEDLINE
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Title
Immunonutrition: the role of arginine.
Author
Evoy D; Lieberman MD; Fahey TJ 3rd; Daly JM
Address
Department of Surgery, New York Hospital, Cornell Medical Center, New York 10021, USA.
Source
Nutrition, 1998 Jul-Aug, 14:7-8, 611-7
Abstract
Clearly, arginine has great potential as an immunomodulator and may prove useful in catabolic conditions such as severe sepsis and postoperative stress. there is a body of evidence suggesting that supplemental arginine upregulates immune function and reduces the incidence of postoperative infection. More modest improvements in nitrogen balance have been observed. Tumor response to arginine appears to depend on the immunogenicity of the particular tumor and on the requirement of arginine by the tumor as a growth substrate. Of note, ornithine shares the thymotrophic, immunostimulatory and secretagogue effects of arginine. It is, therefore, likely that these compounds share the same cellular mechanism of action or that arginine acts via increasing the concentration of available ornithine. The role of arginine in the injured patient and in the tumor-bearing host demands additional study based on the promising experimental evidence regarding the supplemental use of arginine.
Language of Publication
English
Unique Identifier
98348890

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MeSH Heading (Major)
Arginine|AD/CH/ME/*PH; Immunity|*; Nutrition|*
MeSH Heading
Animal; Dietary Supplements; Human; Postoperative Complications; Sepsis; Wounds and Injuries

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0899-9007
Country of Publication
UNITED STATES
CAS Registry/EC Number
7004-12-8 (Arginine)


Record 9 from database: MEDLINE
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Title
The development and function of the endocrine pancreas of fetuses and infants born to normal and diabetic mothers.
Author
Grasso S; Palumbo G; Fallucca F; Lanzafame S; Indelicato B; Sanfilippo S
Address
Source
Acta Endocrinol Suppl (Copenh), 1986, 277:, 130-5
Abstract
The development of the human endocrine pancreas is described. The hormone content and islet responsiveness of foetal and neonatal pancreases of diabetic and non-diabetic pregnant women are reported.
Language of Publication
English
Unique Identifier
87021893

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MeSH Heading (Major)
Islets of Langerhans|EM/*GD; Pregnancy in Diabetes|*CO
MeSH Heading
Alanine|DU; Arginine|DU; Blood Glucose|AN; Female; Glucagon|BL; Human; Infant, Newborn; Infant, Premature; Infant, Small for Gestational Age; Pregnancy; Protirelin|AN; Somatostatin|BL

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0300-9750
Country of Publication
DENMARK
CAS Registry/EC Number
0 (Blood Glucose); 24305-27-9 (Protirelin); 51110-01-1 (Somatostatin); 6898-94-8 (Alanine); 7004-12-8 (Arginine); 9007-92-5 (Glucagon)


Record 10 from database: MEDLINE
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Title
Drug-induced hyperkalemia.
Author
Ponce SP; Jennings AE; Madias NE; Harrington JT
Address
Source
Medicine (Baltimore), 1985 Nov, 64:6, 357-70
Abstract
After reviewing the available data on drug-induced hyperkalemia, we conclude that the situation has not improved since Lawson quantitatively documented the substantial risks of potassium chloride over a decade ago (90). As discussed, the risk of developing hyperkalemia in hospital remains at least at the range of 1 to 2% and can reach 10%, depending on the definition used (Table 2). Potassium chloride supplements and potassium-sparing diuretics remain the major culprits but they have been joined by a host of new actors, e.g., salt substitutes, beta-blockers, converting enzyme inhibitors, nonsteroidal antiinflammatory agents, and heparin, among others. Readily identifiable risk factors (other than drugs) for developing hyperkalemia are well-known but seem to be consistently ignored, even in teaching hospitals. The presence of diabetes mellitus, renal insufficiency, hypoaldosteronism, and age greater than 60 years results in a substantial increase in the risk of hyperkalemia from the use of any of the drugs we have reviewed. If prevention of hyperkalemia is the goal, as it should be, the current widespread and indiscriminate use of potassium supplements and potassium-sparing diuretics will need to end. We remain intrigued by Burchell's prescient pronouncement of over a decade ago that "more lives have been lost than saved by potassium therapy" (28).
Language of Publication
English
Unique Identifier
86039762

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MeSH Heading (Major)
Hyperkalemia|*CI/ET/PC; Potassium|*ME
MeSH Heading
Adrenergic beta-Antagonists|AE; Adrenergic Agonists|AE; Aged; Anti-Inflammatory Agents|AE; Arginine|AE; Blood Transfusion|AE; Body Fluid Compartments|ME; Cyclosporins|AE; Diacetylmorphine|AE; Digitalis Glycosides|AE; Diuretics|TU; Glucose|AE; Heparin|AE; Hormones|ME; Human; Hypertonic Solutions; Kidney|ME/TR; Kidney Transplantation; Lithium|AE; Middle Age; Peptidyl-Dipeptidase A|AI; Potassium Chloride|AE/TU; Prostaglandins|BI; Risk; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0025-7974
Country of Publication
UNITED STATES
CAS Registry/EC Number
EC 3.4.15.1 (Peptidyl-Dipeptidase A); 0 (Adrenergic beta-Antagonists); 0 (Adrenergic Agonists); 0 (Cyclosporins); 0 (Digitalis Glycosides); 0 (Diuretics); 0 (Hormones); 0 (Hypertonic Solutions); 0 (Prostaglandins); 50-99-7 (Glucose); 554-13-2 (Lithium Carbonate); 561-27-3 (Diacetylmorphine); 7004-12-8 (Arginine); 7439-93-2 (Lithium); 7440-09-7 (Potassium); 7447-40-7 (Potassium Chloride); 9005-49-6 (Heparin)


Record 11 from database: MEDLINE
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Title
Glucose regulation in non-insulin-dependent diabetes mellitus. Interaction between pancreatic islets and the liver.
Author
Halter JB; Ward WK; Porte D Jr; Best JD; Pfeifer MA
Address
Source
Am J Med, 1985 Aug 23, 79:2B, 6-12
Abstract
The degree of fasting hyperglycemia in patients with non-insulin-dependent diabetes mellitus is dependent on the rate of hepatic glucose production. The basal rate of hepatic glucose production is increased in patients with non-insulin-dependent diabetes mellitus, and there is a positive correlation between hepatic glucose production and fasting glucose levels. Diminished secretion of insulin, impaired hepatic sensitivity to insulin's effects, or a combination of these factors could contribute to the elevated hepatic glucose production in patients with non-insulin-dependent diabetes mellitus. The relationship between insulin secretion and hepatic glucose production is regulated by a closed feedback loop operating between glucose levels and pancreatic beta cells. Although fasting insulin levels are usually comparable between patients with non-insulin-dependent diabetes mellitus and normal subjects, insulin secretion is markedly impaired in non-insulin-dependent diabetes mellitus in relation to the degree of hyperglycemia present. In fact, the degree of fasting hyperglycemia in a given patient with non-insulin-dependent diabetes mellitus is closely related to the degree of impaired pancreatic beta-cell responsiveness to glucose. Such findings suggest that impaired insulin secretion leads to increased hepatic glucose production, which raises the plasma glucose level. The resulting hyperglycemia helps to maintain relatively normal basal insulin output. Chronic sulfonylurea drug therapy of patients with non-insulin-dependent diabetes mellitus enhances pancreatic islet sensitivity to glucose, leading to increased insulin secretion, suppression of hepatic glucose production, and a decline in the steady-state fasting glucose level.
Language of Publication
English
Unique Identifier
85304191

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MeSH Heading (Major)
Diabetes Mellitus, Non-Insulin-Dependent|*PP/TH; Glucose|*BI; Homeostasis|*; Islets of Langerhans|*PP; Liver|*PP
MeSH Heading
Arginine|DU; Blood Glucose|ME; Fasting; Fatty Acids, Nonesterified|ME; Feedback; Glucagon|PH; Gluconeogenesis; Glycogen|ME; Human; Insulin|SE/TU; Insulin Resistance; Somatostatin|PH; Sulfonylurea Compounds|TU; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0002-9343
Country of Publication
UNITED STATES
CAS Registry/EC Number
0 (Blood Glucose); 0 (Fatty Acids, Nonesterified); 0 (Sulfonylurea Compounds); 11061-68-0 (Insulin); 50-99-7 (Glucose); 51110-01-1 (Somatostatin); 7004-12-8 (Arginine); 9005-79-2 (Glycogen); 9007-92-5 (Glucagon)


Record 12 from database: MEDLINE
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Title
Treatment strategies for patients with non-insulin-dependent diabetes mellitus.
Author
Boden G
Address
Source
Am J Med, 1985 Aug 23, 79:2B, 23-6
Abstract
Strategies for the treatment of patients with non-insulin-dependent diabetes mellitus are discussed. In order to achieve treatment goals, diet and exercise remain important components of an overall treatment program that may include sulfonylurea drugs, especially in cases where patients are of normal weight or only slightly obese, have had the disease less than five years, and are taking little or no insulin. Failure to control blood sugar levels with sulfonylurea drugs may lead to combining this therapy with insulin or administering insulin alone, regardless of patients' weights.
Language of Publication
English
Unique Identifier
85304187

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MeSH Heading (Major)
Diabetes Mellitus, Non-Insulin-Dependent|DH/DT/*TH
MeSH Heading
Arginine|DU; Blood Glucose|ME; Blood Proteins|ME; Body Weight; Chlorpropamide|AE/TU; Diet, Reducing; Dietary Carbohydrates|AD; Dietary Fiber|TU; Drug Therapy, Combination; Exertion; Glucose Tolerance Test; Human; Insulin|AD/BL/TU; Sulfonylurea Compounds|AD/BL/TU; Support, U.S. Gov't, P.H.S.; Time Factors

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0002-9343
Country of Publication
UNITED STATES
CAS Registry/EC Number
0 (Blood Glucose); 0 (Blood Proteins); 0 (Sulfonylurea Compounds); 11061-68-0 (Insulin); 7004-12-8 (Arginine); 94-20-2 (Chlorpropamide)


Record 13 from database: MEDLINE
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Title
Conversion factors of high- to low-molecular-weight forms of atrial natriuretic factor.
Author
Trippodo NC; Januszewicz A; Cole FE; MacPhee AA; Pegram BL; Kardon MB
Address
Source
Fed Proc, 1986 Jun, 45:7, 2091-5
Abstract
The atrial natriuretic factor (ANF) is comprised of a 126-amino-acid precursor (pro-ANF) and its biologically active fragments. Partially purified pro-ANF and its larger fragments (greater than 10,000 daltons) have been referred to as high-molecular-weight (Mr) ANF, the partially purified smaller fragments (less than 10,000 daltons) as low Mr ANF. In vitro, mild proteolysis of high Mr ANF yielded low Mr ANF and enhanced biological activity. In the rat, pro-ANF was the predominant atrial form; however, low Mr ANF was largely released from isolated perfused hearts, which suggests that conversion of pro-ANF to low Mr ANF occurred immediately before or during secretion. High Mr ANF was also found in the perfusate of isolated rat hearts and in the plasma of rats, which suggests that some pro-ANF was secreted with low Mr ANF. Evidence for extraatrial conversion and activation of pro-ANF comes from two studies. 1) Intra-renal-arterial injection of high Mr ANF had little renal vascular action, whereas its i.v. injection caused renal vascular dilation, which suggests that the renal vasodilatory action of high Mr ANF became activated during circulation. 2) When high Mr ANF was incubated with rat blood or rat platelets in vitro, its natriuretic activity was converted to low Mr ANF within minutes; the platelet-induced conversion was associated with enhanced activity in relaxing aortic smooth muscle.
Language of Publication
English
Unique Identifier
86220856

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MeSH Heading (Major)
Atrial Natriuretic Factor|BL/*ME/PD; Protein Precursors|BL/*ME; Protein Processing, Post-Translational|*
MeSH Heading
Animal; Arginine|ME; Biological Assay; Cytoplasmic Granules|ME; Golgi Apparatus|ME; Heart Atrium|ME; Human; Kidney|BS; Microsomes|ME; Molecular Weight; Natriuresis; Peptide Fragments|ME; Peptide Hydrolases|ME; Rats; Signal Peptides|ME; Translation, Genetic; Trypsin|ME; Vascular Resistance|DE

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0014-9446
Country of Publication
UNITED STATES
CAS Registry/EC Number
EC 3.4 (Peptide Hydrolases); EC 3.4.21.4 (Trypsin); 0 (atrial natriuretic factor precursors); 0 (Peptide Fragments); 0 (Protein Precursors); 0 (Signal Peptides); 7004-12-8 (Arginine); 85637-73-6 (Atrial Natriuretic Factor)


Record 14 from database: MEDLINE
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Title
Dietary protein effects on cholesterol and lipoprotein concentrations: a review.
Author
Forsythe WA; Green MS; Anderson JJ
Address
Source
J Am Coll Nutr, 1986, 5:6, 533-49
Abstract
Different dietary proteins exert different effects on plasma cholesterol concentrations. Animal studies have shown that animal proteins, most notably casein, increase plasma total cholesterol concentrations compared with vegetable proteins, such as soy. Soy protein has been shown to be hypocholesterolemic in rats, swine, primates, and rabbits. Epidemiologic studies have disclosed that vegetarians have lower mean plasma cholesterol concentrations than populations consuming diets of mixed proteins, but it is unclear whether this effect results specifically from the animal or vegetable nature of the protein. In human clinical experiments, substituting soy protein for mixed protein reduces plasma total cholesterol concentration in hypercholesterolemic subjects, but it causes only a small, nonsignificant change in persons with normal plasma cholesterol concentrations. The mechanism responsible for the effects of different proteins on plasma cholesterol concentrations has not been established. One hypothesis suggests that animal proteins, which have a greater content of phosphorylated amino acids than vegetable proteins, interfere with bile acid reabsorption. Another hypothesis suggests that the amino acid content of the protein affects cholesterol absorption, tissue storage, synthesis, and excretion. The dietary protein may also alter cholesterol metabolism by affecting plasma hormone concentrations, either postprandially or over weeks to months. Among the hormones thought to be affected by dietary protein source are insulin, glucagon, and thyroid hormones. Gastrointestinal hormones, such as gastrointestinal inhibitory polypeptide, may also be affected by dietary protein.
Language of Publication
English
Unique Identifier
87058559

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MeSH Heading (Major)
Cholesterol|*BL; Dietary Proteins|*PD; Lipoproteins|*BL
MeSH Heading
Amino Acids|AN; Animal; Apolipoproteins|BL; Arginine|ME; Digestion; Glucagon|BL; Human; Insulin|BL; Intestinal Absorption; Lipoproteins, HDL Cholesterol|BL; Lipoproteins, LDL Cholesterol|BL; Lysine|ME; Saponins|ME; Sterols|ME; Tissue Distribution

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0731-5724
Country of Publication
UNITED STATES
CAS Registry/EC Number
0 (Amino Acids); 0 (Apolipoproteins); 0 (Dietary Proteins); 0 (Lipoproteins); 0 (Lipoproteins, HDL Cholesterol); 0 (Lipoproteins, LDL Cholesterol); 0 (Saponins); 0 (Sterols); 11061-68-0 (Insulin); 56-87-1 (Lysine); 57-88-5 (Cholesterol); 7004-12-8 (Arginine); 9007-92-5 (Glucagon)


Record 15 from database: MEDLINE
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Title
Effect of ethanol on spontaneous and stimulated growth hormone secretion.
Author
Redmond GP
Address
Source
Prog Biochem Pharmacol, 1981, 18:, 58-74
Abstract
Growth hormone (GH) regulates not only somatic growth but also carbohydrate, protein and lipid metabolism. Altered secretory states resulting from alcohol use could have pathogenetic significance. The pattern of spontaneous GH secretion in man is reviewed and previously published human studies on ethanol and GH examined to develop a coherent formulation of the nature of ethanol effects on GH secretion. The weight of the evidence suggests that ethanol suppresses GH secretion. Studies using the rat indicates that the dose-response relationship is of a threshold nature, with doses of 3 g/kg or greater abolishing spontaneous secretion. The possible role of diminished GH secretion in the pathogenesis of the fetal alcohol syndrome is discussed.
Language of Publication
English
Unique Identifier
82082674

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MeSH Heading (Major)
Alcohol, Ethyl|*PD; Somatotropin|*SE
MeSH Heading
Adult; Animal; Arginine|DU; Child; Circadian Rhythm; Corticotropin|DF; Fatty Acids, Nonesterified|BL; Female; Glucagon|PD; Human; Hydrocortisone|BL; Hypoglycemia|ME; LH|BL; Male; Prolactin|BL; Propranolol|PD; Rats; Support, U.S. Gov't, P.H.S.; Testosterone|BL

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0079-6085
Country of Publication
SWITZERLAND
CAS Registry/EC Number
0 (Fatty Acids, Nonesterified); 50-23-7 (Hydrocortisone); 525-66-6 (Propranolol); 57-85-2 (Testosterone); 64-17-5 (Alcohol, Ethyl); 7004-12-8 (Arginine); 9002-60-2 (Corticotropin); 9002-62-4 (Prolactin); 9002-67-9 (LH); 9002-72-6 (Somatotropin); 9007-92-5 (Glucagon)


Record 16 from database: MEDLINE
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Title
Design of nitric oxide synthase inhibitors and their use to reverse hypotension associated with cancer immunotherapy.
Author
Griffith OW; Kilbourn RG
Address
Department of Biochemistry, Medical College of Wisconsin, Milwaukee 53226, USA.
Source
Adv Enzyme Regul, 1997, 37:, 171-94
Abstract
It is now just 10 years since it was first appreciated that NO is endogenously synthesized in mammals. In this period, two constitutive and one inducible isoform of NOS have been isolated, sequenced, and characterized with respect to their protein chemistry and catalytic mechanism. A wide variety of NOS inhibitors, most targeted to the arginine binding site in the oxygenase domain, have been synthesized and used to elucidate the physiological and pathophysiological roles of NO. It is now clear that NO is involved in signal transduction (e.g., in neurotransmission and blood pressure homeostasis), and that these roles are mediated by low concentrations of NO synthesized by nNOS or eNOS. The NO receptor is the heme cofactor of soluble isoform of guanylyl cyclase. Higher amounts of NO, typically but not always synthesized by iNOS, are often cytotoxic. At a minimum, high concentrations of NO derange the signal transduction pathways normally served by nNOS or eNOS. In addition, NO or its nitrosative products (RSNO, N2O3, or ONOO-) inhibit or damage cellular constituents, interfering with DNA synthesis, energy metabolism, and the structural integrity of the cell. Such cytotoxicity can be beneficial to the host if pathogens or tumor cells are destroyed, but is detrimental to the host if it results in inappropriate inflammation, hypotension, or immunosuppression. Therapeutic utility of NOS inhibitors has been demonstrated in sepsis and cytokine-induced hypotension; additional applications are being identified in a treatment of inflammatory and autoimmune disorders.
Language of Publication
English
Unique Identifier
98020944

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MeSH Heading (Major)
Drug Design|*; Enzyme Inhibitors|CH/PD/*TU; Hypotension|*DT/ET; Immunotherapy|*AE; Interleukin-2|PD/*TU; Neoplasms|ME/*TH; Nitric-Oxide Synthase|*AI/ME
MeSH Heading
omega-N-Methylarginine|PD; Animal; Arginine|AA/ME/PD; Blood Pressure|DE/PH; Dogs; Human; Nitric Oxide|ME

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0065-2571
Country of Publication
ENGLAND


Record 17 from database: MEDLINE
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Title
Recent advances: parenteral nutrition support.
Author
Mattox TW; Bertch KE; Mirtallo JM; Strausberg KM; Cuddy PG
Address
H. Lee Moffitt Cancer Center and Research Institute, Colleges of Pharmacy, University of Florida, Tampa, USA.
Source
Ann Pharmacother, 1995 Feb, 29:2, 174-80
Abstract
Even though there is an abundance of research related to the clinical and physiologic effects of parenteral nutrition and specific nutritional substrates, few new products have been released for clinical use. This review illustrates some of the directions being taken in the future development of parenteral nutrition products and some new perspectives related to the current effects (or lack of effects) of TPN. When considering the individual effects of specific nutrient substrates (arginine, glutamine, LCTs, MCTs, SCFAs) as reviewed here, it becomes apparent that the infusion of parenteral nutrition has the potential to produce a variety of metabolic responses that could be both beneficial and harmful. These effects depend on the type and quantity of substance infused as well as the disease and clinical condition of the patient. This also is true for those substances (GH, IGF-1) being evaluated to direct the effects of TPN infusions in a manner that improves protein accretion and supports the immunologic response of the body. At best, these investigations are producing a great amount of new and more specific information about the metabolic response to illness and the effects of TPN and individual substrate on that response.
Language of Publication
English
Unique Identifier
95276336

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MeSH Heading (Major)
Parenteral Nutrition|*TD
MeSH Heading
Arginine|AD/ME/PD; Fat Emulsions, Intravenous|ME/PD; Glutamine|AD/ME/PD; Growth Substances|ME/PD; Human; Insulin-Like Growth Factor I|ME/PD; Nursing Research; Parenteral Nutrition, Total|TD

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
1060-0280
Country of Publication
UNITED STATES


Record 18 from database: MEDLINE
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Title
Use of nitric oxide synthase inhibitors as a novel treatment for septic shock.
Author
Wolfe TA; Dasta JF
Address
College of Pharmacy, Ohio State University, Columbus 43210.
Source
Ann Pharmacother, 1995 Jan, 29:1, 36-46
Abstract
OBJECTIVE: To review the current literature regarding the role of nitric oxide (NO) in the pathogenesis of septic shock and to describe the potential role of NO synthase (NOS) inhibitors in the treatment of septic shock. DATA SOURCES: A MEDLINE, Cancerlit, Biosis, Scisearch, CBAC, bibliography, and current journal search of applicable articles on the involvement of NO in mediating septic shock and the use of NOS inhibitors in septic shock was conducted. Articles that were searched included animal and human studies from January 1990 to August 1994. STUDY SELECTION: Because of the preliminary nature of the research involving NOS inhibitors in septic shock, all available studies were evaluated. DATA SYNTHESIS: NO appears to have a role in the mediation of the hemodynamic instability associated with septic shock. Cytokines and endotoxin stimulate synthesis of the inducible NOS, which produces large amounts of NO over an extended period of time. NO may be the key mediator in the pathogenesis of septic shock. Derivatives of the precursor to NO, L-arginine, have been used to investigate the role of NO in septic shock and as possible therapeutic agents. Comparison of study results among animal studies shows much variability. This variability may be attributable to differences in dosing regimens and models of septic shock. Data obtained from human studies are more consistent, but are limited to a few case series. Results indicate that NOS inhibitors increase blood pressure and systemic vascular resistance and decrease cardiac output. The effects of NOS inhibitors on morbidity and mortality have not been assessed because of the lack of an appropriate sample size. CONCLUSIONS: NO appears to play a role in septic shock; however, the use of NOS inhibitors to treat septic shock requires further studies to determine an appropriate dosing regimen and to determine the effects of these agents on morbidity and mortality.
Language of Publication
English
Unique Identifier
95226751

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MeSH Heading (Major)
Amino Acid Oxidoreductases|*AI/TU; Nitric Oxide|*AE/AI/ME; Shock, Septic|CI/*DT/PP
MeSH Heading
Animal; Arginine|AA/PD/TU; Clinical Trials; Comparative Study; Human

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
1060-0280
Country of Publication
UNITED STATES


Record 19 from database: MEDLINE
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Title
Characterization of mammalian ADP-ribosylation cycles.
Author
Okazaki IJ; Zolkiewska A; Takada T; Moss J
Address
Pulmonary-Critical Care Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Source
Biochimie, 1995, 77:5, 319-25
Abstract
NAD:arginine ADP-ribosyltransferases catalyze the transfer of the ADP-ribose moiety from NAD to an arginine in an acceptor protein, whereas ADP-ribosylarginine hydrolases remove ADP-ribose, regenerating free arginine and completing an ADP-ribosylation cycle. A family of four mono-ADP-ribosyltransferases was isolated and characterized from turkey erythrocytes. Transferases from rabbit and human skeletal muscle were cloned. The muscle transferases are glycosylphosphatidylinositol-anchored proteins and highly conserved across mammalian species. The rat T cell alloantigen RT6.2 has significant amino acid sequence identity to the muscle ADP-ribosyltransferase. Mammalian cells transformed with the RT6.2 coding region cDNA expressed NAD glycohydrolase activity. Sequences of RT6.2, rabbit muscle transferase and several of the bacterial toxin ADP-ribosyltransferases contain regions of amino acid similarity which, in the bacterial toxin ADP-ribosyltransferases, form the NAD-binding and active-site domains. ADP-ribosylarginine hydrolase, initially purified from turkey erythrocytes, was cloned from rat, mouse, and human brain. Deduced amino acid sequences of the rat and mouse hydrolases were 94% identical with five conserved cysteines whereas the human hydrolase sequence was 83% identical to that of the rat, with four conserved cysteines. It is unclear how an intracellular hydrolase acts in concert with a surface ADP-ribosyltransferase.
Language of Publication
English
Unique Identifier
96051172

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MeSH Heading (Major)
Adenosine Diphosphate Ribose|*ME; NAD|*ME; NAD(P)(+)-Arginine ADP-Ribosyltransferase|BL/*ME
MeSH Heading
Amino Acid Sequence; Animal; Arginine|ME; Bacterial Toxins|ME; Binding Sites; Comparative Study; Conserved Sequence; Erythrocytes|EN; Glycoside Hydrolases|ME; Human; Mammals; Mice; Molecular Sequence Data; NAD+ Nucleosidase|ME; Rabbits; Rats; Sequence Homology, Amino Acid; Turkeys

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0300-9084
Country of Publication
FRANCE


Record 20 from database: MEDLINE
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Title
Disorders of prolactin and growth hormone secretion.
Author
Ho KY; Evans WS; Thorner MO
Address
Source
Clin Endocrinol Metab, 1985 Feb, 14:1, 1-32
Abstract
A large range of tests is now available to help us understand, diagnose and manage GH-related growth disorders. The traditional provocative tests of GH secretion will identify short children with severe GH deficiency. However, evidence is emerging that these pharmacological tests may not be sufficiently sensitive to identify some subjects with GH deficiency arising from neurosecretory disturbance of GH release. There is a need for a simple sensitive test that will detect subtle GH secretion of this type. hGRF administration is a reliable test of GH reserve and, when used in combination with conventional tests, may help to identify GH-deficient children with hypothalamic GRF deficiency. Whether the GH responses following GRF administration reflects physiological GH secretory activity needs to be established. The diagnosis of acromegaly is made on clinical grounds. The abnormal GH responses to glucose and TRH support the diagnosis, but by themselves should not be considered to be diagnostic of acromegaly. An elevated Sm C level also helps to establish the diagnosis, although Sm C concentrations may be elevated to the same degree in pregnancy and during puberty. The use of Sm C to monitor disease activity remains to be established. Circulating GRF levels should be measured in patients with acromegaly so that ectopic production of GRF can be identified.
Language of Publication
English
Unique Identifier
85255561

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MeSH Heading (Major)
Prolactin|*SE; Somatotropin|DF/*SE
MeSH Heading
Acromegaly|ET; Arginine|DU; Clonidine|DU; Dwarfism|ET; Exertion; Female; Glucose Tolerance Test; Human; Hypothalamo-Hypophyseal System|PP; Hypothyroidism|CO; Kidney Failure, Chronic|CO; Lactation; Levodopa|DU; Male; Methyldopa|AE; Pituitary Neoplasms|SE; Pregnancy; Propranolol|DU; Protirelin|DU; Reserpine|AE; Sleep|PH; Somatomedins|DU; Somatotropin-Releasing Hormone|DU; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0300-595X
Country of Publication
ENGLAND
CAS Registry/EC Number
0 (Levodopa); 0 (Somatomedins); 24305-27-9 (Protirelin); 4205-90-7 (Clonidine); 50-55-5 (Reserpine); 525-66-6 (Propranolol); 555-30-6 (Methyldopa); 67763-96-6 (Insulin-Like Growth Factor I); 7004-12-8 (Arginine); 9002-62-4 (Prolactin); 9002-72-6 (Somatotropin); 9034-39-3 (Somatotropin-Releasing Hormone)


Record 21 from database: MEDLINE
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Title
Islet-cell abnormalities in non-insulin-dependent diabetes mellitus.
Author
Raskin P
Address
Source
Am J Med, 1985 Aug 23, 79:2B, 2-5
Abstract
Patients with non-insulin-dependent diabetes mellitus have enlarged islets of Langerhans, an increased number of insulin-secreting beta cells, and a "horseshoe-shaped" relationship between plasma insulin and glucose levels. To some extent, beta-cell dysfunction in patients with type II diabetes is reversible with appropriate hypoglycemic therapy. Defects in the glucagon-secreting alpha cells in patients with non-insulin-dependent diabetes mellitus include basal hyperglucagonemia, an exaggerated glucagon response to aminogenic stimuli, and hyposuppressibility of glucagon by hyperglycemia. Although peripheral resistance to insulin may play a role in type II diabetes, defects in islet-cell function clearly play a significant role as well.
Language of Publication
English
Unique Identifier
85304186

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MeSH Heading (Major)
Diabetes Mellitus, Non-Insulin-Dependent|PA/*PP/TH; Islets of Langerhans|PA/*PP
MeSH Heading
Alanine|DU; Arginine|DU; Blood Glucose|ME; Dietary Carbohydrates|PD; Dietary Proteins|PD; Glucagon|BL/SE; Glucose Tolerance Test; Human; Insulin|SE; Insulin Resistance

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0002-9343
Country of Publication
UNITED STATES
CAS Registry/EC Number
0 (Blood Glucose); 0 (Dietary Proteins); 11061-68-0 (Insulin); 6898-94-8 (Alanine); 7004-12-8 (Arginine); 9007-92-5 (Glucagon)


Record 22 from database: MEDLINE
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Title
Selective pharmacological inhibition of distinct nitric oxide synthase isoforms.
Author
Southan GJ; Szabó C
Address
Division of Critical Care, Children's Hospital Medical Center, Cincinnati, OH 45229, USA.
Source
Biochem Pharmacol, 1996 Feb, 51:4, 383-94
Abstract
Nitric oxide (NO) is produced in physiological and pathophysiological conditions by three distinct isoforms of NO synthase (NOS): endothelial NOS (ecNOS), inducible NOS (iNOS), and brain NOS (bNOS). Selective inhibition of iNOS may be beneficial in various forms of shock and inflammation, whereas inhibition of bNOS may protect against neuroinjury. This article surveys the enzymatic mechanism of NO production, lists the strategies and pharmacological tools for selective inhibition of distinct NOS isoforms, and considers the side-effects of the various approaches. Selective inhibition of NOS isoforms is achieved by: (a) targeting the differential co-factor (calmodulin or tetrahydrobiopterin) requirement of various NOS isoforms, and NOS; (b) targeting the differential substrate requirements of cells expressing various isoforms of NOS (L-arginine uptake blockers or arginase); (c) the use of pharmacological agents that are selectively taken up by cells expressing various isoforms of NOS (7-nitroindazole); or (d) developing pharmacological NOS inhibitors with isoform specificity. The amino acid-based NOS inhibitor, NG-nitro-L-arginine, shows a preference for ecNOS and bNOS over iNOS, whereas L-N6-(1-iminoethyl)lysine is selective for iNOS over bNOS. Certain non-amino acid-based small molecules, such as aminoguanidine and certain S-alkylated isothioureas, also express selectivity towards iNOS and have anti-inflammatory and anti-shock properties. 7-nitroindazole, a bNOS-selective inhibitor, protects in central nervous system injury. Clearly, there are a number of distinct approaches that are worthy of further research efforts in order to achieve even more selective targeting of various NOS isoforms
Language of Publication
English
Unique Identifier
96191294

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MeSH Heading (Major)
Enzyme Inhibitors|*PD; Isoenzymes|*AI/BI; Nitric-Oxide Synthase|*AI/BI
MeSH Heading
Animal; Arginase|ME; Arginine|AA/ME/PD; Brain|EN; Endothelium, Vascular|EN; Human; Indazoles|PD; Nitric Oxide|BI

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
ISSN
0006-2952
Country of Publication
ENGLAND


Record 23 from database: MEDLINE
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Title
Vascular biology: relevance of nitric oxide in vascular and nonvascular tissue with normal and decreased renal function.
Author
Blantz RC
Address
Department of Medicine, University of California, San Diego School of Medicine 92161.
Source
Blood Purif, 1994, 12:1, 30-5
Abstract
Nitric oxide has been recognized as an important paracrine or autocrine system during the past decade. The generalized importance of this rather simple molecule has been demonstrated in of a variety of neural, epithelial, vascular and immune systems. The degree to which alterations in nitric oxide metabolism contribute to the physiologic and pathophysiologic status of patients with end-stage renal disease remains to be fully defined in both experimental animals and in humans afflicted with renal disease.
Language of Publication
English
Unique Identifier
95077808

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MeSH Heading (Major)
Endothelium, Vascular|*PH/PP; Kidney Diseases|*PP; Nitric Oxide|*PH
MeSH Heading
Amino Acid Oxidoreductases|ME; Arginine|AA/PD/TU; Enzyme Induction; Hemodynamics|DE; Human; Hypotension|PC/PP; Inflammation|PP; Shock, Septic|PP; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0253-5068
Country of Publication
SWITZERLAND


Record 24 from database: MEDLINE
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Title
Recent progress in pharmacological therapy of male subfertility--a review.
Author
Schill WB
Address
Source
Andrologia, 1979 Mar-Apr, 11:2, 77-107
Abstract
A review of pharmacological therapy in male infertility shows that apart from specific therapy with gonadotropins in hypogonadotropic hypogonadism, treatment in normogonadotropic idiopathic oligozoospermia and asthenozoospermia is still empirical and often unsuccessful. Modern therapy is based on three pharmacological groups of compounds: gonadotropins, androgens and kininogenases, the latter releasing pharmacologic active kinin peptides from kininogen. In addition, antiestrogens and gonadotropin-releasing hormones seem to be promising agents for the near future. The use of antibiotics is of great importance in the therapy of male genital tract infections which often to a reduced fertility. Several other drugs (amino acids, psychopharmaceuticals, spasmolytic agents, trijodothyronine, glucocorticoids, vitamins) seem to be suitable in individuals cases, but in greater group of patients these agents do not improve fertility. Using the mentioned hormonal and nonhormonal pharmacological agents considerable progress can be demonstrated in the therapy of male infertility. However, before initiating any therapy it is important to exclude patients whose cause of infertility is untreatable or those who require surgery. Finally, it is hoped that additional progress in treatment of male infertility will soon be made possible by further improvement of fundamental research in andrology. Especially important is the development of better criteria for selection of patients for any form of therapy in order to make more specific and less empirical approaches for treatment of male infertility available.
Language of Publication
English
Unique Identifier
79185657

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MeSH Heading (Major)
Androgens, Synthetic|*TU; Estrogen Antagonists|*TU; Fertility Agents, Male|*TU; Gonadotropins|*TU; Infertility, Male|*DT
MeSH Heading
Anti-Infective Agents|TU; Arginine|TU; Clomiphene|TU; Drug Therapy, Combination; Glucocorticoids|TU; Gonadotropins, Chorionic|TU; Human; Immunosuppressive Agents|TU; Kallikrein|TU; Male; Menotropins|TU; Parasympatholytics|TU; Pituitary Hormone-Releasing Hormones|TU; Psychotropic Drugs|TU; Tamoxifen|TU; Testosterone|TU; Triiodothyronine|TU; Vitamins|TU

Publication Type
JOURNAL ARTICLE; REVIEW
ISSN
0303-4569
Country of Publication
GERMANY, WEST


Record 25 from database: MEDLINE
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Title
Endothelial dysfunction in chronic heart failure. Experimental and clinical studies.
Author
Drexler H; Hayoz D; Münzel T; Just H; Zelis R; Brunner HR
Address
Medizinische Klinik III, University of Freiburg, Fed. Rep. of Germany.
Source
Arzneimittelforschung, 1994 Mar, 44:3A, 455-8
Abstract
The endothelium plays an important role in the control of human vascular tone by releasing endothelium-derived nitric oxide. Therefore, endothelial dysfunction could be involved in the increased peripheral vasoconstriction of patients with chronic congestive heart failure (CHF). To investigate endothelial function in humans in vivo, agents such as acetylcholine are used to stimulate the release of endothelium-derived nitric oxide (EDRF). Conversely, N-mono-methyl-L-arginine (L-NMMA), a specific inhibitor of nitric oxide synthesis from L-arginine decreases forearm blood flow by inhibiting the basal release of nitric oxide. Consistent with experimental studies, the blood flow response to acetylcholine is blunted in patients with chronic heart failure as compared to healthy age-matched volunteers. In contrast, the decrease in blood flow induced by L-NMMA appears to be exaggerated in CHF. The blood flow response to nitroglycerin or sodium nitroprusside, endothelium-independent vasodilators, is usually preserved in patients with chronic, non-edematous heart failure, indicating a normal response of the vascular smooth muscle of resistance vessels to exogenous nitric oxide. In contrast, the dilator response of the radial artery diameter to nitroglycerin and flow-dependent dilation are impaired in patients with chronic heart failure, indicating that the abnormal flow-mediated relaxation of large arteries may be due to both endothelial and vascular smooth muscle alterations. Thus, impaired endothelium-dependent dilation of peripheral resistance vessels emerges in chronic heart failure, suggesting a reduced release of nitric oxide upon stimulation. Thus, endothelial dysfunction may be involved in the impaired vasodilator capacity in the peripheral circulation, e.g. during exercise.(ABSTRACT TRUNCATED AT 250 WORDS)
Language of Publication
English
Unique Identifier
94242153

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MeSH Heading (Major)
Endothelium, Vascular|DE/*PP; Heart Failure, Congestive|*PP
MeSH Heading
Arginine|AA/PD; Chronic Disease; Human; In Vitro; Nitric Oxide|AI

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0004-4172
Country of Publication
GERMANY


Record 26 from database: MEDLINE
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Title
Beneficial circulatory effect of L-arginine.
Author
Nakaki T; Kato R
Address
Department of Pharmacology, School of Medicine, Keio University, Tokyo, Japan.
Source
Jpn J Pharmacol, 1994 Oct, 66:2, 167-71
Abstract
L-Arginine is an essential amino acid for infants and growing children. This amino acid is a substrate for at least five enzymes identified in mammals, including arginase, arginine-glycine transaminase, kyotorphine synthase, nitric oxide synthase (NOS) and arginine decarboxylase. L-Arginine exerts antihypertensive and antiproliferative effects on vascular smooth muscles. NOS and arginine decarboxylase appear to be important for the effect of L-arginine on the circulatory system, since each produces nitric oxide (NO), a potent vasodilator, and agmatine, an endogenous noncatecholamine ligand for central alpha-2 adrenoceptors, from L-arginine. Several issues must be clarified before the mechanisms by which L-arginine exerts its effects on the circulatory system can be fully understood.
Language of Publication
English
Unique Identifier
95174208

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MeSH Heading (Major)
Arginine|ME/PD/*TU; Hemodynamics|*DE; Hypertension|*DT/PP; Muscle, Smooth, Vascular|CY/*DE
MeSH Heading
Amino Acid Oxidoreductases|ME; Animal; Atherosclerosis|BL/DT; Carboxy-Lyases|ME; Cell Division|DE; Child; Enzymes|ME; Human; Infant; Regional Blood Flow|DE; Substrate Specificity; Vasodilation|DE

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0021-5198
Country of Publication
JAPAN


Record 27 from database: MEDLINE
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Title
Nitric oxide in essential and renal hypertension [editorial]
Author
MacAllister R; Vallance P
Address
Department of Pharmacology and Clinical Pharmacology, St. George's Hospital Medical School, London, United Kingdom.
Source
J Am Soc Nephrol, 1994 Oct, 5:4, 1057-65
Abstract
L-Arginine-derived nitric oxide (NO) maintains the systemic and renal vasculature in a state of active vasodilation. Inhibition of NO synthesis increases renal vascular tone, reducing RBF and GFR. Similar effects reproduced in other vascular beds result in systemic hypertension. In addition, NO modulates natriuresis by a direct effect on renal tubular function. Abnormalities of the L-arginine:NO pathway occur in experimental hypertension and renal disease and could contribute to alterations in vascular tone; similar abnormalities are seen in essential hypertension in humans. In dialysis-dependent renal failure, the accumulation of endogenous compounds that inhibit NO synthase could exacerbate renal hypertension by inhibiting vascular and renal tubular NO synthesis and might provoke atherogenesis.
Language of Publication
English
Unique Identifier
95151996

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MeSH Heading (Major)
Hypertension|*ET/PP; Hypertension, Renal|*ET/PP; Nitric Oxide|*PH
MeSH Heading
Amino Acid Oxidoreductases|AI; Animal; Arginine|AA/PH; Human; Kidney Tubules|PP; Renal Circulation|PH

Publication Type
EDITORIAL; REVIEW; REVIEW, ACADEMIC
ISSN
1046-6673
Country of Publication
UNITED STATES


Record 28 from database: MEDLINE
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Title
Protein metabolism in the cancer patient.
Author
Garlick PJ; McNurlan MA
Address
Department of Surgery, State University of New York, Health Sciences Center, Stony Brook 11794-8191, USA.
Source
Biochimie, 1994, 76:8, 713-7
Abstract
The 'flooding' method has been widely used for measuring protein synthesis in animal tissues in vivo and in vitro, employing radioactively labelled amino acids, because it minimises errors in determining the specific radioactivity of the direct precursor of protein synthesis. This approach has now been modified for measuring protein synthesis rates in tumours and healthy tissues of humans by injection of the stable isotopic labels, [1(-13)C]leucine or [2H5]phenylalanine, followed by tissue sampling during surgery. Based on the observation that rates of protein synthesis correlate with changes in the expression of cell proliferation markers, we have suggested that changes in protein synthesis in tumours can be used as indices of changes in tumour growth. Measurements in colorectal cancer patients have shown that protein synthesis is stimulated 80% by feeding, suggesting that the tumour is not a pure parasite, but responds to exogenous nutrients. Moreover, when the composition of the amino acids given to the patient was changed from a balanced mixture to one supplemented with branched chain amino acids, the response of the tumour to feeding was significantly diminished, suggesting that tumour growth might be modulated by diet composition. Dietary supplements of arginine have been shown previously to inhibit tumour growth in animals, probably by activating the immune system. However, in breast cancer patients arginine stimulated tumour protein synthesis, suggesting that arginine might have separate stimulatory effects on the tumour and the immune system, the outcome depending on which effect predominates.
Language of Publication
English
Unique Identifier
95201034

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MeSH Heading (Major)
Neoplasms|DH/*ME; Proteins|*BI
MeSH Heading
Amino Acids, Branched-Chain|AD/ME; Animal; Arginine|AD/ME; Carbon Isotopes; Deuterium; Fasting; Human

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0300-9084
Country of Publication
FRANCE


Record 29 from database: MEDLINE
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Title
Arginine: new and exciting developments for an "old" amino acid.
Author
Beaumier L; Castillo L; Yu YM; Ajami AM; Young VR
Address
Laboratory of Human Nutrition, School of Science, Massachusetts Institute of Technology, Cambridge 02139, USA.
Source
Biomed Environ Sci, 1996 Sep, 9:2-3, 296-315
Abstract
Arginine (2-amino-5-guanidino pentanoic acid) was shown in 1895 by Hedin to be present in the proteins of horn. Metabolic nitrogen balance studies, conducted in 1957 by Rose in human adults and in 1959 by Snyderman and coworkers in young infants revealed that a dietary source of this amino acid was not an obligatory requirement for growth and maintenance of nitrogen homeostasis in healthy individuals. Hence, it was initially classified as a non-essential (dispensable) amino acid and, perhaps, for reasons of this classification arginine did not receive the earlier attention it now deserves, in relation to an understanding of the nutritional biochemistry and physiology of its metabolism in humans subjects. However, there is currently a considerable interest in the cellular and tissue functions, as well as clinical, therapeutic significance, of arginine. In this paper we review the multiple functions of arginine, including its role in the L-arginine-nitric oxide pathway, cellular regeneration, immune function, protein synthesis and protein breakdown. We then consider some in vivo aspects of the physiology of arginine metabolism, which varies greatly among eukaryotes, with particular reference to humans. Against this background, studies of arginine in the nutrition of humans under various pathophysiological conditions are reviewed briefly. Finally, a new, updated concept for the metabolic basis for the "conditional essentiality" of arginine is proposed.
Language of Publication
English
Unique Identifier
97041055

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MeSH Heading (Major)
Arginine|ME/PD/*PH
MeSH Heading
Homeostasis; Human; Immune System|PH; Nitric Oxide|PH; Nutritional Requirements; Proteins|BI/ME; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0895-3988
Country of Publication
UNITED STATES


Record 30 from database: MEDLINE
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Title
Endothelial function in hypertension.
Author
Mattei P; Virdis A; Ghiadoni L; Taddei S; Salvetti A
Address
Cattedra di Medicina Interna, Clinica Medica I, University of Pisa, Italy.
Source
J Nephrol, 1997 Jul, 10:4, 192-7
Abstract
Endothelial dysfunction has been documented both in the forearm and coronary beds of essential hypertensive patients. Impairment in the tonic release of nitric oxide (NO) is secondary to hypertension, while the alteration in agonist-induced endothelium-dependent vasodilation seems to be a primary defect caused both by an alteration of the L-arginine-NO pathway and the production of cyclooxygenase-dependent EDCFs, such as prostanoids or superoxide anions. These latter substances curtail endothelium-dependent vasodilation mainly by inactivating NO production. Although experimental data clearly indicate that the L-arginine-NO pathway participates in the regulation of renal hemodynamics and renal excretory function under basal and stimulated conditions, data in humans are scanty and confounded by methodological approaches. A posteriori interpretation of data obtained with intrarenal infusion of acetylcholine in kidney donors suggests that endothelium dependent vasodilation in the kidney is impaired by aging, a phenomenon well documented in the forearm and coronary circulation. Systemic infusion of L-arginine induced renal vasodilation and natriuresis in normotensive subjects, an effect which seems to be mediated mainly by intrarenal NO production. Moreover the few available data suggest that both renal vasodilation and renal production of NO in response to L-arginine are blunted in patients with essential hypertension and that superoxide anions, may be, at least partially, responsible for this alteration of the L-arginine-NO pathway. In conclusion, endothelial dysfunction has been well documented in the forearm and coronary circulation of patients with essential hypertension. Available data suggest that endothelial, dysfunction is also detectable in the kidney and that a common mechanism, probably superoxide anions, can account for this abnormality.
Language of Publication
English
Unique Identifier
98017366

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MeSH Heading (Major)
Endothelium, Vascular|*PP; Hypertension|*PP; Kidney|BS/DE/*PP; Superoxides|*ME
MeSH Heading
Arginine|PD/PH; Human; Nitric Oxide|BI; Vasodilation

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
1120-3625
Country of Publication
ITALY


Record 31 from database: MEDLINE
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Title
Role of arginine in health and in renal disease [editorial]
Author
Reyes AA; Karl IE; Klahr S
Address
Source
Am J Physiol, 1994 Sep, 267:3 Pt 2, F331-46
Abstract
In addition to participating in protein synthesis in cells and tissues, L-arginine is essential for the synthesis of urea, creatine, creatinine, nitric oxide, and agmatine and influences hormonal release and the synthesis of pyrimidine bases. This places L-arginine, its precursors and its metabolites at the center of the interaction of different metabolic pathways and interorgan communication. Thus L-arginine participates in changing the internal environment in different but simultaneous ways, ranging from disposal of protein metabolic waste, muscle metabolism, vascular regulation, immune system function, and neurotransmission, to RNA synthesis and hormone-mediated regulation of the internal milieu. In normal rats, inhibition of the nitric oxide pathway results in systemic hypertension and decreased glomerular filtration rate and effective renal plasma flow. If the inhibition of this pathway is sustained, then glomerulosclerosis and death from uremia follow. Dietary intervention with L-arginine has resulted in amelioration of a number of experimental kidney diseases, such as those caused by subtotal nephrectomy, diabetic, nephropathy, cyclosporin A administration, salt-sensitive hypertension, ureteral obstruction, puromycin amino-nucleoside nephrosis, kidney hypertrophy due to high-protein feeding, and glomerular thrombosis due to administration of lipopolysaccharide. The present review addresses the current evidence for the beneficial effects of dietary intervention with L-arginine in a number of experimental renal diseases and describes the basis for the concept of L-arginine deficiency (absolute or relative) in certain settings in which supplementation of the diet with this amino acid may be beneficial.
Language of Publication
English
Unique Identifier
94379146

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MeSH Heading (Major)
Arginine|ME/PD/*PH; Health|*; Kidney Diseases|*PP
MeSH Heading
Animal; Animal Nutrition; Blood Pressure|DE; Growth; Human; Kidney|DE; Reference Values; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type
EDITORIAL; REVIEW; REVIEW, TUTORIAL
ISSN
0002-9513
Country of Publication
UNITED STATES


Record 32 from database: MEDLINE
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Title
ADP-ribosylarginine hydrolases and ADP-ribosyltransferases. Partners in ADP-ribosylation cycles.
Author
Moss J; Zolkiewska A; Okazaki I
Address
Pulmonary-Critical Care Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
Source
Adv Exp Med Biol, 1997, 419:, 25-33
Abstract
Mono-ADP-ribosylation is a reversible modification of arginine residues in proteins, with NAD:arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolases constituting opposing arms of a putative ADP-ribosylation cycle. The enzymatic components of an ADP-ribosylation cycle have been identified in both prokaryotic and eukaryotic systems. The regulatory significance of the cycle has been best documented in prokaryotes. As shown by Ludden and coworkers, ADP-ribosylation controls the activity of dinitrogenase reductase in the phototropic bacterium Rhodospirillum rubrum. ADP-ribosylation of other amino acids, such as cysteine, has also been demonstrated, lending credence to the hypothesis that this modification is heterogeneous. In eukaryotes, the functional relationship between ADP-ribosyltransferases and ADP-ribosylarginine hydrolases is less well documented. The transferase-catalyzed reaction results in sterospecific formation of alpha-ADP-ribosylarginine from beta-NAD; ADP-ribosylarginine hydrolases specifically cleave the alpha-anomer, leading to release of ADP-ribose and regeneration of the free guanidino group of arginine. The two reactions can thus be coupled in vitro. Coupling in vivo is dependent on cellular localization. The deduced amino acid sequences of ADP-ribosyltransferases from avian and mammalian tissues have common consensus sequences involved in catalytic activity but, in some instances, enzyme-specific cellular localization signals. The presence of amino- and carboxy-terminal signal sequences is consistent with the glycosylphosphatidylinositol(GPI)-anchoring to the cell surface. The muscle and lymphocyte transferases ADP-ribosylate integrins. Some transferases lack the carboxy- terminal signal sequence needed for GPI-anchoring. Most ADP-ribosylarginine hydrolase activity is cytosolic, although perhaps some is located at the cell surface. Deduced amino acid sequences of hydrolases from a number of mammalian species are consistent with their cytoplasmic localization. Katada and coworkers have determined, however, that auto-ADP-ribosylated RT6, a GPI-linked protein, is metabolized by a hydrolase-like activity, consistent with the existence of an ADP-ribosylation cycle. ADP-ribosyl RT6 may be internalized, thereby coming in contact with the cytosolic hydrolase; alternatively, a novel form of the hydrolase may be located at the surface. The mechanism of coupling of ADP-ribosyltransferases and hydrolases in eukaryotic ADP-ribosylation cycles has yet to be clarified.
Language of Publication
English
Unique Identifier
97336886

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MeSH Heading (Major)
Adenosine Diphosphate Ribose|*ME; Glycoside Hydrolases|*ME; NAD(P)(+)-Arginine ADP-Ribosyltransferase|CH/GE/*ME
MeSH Heading
Amino Acids; Animal; Cysteine|ME; Human; Mammals; Pentosyltransferases|ME; Turkeys

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0065-2598
Country of Publication
UNITED STATES


Record 33 from database: MEDLINE
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Title
Alternative pathway therapy for urea cycle disorders.
Author
Feillet F; Leonard JV
Address
Biochemistry, Endocrine and Metabolic Unit, Institute of Child Health, London, UK.
Source
J Inherit Metab Dis, 1998, 21 Suppl 1:, 101-11
Abstract
In man the major pathway for the disposal of waste nitrogen is the urea cycle; in inborn errors of this pathway, nitrogen flux is reduced. As a result there is accumulation of ammonia and glutamine with disordered metabolism of other amino acids. Nitrogen homeostasis can be restored in these patients with a low-protein diet combined with compounds that create alternative pathways for nitrogen excretion. The introduction of these compounds has been a major advance in the management of these inborn errors and as a result the outcome, particularly for those treated early, has improved.
Language of Publication
English
Unique Identifier
98350965

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MeSH Heading (Major)
Amino Acid Metabolism, Inborn Errors|DH/*DT/ME; Urea|*ME
MeSH Heading
Animal; Arginine|ME/TU; Benzoates|AE/TU; Child; Citrulline|ME/TU; Combined Modality Therapy; Female; Human; Male; Nitrogen|ME; Phenylacetates|TU; Phenylbutyrates|AE/TU

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0141-8955
Country of Publication
NETHERLANDS
CAS Registry/EC Number
0 (Benzoates); 0 (Phenylacetates); 0 (Phenylbutyrates); 103-82-2 (phenylacetic acid); 372-75-8 (Citrulline); 57-13-6 (Urea); 65-85-0 (benzoic acid); 7004-12-8 (Arginine); 7727-37-9 (Nitrogen)


Record 34 from database: MEDLINE
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Title
Invited opinion: role of nitric oxide in hemorrhagic, traumatic, and anaphylactic shock and thermal injury.
Author
Szabó C; Thiemermann C
Address
William Harvey Research Institute, St. Bartholomew's Hospital Medical Center, London, United Kingdom.
Source
Shock, 1994 Aug, 2:2, 145-55
Abstract
The free radical nitric oxide (NO) is synthesized from the guanidino group of L-arginine by a family of enzymes termed NO synthase (NOS). Hemorrhagic shock leads to an inhibition of NO production by the calcium-dependent, endothelial NOS (ecNOS), which may lead to maldistribution of blood flow leading to, e.g., coronary, renal, and cerebral ischemia and may enhance the adhesion of neutrophil granulocytes and platelets to the endothelial surface. Prolonged periods of hemorrhagic shock are associated with the induction of a calcium-independent isoform of NOS in a variety of organs and in the vascular smooth muscle. The formation of large quantities of NO by inducible isoform of NOS (iNOS) contributes to the delayed vascular decompensation and to the hyporeactivity of the vasculature to vasoconstrictor agents. An impairment of NO formation by the ecNOS has been demonstrated in various models of traumatic shock, whereas there is good experimental evidence supporting the hypothesis that an enhanced formation of NO contributes to the pathophysiology of experimental thermal injury and anaphylactic shock. We speculate that a pharmacological modulation of NO biosynthesis which either enhances NO concentration in the vicinity of endothelium (i.e., NO donors) or inhibits NO overproduction following iNOS expression (i.e., iNOS-selective NOS inhibitors) may become novel therapies to improve the outcome of patients with circulatory shock of various etiologies.
Language of Publication
English
Unique Identifier
95245825

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MeSH Heading (Major)
Amino Acid Oxidoreductases|*ME; Anaphylaxis|*PP; Endothelium, Vascular|PH/*PP; Nitric Oxide|AI/*PH; Shock|*PP; Shock, Hemorrhagic|*PP; Wounds and Injuries|*PP
MeSH Heading
Animal; Arginine|AA/PD; Burns|PP; Human; Liver Circulation|DE/PH; Models, Biological

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
ISSN
1073-2322
Country of Publication
UNITED STATES


Record 35 from database: MEDLINE
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Title
Mono(ADP-ribosyl)transferases and related enzymes in animal tissues. Emerging gene families.
Author
Koch Nolte F; Haag F
Address
Department of Immunology, University Hospital, Hamburg, Germany.
Source
Adv Exp Med Biol, 1997, 419:, 1-13
Abstract
Mono-ADP-ribosylation, like phosphorylation, is an enzyme-catalyzed, reversible post-translational modification that modulates protein function. It was originally discovered as the pathogenic principle of diphtheria-, cholera-, and other potent bacterial toxins. By analogy, corresponding enyzmes were postulated to exist in animal tissues, and mounting biochemical evidence indicates that such enzymes, indeed, play important regulatory roles in cellular functions. The molecular cloning of the first mammalian mono(ADP-ribosyl)transferase from rabbit skeletal muscle, the finding of its homology to a well-studied T-cell marker, RT6, and the molecular cloning of additional gene family members from mammals and birds is providing fresh impetus to research in this field. Intriguingly, these vertebrate enzymes are predicted to be secretory or membrane proteins. They are expressed in lymphatic tissues, muscle, testis, bone marrow, and erythroblasts. Here we review the relationship between this novel family of eucaryotic mono(ADP-ribosyl)transferases (mADPRTs), ADP-ribosylating bacterial toxins, the poly(ADP-ribose)polymerase (PARP), the ADP-ribosyl cyclases, and the ADP-ribosylprotein hydrolase (ARH) in terms of their structure, enzymatic properties and possible biological functions.
Language of Publication
English
Unique Identifier
97336884

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MeSH Heading (Major)
NAD(P)(+)-Arginine ADP-Ribosyltransferase|CH/GE/*ME
MeSH Heading
Adenosine Diphosphate Ribose|ME; Animal; Antigens, Differentiation|ME; Autoimmune Diseases|EN/GE; Bacterial Toxins|ME; Catalysis; Glycoside Hydrolases|ME; Human; Lyases|ME; Multigene Family; Nucleosidases|ME; NAD+ ADP-Ribosyltransferase|ME

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0065-2598
Country of Publication
UNITED STATES


Record 36 from database: MEDLINE
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Title
Apparent affinity and potency of BIBP3226, a non-peptide neuropeptide Y receptor antagonist, on purported neuropeptide Y Y1, Y2 and Y3 receptors.
Author
Jacques D; Cadieux A; Dumont Y; Quirion R
Address
Douglas Hospital Research Centre, Faculty of Medicine, McGill University, Verdun, QuÆebec, Canada.
Source
Eur J Pharmacol, 1995 May, 278:1, R3-5
Abstract
The newly developed, purported non-peptide neuropeptide Y Y1 receptor antagonist BIBP3226 was evaluated for its potential effect on the recently characterized Y3 receptor subtype and for its apparent affinity in rat and human brain membrane binding assays using highly selective neuropeptide Y Y1 and Y2 radioligands. BIBP3226 potently blocked (pA2 = 7.36) the contractile effect of neuropeptide Y in the rabbit saphenous vein, a Y1 receptor bioassay and demonstrated nM affinity for Y1/[125I][Leu31,Pro34]peptide YY binding sites. In contrast, it failed to antagonize the biological effects of neuropeptide Y in the rat vas deferens (Y2) and rat colon (Y3) and did not significantly competed for Y2/[125I]peptide YY-(3-36) binding sites in rat and human brain homogenates. Taken together, the results demonstrate further the high potency and selectivity of BIBP3226 for the neuropeptide Y Y1 receptor by establishing its lack of antagonist activity on the Y3 subtype.
Language of Publication
English
Unique Identifier
95394058

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MeSH Heading (Major)
Arginine|*AA/ME/PD; Gastrointestinal Hormones|*AI; Peptides|*AI; Receptors, Neuropeptide Y|*AI/CL
MeSH Heading
Animal; Binding, Competitive|DE; Brain|DE/ME; Colon|DE; Dose-Response Relationship, Drug; Human; Male; Muscle Contraction|DE; Muscle, Smooth|DE; Muscle, Smooth, Vascular|DE; Rabbits; Radioligand Assay; Rats; Saphenous Vein|DE; Vas Deferens|DE/ME

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0014-2999
Country of Publication
NETHERLANDS


Record 37 from database: MEDLINE
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Title
Nitric oxide as a neurotransmitter in human airways.
Author
Belvisi MG; Ward JK; Mitchell JA; Barnes PJ
Address
Department of Thoracic Medicine, National Heart and Lung Institute, Chelsea, London, U.K.
Source
Arch Int Pharmacodyn Ther, 1995 Jan, 329:1, 97-110
Abstract
Human airway smooth muscle possesses a prominent nonadrenergic noncholinergic (i-NANC) bronchodilator response. Nitric oxide (NO) appears to account for all the i-NANC response in human central and peripheral airways in vitro. Furthermore, it appears that i-NANC relaxations in human trachea are associated with a concomitant selective elevation of cGMP, but not cAMP levels, which are inhibited by an NO synthase (NOS) inhibitor. This confirms the hypothesis that the L-arginine/NO/cGMP pathway is responsible for mediating the i-NANC response in this tissue. It is not certain from where the NO is formed or the location of the NOS enzyme. However, in human trachea, NOS immunoreactivity (NOS-IR) has been described in nerve fibres originating from intrinsic neurons. In addition, the density of NOS-IR is reduced from proximal to distal airways and this correlates with functional data describing a reduced i-NANC relaxation response from central to peripheral airways. The i-NANC bronchodilator nerves are the only neural relaxant pathway in human airways and, therefore, it is important to determine whether there is any defect in the ability of these nerves to function in diseased airways. In fact, functional and immunohistochemical data suggest that there may be a deficiency in NOS-IR nerves leading to a decreased i-NANC response in tissue from patients with cystic fibrosis. NOS inhibitors appear to enhance the cholinergic bronchoconstriction in human airways in vitro. Therefore, if the nitrergic innervation is dysfunctional in inflammatory conditions, its absence may lead to exaggerated bronchoconstriction.
Language of Publication
English
Unique Identifier
95366871

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MeSH Heading (Major)
Neurotransmitters|*PH; Nitric Oxide|AI/*PH; Respiratory Physiology|*; Respiratory System|DE/*PH
MeSH Heading
Arginine|AA/PD; Bronchoconstriction|PH; Bronchodilator Agents|PD; Human; Muscle, Smooth|PH; Respiration|DE/PH; Support, Non-U.S. Gov't

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0003-9780
Country of Publication
BELGIUM


Record 38 from database: MEDLINE
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Title
New biomarkers of Maillard reaction damage to proteins.
Author
Wells Knecht KJ; Brinkmann E; Wells Knecht MC; Litchfield JE; Ahmed MU; Reddy S; Zyzak DV; Thorpe SR; Baynes JW
Address
Department of Chemistry and Biochemistry, University of South Carolina, Columbia 29208, USA.
Source
Nephrol Dial Transplant, 1996, 11 Suppl 5:, 41-7
Abstract
The amount of advanced glycation end-products (AGE) in tissue proteins increases in diabetes mellitus, and the concentration of a subclass of AGEs, known as glycoxidation products, also increases with chronological age in proteins. The rate of accumulation of glycoxidation products is accelerated in diabetes and age-adjusted concentrations of two glycoxidation products, N epsilon-(carboxymethyl)lysine (CML) and pentosidine, correlate with the severity of complication in diabetic patients. Although AGEs and glycoxidation products are implicated in the development of diabetic complications, these compounds are present at only trace concentrations in tissue proteins and account for only a fraction of the chemical modifications in AGE proteins prepared in vitro. The future of the AGE hypothesis depends on the chemical characterization of a significant fraction of the total AGEs in tissue proteins, a quantitative assessment of their effects on protein structure and function, and an assessment of their role as mediators of biological responses. In this manuscript we describe recent work leading to characterization of new AGEs and glycoxidation products. These compounds include: (1) the imidazolone adduct formed by reaction of 3-deoxyglucosone with arginine residues in protein; (2) N epsilon-(carboxyethyl)lysine, an analogue of CML formed on reaction of methylglyoxal with lysine; (3) glyoxal-lysine dimer; and (4) methyl-glyoxal-lysine dimer, which are imidazolium crosslinks formed by reaction of glyoxal or methylglyoxal with lysine residues in protein. The presence of 3-deoxyglucosone, methylglyoxal and glyoxal in vivo and the formation of the above AGEs in model carbonyl-amine reaction systems suggests that these AGEs are also formed in vivo and contribute to tissue damage resulting from the Maillard reaction.
Language of Publication
English
Unique Identifier
97197246

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MeSH Heading (Major)
Glycosylation End Products, Advanced|CH/*ME; Maillard Reaction|*; Proteins|*ME
MeSH Heading
Aging|ME; Arginine|AA/ME; Biological Markers; Diabetes Mellitus|CO/ME; Glycosylation; Human; Lysine|AA/ME; Molecular Structure; Norleucine|AA/ME; Oxidation-Reduction; Pyrroles|ME; Support, U.S. Gov't, P.H.S.

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0931-0509
Country of Publication
ENGLAND


Record 39 from database: MEDLINE
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Title
Modulation of coronary autoregulatory responses by endothelium-derived nitric oxide.
Author
Canty JM Jr; Smith TP Jr
Address
Department of Medicine, State University of New York, Buffalo Clinical Center 14215-3012, USA.
Source
Int J Cardiol, 1995 Jul, 50:3, 207-15
Abstract
There is increasing evidence that endothelium-derived nitric oxide production is an important mechanism contributing to the regulation of myocardial perfusion during ischemia distal to a coronary stenosis. Studies in conscious chronically instrumented animals have extended observations in isolated arterioles to demonstrate that inhibiting nitric oxide synthase with L-arginine analogs increases the vulnerability of the myocardium to ischemia. The variable extent to which endothelium-dependent function is impaired in human atherosclerosis raises the possibility that abnormalities in resistance vessel control contribute to the functional significance of a fixed epicardial coronary stenosis. This may explain the wide variability between the physiological effects of a given coronary stenosis and its angiographic severity. Aggressive intervention to normalize endothelium-dependent vasodilation and local nitric oxide release may have beneficial effects on the functional significance of a coronary stenosis.
Language of Publication
English
Unique Identifier
96103959

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MeSH Heading (Major)
Coronary Circulation|*; Endothelium-Derived Relaxing Factor|*PH; Homeostasis|*
MeSH Heading
Animal; Arginine|AA/PD; Constriction, Pathologic|ME; Coronary Disease|ME; Dogs; Human; Myocardial Ischemia|ME/PP; Nitric Oxide|AI/BI; Nitric-Oxide Synthase|AI; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0167-5273
Country of Publication
IRELAND


Record 40 from database: MEDLINE
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Title
BIBP 3226, the first selective neuropeptide Y1 receptor antagonist: a review of its pharmacological properties.
Author
Doods HN; Wieland HA; Engel W; Eberlein W; Willim KD; Entzeroth M; Wienen W; Rudolf K
Address
Division of Preclinical Research, Dr. Karl Thomae GmbH, Biberach, Germany.
Source
Regul Pept, 1996 Aug, 65:1, 71-7
Abstract
Based on the assumption that the pharmacophoric groups interacting with the Y1 receptor are located in the C-terminal part of neuropeptide Y, low molecular weight compounds with high affinity and selectivity for the Y1 receptor were designed and synthesized. The prototype BIBP 3226 possesses affinity for the Y1 receptor in the nanomolar range. In addition, this compound is selective displaying rather low affinity for Y2, Y3, Y4 and a set of 60 other receptors. Both biochemical and pharmacological studies showed that BIBP 3226 behaves as a competitive antagonist. Using BIBP 3226 it was possible to investigate the role of NPY and/or Y1 receptors in blood pressure regulation. The interesting observation was that antagonism to Y1 receptors had no major influence on the basal blood pressure but attenuated stress induced hypertension. This strongly supports the hypothesis that NPY is mainly released during stress involving intense sympathetic nervous system activation. Moreover, BIBP 3226 can be used to characterize NPY receptor subtypes. For instance, we were able to show that presynaptic NPY receptors mediating catecholamine release do not solely belong to the Y2 subtype, but that presynaptic Y1 receptors also exist. In conclusion, BIBP 3226 has been shown to be an important tool for the elucidation of the physiological role of Y1 receptors in the cardiovascular system.
Language of Publication
English
Unique Identifier
97030097

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MeSH Heading (Major)
Arginine|*AA/CH/PD; Receptors, Neuropeptide Y|*AI
MeSH Heading
Animal; Calcium|ME; Cyclic AMP|ME; Eating|DE; Heart|DE; Human; Presynaptic Terminals|DE; Rabbits; Rats

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0167-0115
Country of Publication
NETHERLANDS


Record 41 from database: MEDLINE
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Title
The role of orthotopic liver transplantation in the treatment of ornithine transcarbamylase deficiency.
Author
Busuttil AA; Goss JA; Seu P; Dulkanchainun TS; Yanni GS; McDiarmid SV; Busuttil RW
Address
Department of Surgery, University of California-Los Angeles School of Medicine, Los Angeles, CA 90095, USA.
Source
Liver Transpl Surg, 1998 Sep, 4:5, 350-4
Abstract
The purpose of this study was to combine our clinical experience with a review of the literature to determine the value of orthotopic liver transplantation in the treatment of both boys and girls with ornithine transcarbamylase deficiency. Three boys younger than 1 year of age with symptomatic ornithine transcarbamylase deficiency (median age, 116 days; range, 40 to 223 days) underwent orthotopic liver transplantation. The patients' growth, developmental progress, ammonia levels, and amino acid levels were analyzed pre- and post-liver transplantation. The clinical courses of the respective patients and the treatment modalities used were compared with published reports from 1978 through 1997. The median follow-up period in these 3 patients was 3.2 years (range, 9 months to 5.2 years). Orthotopic liver transplantation restored normal urea production and stabilized ammonia levels within 24 hours of surgery (median serum ammonia level 24 hours post-liver replacement, 43 micromol/L; range, 30 to 66 micromol/L). After liver replacement, arginine synthesis was normalized; however, plasma citrulline levels remained less than normal in all patients. Linear growth was evaluated in all 3 patients at the time of the most recent follow-up; median z scores for patient height and weight were -2.16 and -1.16, respectively. Standardized intelligence tests showed that 2 of the 3 patients continue to perform at age-appropriate levels. The third child was developmentally delayed pretransplantation at 4 months of age on presentation and continues to perform in a below-average fashion. Orthotopic liver transplantation results in the restoration of normal urea production and serum ammonia levels in the boy suffering from symptomatic ornithine transcarbamylase deficiency. Serum arginine, but not citrulline, levels are normalized, probably because of the persistent intestinal mucosa defect. Patient growth is similar to that in infants undergoing liver transplantation for other causes. When liver transplantation is performed before cognitive impairment occurs, intellectual development is normal, because the risk of additional episodes of hyperammonemia is elevated.
Language of Publication
English
Unique Identifier
98391803

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MeSH Heading (Major)
Amino Acid Metabolism, Inborn Errors|BL/EN/*SU; Ammonia|*BL; Arginine|*BL; Liver Transplantation|*; Ornithine Carbamoyltransferase|*DF
MeSH Heading
Case Report; Follow-Up Studies; Human; Infant; Infant, Newborn; Male; Retrospective Studies; Support, Non-U.S. Gov't; Transplantation, Homologous; Urea|BL

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW OF REPORTED CASES
ISSN
1074-3022
Country of Publication
UNITED STATES
CAS Registry/EC Number
EC 2.1.3.3 (Ornithine Carbamoyltransferase); 57-13-6 (Urea); 7004-12-8 (Arginine); 7664-41-7 (Ammonia)


Record 42 from database: MEDLINE
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Title
Renal endothelial function in humans.
Author
Mimran A
Address
Department of Internal Medicine, Hospital Lapeyronie, Montpellier, France.
Source
Curr Opin Nephrol Hypertens, 1998 Mar, 7:2, 149-52
Abstract
Animal experiments have shown extensively that the endothelial generation of nitric oxide participates in the regulation of renal haemodynamics and function, probably as a factor modulating the effects of endogenous vasoconstrictors. Although the endothelial function of the systemic vasculature is assessed through the vasodilatory effect of acetylcholine, only L-arginine infusion is available for studies of the influence of nitric oxide on the renal circulation in humans. In addition to peripheral vessels, L-arginine is a potent renal vasodilator, having no effect on the glomerular filtration rate; and the renal relaxation induced by L-arginine is markedly blunted in patients with essential hypertension. A few studies showing the renal vasoconstrictor effect of an inhibitor of nitric oxide synthesis have been reported.
Language of Publication
English
Unique Identifier
98190453

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MeSH Heading (Major)
Kidney|DE/*PH/PP
MeSH Heading
omega-N-Methylarginine|PD; Albuminuria|PP; Arginine|DU; Endothelium|PH/PP; Enzyme Inhibitors|PD; Human; Hypertension|PP; Nitric-Oxide Synthase|AI

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
1062-4821
Country of Publication
UNITED STATES


Record 43 from database: MEDLINE
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Title
Cardiovascular effects of L-arginine.
Author
Maxwell AJ; Cooke JP
Address
Section of Vascular Medicine, Stanford University, California, USA.
Source
Curr Opin Nephrol Hypertens, 1998 Jan, 7:1, 63-70
Abstract
Most of the known cardiovascular effects of L-arginine are exerted via its conversion to nitric oxide by nitric oxide synthase. Accumulating evidence indicates that supplemental administration of L-arginine is sufficient to restore endothelium-derived nitric oxide production in many disorders in which endothelium-derived nitric oxide production is altered. L-arginine may enhance nitric oxide production by competing as a substrate with an endogenous antagonist for nitric oxide synthase. In other cases, L-arginine may act by competing with molecular oxygen as a substrate so as to reduce the production of superoxide anion. It is likely that other mechanisms exist by which the nitric oxide synthase pathway can be perturbed. Regardless of the mechanism, a wide array of cardiovascular disorders characterized by endothelial dysfunction are reversible by L-arginine.
Language of Publication
English
Unique Identifier
98104447

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MeSH Heading (Major)
Arginine|PD/*PH; Cardiovascular Physiology|*/DE
MeSH Heading
Animal; Cardiovascular Diseases|DT/PP; Human

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
ISSN
1062-4821
Country of Publication
UNITED STATES


Record 44 from database: MEDLINE
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Title
Enhancement of nitric oxide synthesis by L-arginine supplementation in renal disease: is it good or bad?
Author
De Nicola L; Minutolo R; Bellizzi V; Andreucci M; La Verde A; Cianciaruso B
Address
Nephrology Division, School of Medicine-University Federico II, Naples, Italy.
Source
Miner Electrolyte Metab, 1997, 23:3-6, 144-50
Abstract
L-Arginine is a important component of our diet characterized by multiple physiological and pharmacological actions. In the last decade, this amino acid has attracted major interest since it has been identified as the natural substrate of nitric oxide, and is now recognized to play a major role in the regulation of vascular tone. This review, while summarizing the knowledge of the renal actions of the L-arginine/nitric oxide pathway in health and renal disease, focuses on the potential therapeutic implications of the increase in nitric oxide synthesis attained by L-arginine supplementation.
Language of Publication
English
Unique Identifier
98048346

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MeSH Heading (Major)
Arginine|ME/*TU; Dietary Supplements|*; Kidney Diseases|*DH/ME; Nitric Oxide|*BI
MeSH Heading
Animal; Comparative Study; Disease Models, Animal; Human; Reference Values; Support, Non-U.S. Gov't; Treatment Outcome

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0378-0392
Country of Publication
SWITZERLAND


Record 45 from database: MEDLINE
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Title
Cytokines and L-arginine in renal injury and repair [editorial]
Author
Ketteler M; Border WA; Noble NA
Address
Source
Am J Physiol, 1994 Aug, 267:2 Pt 2, F197-207
Abstract
Advances in molecular biology have identified cytokines as mediators of pathophysiological changes in chronic renal disease. Transforming growth factor-beta (TGF-beta) plays an important role in the pathogenesis of glomerular and interstitial fibrosis, whereas platelet-derived growth factor (PDGF) is involved in proliferative changes in chronic progressive renal diseases. Tumor necrosis factor-alpha and interleukins are expressed in experimental models of renal disease and are causes of inflammation and cell migration. Cytokines act by many different mechanisms, and one target of their action may be L-arginine metabolism. Since the discovery of the effector molecule nitric oxide (NO), generated from L-arginine, knowledge of this pathway has increased dramatically. It became evident that the L-arginine/NO pathway is of major importance in the regulation of hemodynamics and neurotransmission, in host defense against intracellular microorganisms, and in immunologic tissue injury. This pathway is induced by proinflammatory cytokines and possibly regulated by TGF-beta and PDGF. L-Arginine is also metabolized to L-ornithine, which can be processed to polyamines or to L-proline. As polyamines are important mediators of cell growth and L-proline is a substrate for collagen synthesis, both pathways, once activated, may be important in repair processes. It is likely that cytokines and L-arginine metabolism are interconnected and that both are involved in the inflammation, tissue repair, and fibrogenesis processes in the kidney. Dietary protein restriction in progressive renal diseases may substantially affect both systems. This review summarizes current knowledge about interactions of cytokines and L-arginine metabolism and the relevance to renal diseases.
Language of Publication
English
Unique Identifier
94346412

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MeSH Heading (Major)
Arginine|AD/*PH; Cytokines|*PH; Kidney Diseases|*PP; Wound Healing|*PH
MeSH Heading
Animal; Diet; Human; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type
EDITORIAL; REVIEW; REVIEW, TUTORIAL
ISSN
0002-9513
Country of Publication
UNITED STATES


Record 46 from database: MEDLINE
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Title
L-arginine and malignant disease: a potential therapeutic role?
Author
Brittenden J; Heys SD; Eremin O
Address
Department of Surgery, University of Aberdeen, UK.
Source
Eur J Surg Oncol, 1994 Apr, 20:2, 189-92
Abstract
The beneficial effects of L-arginine on nitrogen metabolism, wound healing and host defences demonstrated in animal studies have been shown to be significant in patient studies as well. With tumours, interacting effects on neoplastic cells and host defence mechanisms indicate strategies for beneficial use in cancer patients, especially in association with chemotherapy.
Language of Publication
English
Unique Identifier
94237311

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MeSH Heading (Major)
Arginine|PD/*TU; Neoplasms|*DT
MeSH Heading
Animal; Human; Neoplasms, Experimental|DT; Wound Healing|DE

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0748-7983
Country of Publication
ENGLAND


Record 47 from database: MEDLINE
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Title
Can arginine and ornithine support gut functions?
Author
Cynober L
Address
Laboratoire de Biochimie, HÈopital Saint-Antoine, Paris, France.
Source
Gut, 1994 Jan, 35:1 Suppl, S42-5
Abstract
Arginine and ornithine are precursors of nitric oxide and polyamines, respectively. These metabolites intimately participate in permeability and adaptive responses of the gut. The liver possesses high arginase activity as an intrinsic part of urea synthesis and would consume most of the portal supply of dietary arginine. The gut reduces this possibility by converting dietary arginine to citrulline, which effectively bypass the liver and is resynthesized to arginine in the kidney. Dietary ornithine supplementation, in the form of ornithine alpha-ketoglutarate (OKG) can be considered as an arginine precursor. Several supplement studies have shown both amino acids to promote growth hormone and insulin secretion with anabolic effects in postoperative patients. Their intermediary metabolites (for example, glutamine, proline) may also be of benefit in trauma metabolism. Specific effects of either amino acid on the gut are poorly reported. One recent animal study showed improved morphology after OKG administration, perhaps through increased polyamine secretion. Generation of nitric oxide from arginine has two facets. Excess production from high dose arginine potentiated the effects of experimentally induced sepsis, whereas low doses improved survival. These considerations suggest that the role of enteral diet supplementation with arginine or OKG should be urgently examined for any benefits it may have on mucosal barrier function.
Language of Publication
English
Unique Identifier
94171129

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MeSH Heading (Major)
Arginine|*ME/PD; Enteral Nutrition|*; Intestines|DE/ME/*PH; Ornithine|*ME/PD
MeSH Heading
Citrulline|ME; Human; Nitric Oxide|ME

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0017-5749
Country of Publication
ENGLAND


Record 48 from database: MEDLINE
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Title
Impact of the L-arginine/nitric oxide system in pregnancy.
Author
Neri I; Di Renzo GC; Caserta G; Gallinelli A; Facchinetti F
Address
Department of Obstetrics and Gynecology, University of Modena, Italy.
Source
Obstet Gynecol Surv, 1995 Dec, 50:12, 851-8
Abstract
Nitric Oxide (NO) recently becomes of clinical interest because of its relaxant effects on smooth muscle. In addition to endothelial cells, also myometrial cells contain the enzyme implicated in the NO production. This review is aimed toward those studies concerned with the production, metabolism, and effects of NO that could be relevant for the obstetricians. The potential clinical interest of such information covers the main areas of pregnancy complications, namely preterm delivery, preeclampsia, and intrauterine growth retardation. Moreover, original data are included in order to support the therapeutical implications of the manipulation of L-arginine-NO system in case of pregnancy disorders.
Language of Publication
English
Unique Identifier
96164291

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MeSH Heading (Major)
Arginine|AA/*PD; Nitric Oxide|BI/*PD; Pregnancy|BL/*PH
MeSH Heading
Female; Human; Muscle, Smooth, Vascular|PH; Nitric-Oxide Synthase|ME; Pre-Eclampsia|BL; Uterine Contraction; Uteroplacental Circulation|PH

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW LITERATURE
ISSN
0029-7828
Country of Publication
UNITED STATES


Record 49 from database: MEDLINE
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Title
Nitric oxide in the regulation of renal blood flow.
Author
Ito S; Carretero OA; Abe K
Address
Second Department of Internal Medicine, Tohoku University School of Medicine, Sendai, Japan.
Source
New Horiz, 1995 Nov, 3:4, 615-23
Abstract
Nitric oxide (NO.) is a simple molecule, synthesized from the amino acid L-arginine by a family of enzymes, NO. synthase (NOS). The L-arginine-NO. pathway plays a dominant role in the control of renal function under various physiologic and pathologic conditions. NO. is continuously released by the endothelium, and controls the tone of the glomerular afferent arteriole by modulating myogenic response and the action of various vasoconstrictors. On the other hand, NO. produced by the macula densa controls glomerular hemodynamics indirectly through tubuloglomerular feedback and renin release. It appears that NO. is also involved in medullary circulation and tubular function and, therefore, pressure natriuresis. Thus, the L-arginine-NO. pathway seems to play an important role in sodium hemostasis. Under certain pathologic conditions, NOS may be induced in the endothelial, vascular smooth muscle, mesangial, and tubular epithelial cells, and in macrophages, producing a large amount of NO., which may contribute to progression of renal disease. In acute renal failure, endogenous NO. seems to have a protective role against renal damage, as the inhibition of NOS aggravates renal dysfunction and histology. Although dietary L-arginine supplementation has been shown to protect against progression of renal damage, clarification of the exact role of NO. and the mechanism of L-arginine's beneficial effects must await further investigation. Finally, the recent development of targeting specific NOS isoforms or tissue may help clarify the role of the L-arginine-NO pathway in various physiologic and pathologic conditions, leading to the development of new therapeutic modalities.
Language of Publication
English
Unique Identifier
96162665

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MeSH Heading (Major)
Glomerular Filtration Rate|*/DE; Kidney Failure, Acute|*DT/*PP; Nitric Oxide|CH/*PH; Renal Circulation|*/DE
MeSH Heading
Arginine|TU; Homeostasis|DE; Human; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
1063-7389
Country of Publication
UNITED STATES


Record 50 from database: MEDLINE
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Title
Advanced glycation end-products in diabetic nephropathy.
Author
Sugiyama S; Miyata T; Horie K; Iida Y; Tsuyuki M; Tanaka H; Maeda K
Address
Department of Nephrology, Chukyo Hospital, Nagoya, Japan.
Source
Nephrol Dial Transplant, 1996, 11 Suppl 5:, 91-4
Abstract
Advanced glycation end-products (AGEs) are the pigmented and fluorescent adduct formed by a non-enzymatic reaction between sugar and protein. Since AGEs are generated in high glucose milieu, then induce the structural and functional alteration of matnx proteins, and have biological effects on various kinds of cells including mesangial cells, AGEs have been implicated in tissue damage of diabetic nephropathy. To elucidate the factor(s) that determine the AGEs level in diabetic nephropathy, we quantitated the plasma pentosidine level of different status of diabetic nephropathy by HPLC assay. The plasma pentosidine level in diabetic nephropathy was found to be determined by factors such as renal function control of glucose and the patient's age; of these, renal function was the most critical factor. For a better understanding of the pathological role of AGEs in diabetic nephropathy, we then examined renal tissues of diabetic nephropathy immunohistochemically using antibodies specific for AGE proteins. Immunohistochemistry revealed the positive immunostaining for AGEs in the expanded mesangial area of diffuse diabetic glomerulosclerosis. The degree of staining was stronger than that in patients of IgA nephropathy with a similar degree of mesangial expansion. The nodular lesions, characteristic of diabetic nephropathy, were also stained positive for AGEs. These findings suggests a potential link of AGEs accumulation, which may be determined by renal function, control of glucose and age, to renal tissue damage in diabetic nephropathy.
Language of Publication
English
Unique Identifier
97197256

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MeSH Heading (Major)
Diabetic Nephropathies|*ET/*ME/PA; Glycosylation End Products, Advanced|*ME
MeSH Heading
Animal; Arginine|AA/ME; Blood Glucose|ME; Glycosylation; Human; Immunohistochemistry; Lysine|AA/ME; Norleucine|AA/ME; Proteins|ME; Pyrroles|ME

Publication Type
JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN
0931-0509
Country of Publication
ENGLAND

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