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DIMETHYL GLYCINE HYDROCHLORIDE

or

N,N-DIMETHYL GLYCINE

Technical Studies

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HealthGate Documents

Record 1 from database: MEDLINE

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Title

Effects of iron chelates on the transferrin-free culture of rat dermal fibroblasts through active oxygen generation.

Author

Yabe N; Matsui H

Address

Department of Hygiene, Dokkyo University School of Medicine, Tochigi, Japan.

Source

In Vitro Cell Dev Biol Anim, 1997 Jul, 33:7, 527-35

Abstract

Effects of nonchelating and chelating agents at 10 mM on the serum-free culture of rat dermal fibroblasts were investigated. A strong iron-chelating agent, iminodiacetic acid (IDA), and a weak one, dihydroxyethylglycine (DHEG), decreased iron permeation into preconfluent fibroblasts. A weak iron-chelating agent, glycylglycine (GG), a nonchelating agent, N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid (HEPES), and human apotransferrin (10 micrograms/ml) increased the permeation with time. Iron may be essential for survival of fibroblasts because subconfluent fibroblasts exposed to 100 microM FeSO4 in combination with transferrin, HEPES, or GG significantly decreased to release lactate dehydrogenase into the medium. Superoxide dismutase and dimethyl sulfoxide blocked the enzyme release, suggesting that superoxide and hydroxyl radical induce cellular damage but hydrogen peroxide (H2O2) generated by superoxide dismutation does not. GG significantly reduced H2O2 cytotoxicity. DHEG acted as a potent promoter of the iron-stimulated cellular damage if ascorbate or H2O2 was added to the medium. FeSO4 and FeCl3 (50 to 100 microM) individually combined with IDA maximally promoted fibroblast proliferation. Ascorbate increased formation of thiobarbituric acid-reactive substances from deoxyribose in the medium supplemented with FeSO4 and either IDA or DHEG. Conversely, ascorbate decreased the formation in the medium with FeSO4 and with or without other agents. Fibroblast proliferation may thus be stimulated through the active oxygen generation mediated by a redox-cycling between Fe3+ and Fe2+, which are dissolved in the medium at a high concentration, rather than through delivery of iron into the cells.

Language of Publication

English

Unique Identifier

97427281

MeSH Heading (Major)

Fibroblasts|*DE/*ME; Iron Chelating Agents|*PD; Oxygen|*ME; Transferrin|PD/*PH

MeSH Heading

Animal; Antioxidants|PD; Apoproteins|PD; Cell Division|DE; Cells, Cultured; Dimethyl Sulfoxide|PD; Ferrous Compounds|PD; Glycine|AA/PD; Glycylglycine|PD; Human; Hydrogen Peroxide|ME/PD; Imino Acids|PD; Lactate Dehydrogenase|SE; Male; Rats; Rats, Wistar; Superoxide Dismutase|PD; Thiobarbituric Acid Reactive Substances|ME

Publication Type

JOURNAL ARTICLE

ISSN

1071-2690

Country of Publication

UNITED STATES

Record 2 from database: MEDLINE
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Title

A postmortem study of glycine and its potential precursors in chronic schizophrenics.

Author

Kurumaji A; Watanabe A; Kumashiro S; Semba J; Toru M

Address

Department of Neuropsychiatry, Tokyo Medical and Dental University School of Medicine, Japan.

Source

Neurochem Int, 1996 Sep, 29:3, 239-45

Abstract

We have measured the concentrations of glycine and its potential precursors, serine and threonine, in 20 areas of the postmortem brains of chronic schizophrenics and controls using high-performance liquid chromatography by pre-column derivatization with dimethyl-amino-azobenzene sulphonyl chloride. The regional distribution pattern of glycine in the postmortem brains with and without the disease was more similar to that of serine (r = 0.874, P < 0.0001) than to that of threonine (r = 0.476, P < 0.01). A multiple regression analysis with regressor variables including diagnosis, age at death and interval between death and freezing revealed that there is a significant difference between schizophrenics and controls in the contents of these amino acids in a number of brain areas. The level of glycine in the orbitofrontal cortex of schizophrenics was found to be significantly increased in schizophrenics, with a tendency to an increase in that of serine. The increase in glycine was also significantly high in the off-drug group of schizophrenics who had not taken antipsychotics more than 40 days before death. Prominent decreases in both glycine and serine were observed in the somesthetic cortex of the on-drug schizophrenics. Serine was found to be significantly decreased in the putamen of the off-drug schizophrenics. A marked decrease in threonine was also observed in the supramarginal cortex and posterior portion of the lateral occipitotemporal cortex of the off-drug group of schizophrenics and in the putamen of all schizophrenics. The highly similar distribution pattern of glycine and serine in the postmortem brains supports the close coupling of synthesis and metabolism between these chemicals in human brains. The increased content of glycine in the orbitofrontal cortex, the reduced level of serine in the putamen and the decrease in threonine in the cerebral cortices, which were prominent in the off-drug schizophrenics, may be involved in the pathophysiology of schizophrenia.

Language of Publication

English

Unique Identifier

97039730

MeSH Heading (Major)

Brain Chemistry|*PH; Glycine|*ME; Schizophrenia|*ME

MeSH Heading

p-Dimethylaminoazobenzene; Adult; Aged; Chromatography, High Pressure Liquid; Chronic Disease; Female; Human; Indicators and Reagents; Male; Middle Age; Postmortem Changes; Serine|ME; Support, Non-U.S. Gov't; Threonine|ME

Publication Type

JOURNAL ARTICLE

ISSN

0197-0186

Country of Publication

ENGLAND

Record 3 from database: MEDLINE
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Title

Inhibition of redox cycling of methoxatin (PQQ), and of superoxide release by phagocytic white cells.

Author

Bishop A; Paz MA; Gallop PM; Karnovsky ML

Address

Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.

Source

Free Radic Biol Med, 1995 Mar, 18:3, 617-20

Abstract

The iodonium compounds diphenyleneiodonium and diphenyliodonium, and the amine compounds, 4,5-dimethyl phenylene diamine, N,N-dimethyl 1,4-phenylene diamine, 1,2-diamino-4,5-methyleneoxybenzene, and aminomalononitrile inhibit methoxatin's (PQQ's) redox activity in vitro, that is, the methoxatin-coupled oxidation of glycine and reduction of nitroblue tetrazolium to formazan. The compounds mentioned above also inhibit phorbol myristate acetate (PMA) stimulated superoxide release by phagocytic white cells--determined mainly as the superoxide dismutase sensitive reduction of ferricytochrome C. Related compounds, 3,4-diaminopyridine and 4-dimethylamino-benzylamine, did not inhibit redox activity of PQQ in vitro, nor did they inhibit PMA stimulated superoxide production in monocytes or neutrophils. Thus, there is a correlation between an agent's ability to inhibit PQQ redox cycling and its ability to inhibit superoxide release by phagocytes. The findings are a further indication that PQQ is involved in the respiratory burst of phagocytic cells.

Language of Publication

English

Unique Identifier

97255925

MeSH Heading (Major)

Coenzymes|*ME; Phagocytes|DE/*ME; Quinolones|*ME; Superoxides|*ME

MeSH Heading

Amines|PD; Animal; Biphenyl Compounds|PD; Free Radicals|ME; Guinea Pigs; Human; In Vitro; Onium Compounds|PD; Oxidation-Reduction; Respiratory Burst; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0891-5849

Country of Publication

UNITED STATES

Record 4 from database: MEDLINE
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Title

Design, synthesis, and evaluation of mitomycin-tethered phosphorothioate oligodeoxynucleotides.

Author

Huh N; Rege AA; Yoo B; Kogan TP; Kohn H

Address

Department of Chemistry, University of Houston, Texas 77204-5641, USA.

Source

Bioconjug Chem, 1996 Nov, 7:6, 659-69

Abstract

Mitomycin C (1) is the prototypical bioreductive alkylating agent. Studies have shown that mitomycin C and its derivatives selectively alkylate guanine residues within di- and trinucleotide DNA sequences. This investigation sought to improve the selective DNA bonding properties of the mitomycins by coupling them with antisense oligodeoxynucleotides. Two procedures were developed that allowed the attachment of a phosphorothioate oligodeoxynucleotide containing a hexylamino spacer at the 5' terminus with a C(10)-activated mitomycin. In the first procedure, decarbamoylation of 1 (NaOCH3/ benzene) afforded 10-decarbamoylmitomycin C (10), which was treated with either dimethyl sulfate or methylthiochloroformate and base to yield 10-decarbamoylporfiromycin (11) and N(1a)-[(methylthio)-carbonyl]-10-decarbamoylmitomycin C (12), respectively. Activation of the C(10) site in 11 and 12 with 1,1'-carbonyldiimidazole or with 1,1'-thiocarbonyldiimidazole provided the N(1a)-substituted mitomycin 10-decarbamoyl-10-O-carbonylimidazoles (5, 7) and 10-decarbamoyl-10-O-thiocarbonylimidazoles (6, 8), respectively. Compounds 5-8 were reacted with glycine methyl ester hydrochloride (17) and base in both methylene chloride and aqueous buffered solutions to determine the ease and efficiency in which these C(10)-activated mitomycin derivatives coupled to amines. It was found that 5-8 all reacted with 17 in methylene chloride to give the coupled products 18-21 but that improved amine coupling yields in water were observed for the 10-decarbamoyl-10-O-thiocarbonylimidazoles 6 and 8 as compared with the 10-decarbamoyl-10-O-carbonylimidazoles 5 and 7. This finding led to the coupling of the phosphorothioate oligodeoxynucleotide, H2N(CH2)6-P(S)(OH)-GGCCCCGTG-GTGGCTCCAT (22) to 8. Compound 22 complemented a 19-base sequence in the translation initiation region of the human A-raf-1 gene. Use of excess 8 (28 equiv) with 22 gave only a 36% yield of the coupled product 23, which proved difficult to separate from 22. In the second procedure, phosphorothioate oligodexynucleotides that contained a hexylamino spacer at the 5'termini were coupled to 10-des(carbamoyloxy)-10-isothiocyanatoporfiromycin (9). Compound 9 was prepared in four steps from 11. Mesylation (methanesulfonyl chloride/pyridine) of 11 gave the C(10) mesylate 13, which was then treated with NaN3 (dimethylformamide, 90 degrees C) to give 10-des(carbamoyloxy)-10-azidoporfiromycin (14). Catalytic reduction (PtO2, H2) of 14 in pyridine afforded C(10) amine 15. Treatment of 15 with di-2-pyridyl thionocarbonate provided the desired 10-des(carbamoyloxy)-10-isothiocyanatoporfiromycin (9). Compound 9 readily coupled with 17 and base in both methylene chloride and aqueous buffered solutions to give 25. Use of the 5'hexylaminophosphorothioate oligodeoxynucleotides 32-35 in place of 17 gave the conjugated adducts 28-31, respectively, in a 12% to near-quantitative yield. The products were purified by semipreparative HPLC. Antisense agents 28-31 were designed to target a 30-base-long region from the coding region of the human FGFR1 gene. One adduct, 29, reduced the number of FGFR1 receptors in human aortic smooth cells for bFGF on the cell surface, which suggested down-regulation of FGFR1 gene expression. Further, 29 inhibited cultured human aortic smooth muscle cell proliferation and was less cytotoxic than porfiromycin (2). The biological assay data suggest that the phosphorothioate oligodexynucleotide porfiromycin conjugates may be more target selective and less toxic than either mitomycin or porfiromycin and thus be promising therapeutic agents.

Language of Publication

English

Unique Identifier

97107759

MeSH Heading (Major)

Mitomycin C|*AA/CH; Oligonucleotides|*CS; Organothiophosphorus Compounds|CH/*CS; Porfiromycin|*AA/CH/PD

MeSH Heading

Chromatography, High Pressure Liquid; Human; Muscle, Smooth, Vascular|DE/ME; Nuclear Magnetic Resonance; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

1043-1802

Country of Publication

UNITED STATES

Record 5 from database: MEDLINE
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Title

Assessment of the anti-microbial agent C31G as a spermicide: comparison with nonoxynol-9.

Author

Thompson KA; Malamud D; Storey BT

Address

Department of Obstetrics and Gynecology, School of Medicine, University of Pennsylvania, Philadelphia, USA.

Source

Contraception, 1996 May, 53:5, 313-8

Abstract

The broad-spectrum anti-microbial agent, C31G, containing an equimolar mixture of n-dodecyl-dimethylamine-N-oxide (C12-N-O) and N-(n-dodecyl), N-dimethyl-glycine (C12-betaine), was tested for spermicidal activity in comparison with the currently used spermicide, nonoxynol-9 (N-9). The rate of sperm cell permeabilization by the spermicides, as assayed with the fluorescent probe, TO-PRO-1, increased as the cube of the C31G concentration, while the rate increase was linear with N-9 concentration. At 0.04%, the rate of sperm cell permeabilization with both spermicides is at the limit of rapid measurement. C31G diffuses through cervical mucus at a more rapid rate than does N-9. C31G has long been known to aid wound healing and reduce inflammation, whereas N-9 has been reported to induce vaginal irritation. C31G would, thus, seem to have the spermicidal efficacy, the broad range of anti-microbial activity, and the lack of inflammatory activity that is sought in the ideal vaginal spermicide.

Language of Publication

English

Unique Identifier

96315389

MeSH Heading (Major)

Anti-Infective Agents|*; Betaine|*AA/AE/ME; Fatty Acids, Unsaturated|*/AE/ME; Nonoxynol|*/AE; Spermatocidal Agents|*

MeSH Heading

Adult; Cell Membrane Permeability|DE; Cervix Mucus|ME; Comparative Study; Fluorescent Dyes; Human; Male; Spermatozoa|DE; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0010-7824

Country of Publication

UNITED STATES

Record 6 from database: MEDLINE
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Title

NADPH-cytochrome c reductase from human neutrophil membranes: purification, characterization and localization.

Author

Nisimoto Y; Otsuka Murakami H; Iwata S

Address

Department of Biochemistry, Aichi Medical University, Japan.

Source

Biochem J, 1994 Feb, 297 ( Pt 3):, 585-93

Abstract

Neutrophil-membrane-associated NADPH-cytochrome c reductase and cytochrome b558 were separately eluted and highly purified by a combination of ion-exchange Sepharose, N-amino-octylagarose, 2',5'-ADP-Sepharose and heparin-Sepharose column chromatographies. The purified cytochrome c reductase with an apparent molecular mass of 68 kDa contained FMN and FAD (FMN/FAD approx. 1). Cytochrome b558 prepared in the presence of phospholipids and FAD showed marked O2-.-producing activity (Vmax., 8.53 mumol of O2-./min per mg of cytochrome; Km for NADPH 58.8 microM) in a cell-free assay system consisting of cytosol, arachidonate and GTP[S]. However, when it was obtained without FAD added to the purification process, it had negligible FAD and little or no O2-.-forming activity in the reconstituted system. The NADPH oxidase activity was not markedly stimulated on incubation of the purified reductase with either flavinated or flavin-depleted cytochrome b558 in the cell-free system, suggesting that the reductase is not likely to be involved in neutrophil O2-. generation. The purified reductase cross-reacted with polyclonal antibodies against both hepatic NADPH-cytochrome P-450 reductase and a synthetic peptide, ILVGPGTGIAPFRSF, which indicates residues 529-543 located in the glycine-rich NADPH-binding domain of the P-450 reductase, but cytochrome b558 did not produce any immunoreactive bands to these antibodies. These antibodies also produced a positive reaction with a 76 kDa protein from dimethyl sulphoxide-induced HL-60-cell microsomes. After solubilization of the microsomal membranes, the 76 kDa protein was readily converted into a partially proteolysed form (68 kDa) even in the presence of antiproteases. In addition, the microsomal fraction shows a CO difference spectrum with a peak at about 454 nm and a trough at 476 nm in the presence of dithionite, indicating the presence of a cytochrome P-450-like haemoprotein.

Language of Publication

English

Unique Identifier

94153334

MeSH Heading (Major)

Neutrophils|*EN; NADPH-Ferrihemoprotein Reductase|*IP/ME

MeSH Heading

Amino Acid Sequence; Blotting, Western; Carbon Monoxide; Catalysis; Cell Membrane|EN; Chromatography, Affinity; Chromatography, Gel; Chromatography, Ion Exchange; Cytochrome b|IP/ME; Electrophoresis, Polyacrylamide Gel; Human; Microsomes|EN; Molecular Sequence Data

Publication Type

JOURNAL ARTICLE

ISSN

0264-6021

Country of Publication

ENGLAND

Record 7 from database: MEDLINE
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Title

Effect of cystine dimethylester on renal solute handling and isolated renal tubule transport in the rat: a new model of the Fanconi syndrome.

Author

Foreman JW; Bowring MA; Lee J; States B; Segal S

Address

Division of Biochemical Development and Molecular Diseases, Children's Hospital of Philadelphia, PA 19104.

Source

Metabolism, 1987 Dec, 36:12, 1185-91

Abstract

The effect of cystine dimethylester on the renal handling of phosphate, glucose, alpha-amino nitrogen, amino acids, and protein in vivo and on the uptake of lysine, glycine, taurine, and alpha-methyl glucoside by isolated renal tubules in vitro was studied in adult male rats. Parenteral administration of 400 mumol twice a day for four days of cystine dimethylester led to an increased urine volume, and excretion of phosphate, glucose, alpha-amino nitrogen, and the amino acids glutamine, proline, alanine, 1/2 cystine, ornithine, lysine, histidine, and glycine. Cystine dimethylester treatment did not affect the creatine clearance nor were any renal anatomic abnormalities noted. Intracellular cysteine, but not cystine, was increased in the kidney after the four days of treatment. Pre-incubation of isolated renal tubules with 2 mmol/L cystine dimethylester for ten minutes markedly inhibited the uptake of 0.025 mmol/L lysine, 0.1 mmol/L glycine, 0.01 mmol/L taurine, and 2 mmol/L alpha-methyl glucoside. Incubation with 2 mmol/L cystine dimethylester for ten minutes did not affect the ability of the renal tubule to exclude trypan blue dye, although longer incubation times did lead to significant staining. The intracellular cystine concentration of the renal tubule did rise significantly after incubation with cystine dimethylester, a biochemical correlate of the human disease cystinosis. These studies indicate that cystine dimethylester can induce an experimental form of the Fanconi syndrome both in vivo and in vitro and offers a new model for investigating the mechanisms underlying this enigmatic disorder.

Language of Publication

English

Unique Identifier

88065063

MeSH Heading (Major)

Cystine|*AA/PD/TO; Disease Models, Animal|*; Fanconi Syndrome|CI/*ME; Kidney Tubules, Proximal|DE/*ME

MeSH Heading

Amino Acids|ME; Animal; Cystinosis|CI/ME; Human; Male; Methylglucosides|ME; Rats; Rats, Inbred Strains; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0026-0495

Country of Publication

UNITED STATES

CAS Registry/EC Number

0 (Amino Acids); 0 (Methylglucosides); 1069-29-0 (cystine dimethyl ester); 24645-67-8 (Cystine); 97-30-3 (alpha-methylglucoside)

Record 8 from database: MEDLINE
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Title

Inhibition of human leukocyte elastase by N-substituted tripeptide trifluoromethyl ketones.

Author

Skiles JW; Fuchs V; Chow G; Skoog M

Address

Department of Biochemistry, Boehringer Ingelheim Pharmaceuticals Inc., Ridgefield, CT 06877.

Source

Res Commun Chem Pathol Pharmacol, 1990 Jun, 68:3, 365-74

Abstract

Several tripeptide trifluoromethyl ketones containing non-naturally occurring N-substituted glycine residues at the P2-position are effective human leukocyte elastase (HLE) inhibitors in vitro and possess IC50 values in the submicromolar range. Deletion of the amino acid at the P3-subsite region affords inactive compounds. The trifluoromethyl ketone derivative of valine is the preferred residue at the P1-position; whereas, the corresponding glycine or alpha, alpha-dimethyl glycine analogs result in inactive compounds.

Language of Publication

English

Unique Identifier

90349916

MeSH Heading (Major)

Ketones|*PD; Leukocytes|*EN; Oligopeptides|*PD; Pancreatopeptidase|*AI

MeSH Heading

Amino Acid Sequence; Binding Sites; Human; In Vitro; Molecular Sequence Data; Structure-Activity Relationship; Substrate Specificity

Publication Type

JOURNAL ARTICLE

ISSN

0034-5164

Country of Publication

UNITED STATES

CAS Registry/EC Number

EC 3.4.21.36 (Pancreatopeptidase); 0 (Ketones); 0 (Oligopeptides)

Record 9 from database: MEDLINE
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Title

Activating mutation of the Ha-ras gene in chemically induced tumors of the hamster cheek pouch.

Author

Gimenez-Conti IB; Bianchi AB; Stockman SL; Conti CJ; Slaga TJ

Address

Science Park-Research Division, University of Texas M. D. Anderson Cancer Center, Smithville 78957.

Source

Mol Carcinog, 1992, 5:4, 259-63

Abstract

The presence of an activating mutation in the Ha-ras gene in hamster cheek pouch tumors induced by 7,12-dimethylbenz[a]a nthracene (DMBA) complete carcinogenesis was investigated. The normal sequence of a fragment of genomic DNA encompassing codon 61 of the Ha-ras gene was amplified by the polymerase chain reaction using primers designed for a highly conserved region of the mouse Ha-ras-1 gene. The sequence of the amplified fragment was determined by a direct sequencing technique and exhibited 83.3% and 87.5% homology with the corresponding human and mouse sequences, respectively. At the amino acid level, the sequence was identical among the three species. Paraffin sections of 11 squamous cell carcinomas of the cheek pouch were used to detect mutated Ha-ras alleles. DNA sequencing of the tumors showed that six of 11 tumors presented an A----T transversion in the second position of codon 61, resulting in an amino acid change from glycine to leucine. As has been demonstrated in other systems, we have shown a specific mutation of the Ha-ras gene in chemically induced tumors of the hamster cheek pouch, further supporting the role of this oncogene in chemical carcinogenesis.

Language of Publication

English

Unique Identifier

92360141

MeSH Heading (Major)

Carcinoma, Squamous Cell|CI/*GE/PA; Genes, ras|*; Mouth Neoplasms|CI/*GE/PA; Mutagenesis|*

MeSH Heading

Alleles; Amino Acid Sequence; Animal; Base Sequence; Comparative Study; DNA Mutational Analysis; Hamsters; Human; Mesocricetus; Mice; Molecular Sequence Data; Oligodeoxyribonucleotides; Polymerase Chain Reaction; Sequence Homology, Nucleic Acid; Support, U.S. Gov't, P.H.S.; 9,10-Dimethyl-1,2-benzanthracene|DIMETHYLBENZANTHRACENE 09 10 01 02

Publication Type

JOURNAL ARTICLE

ISSN

0899-1987

Country of Publication

UNITED STATES

CAS Registry/EC Number

0 (Oligodeoxyribonucleotides); 57-97-6 (9,10-Dimethyl-1,2-benzanthracene)

Record 10 from database: MEDLINE
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Title

C31G, a new agent for oral use with potent antimicrobial and antiadherence properties.

Author

Corner AM; Dolan MM; Yankell SL; Malamud D

Address

Department of Biochemistry, School of Dental Medicine, University of Pennsylvania, Philadelphia 19104.

Source

Antimicrob Agents Chemother, 1988 Mar, 32:3, 350-3

Abstract

C31G, an equimolar mixture of alkyl dimethyl glycine and alkyl dimethyl amine oxide, was evaluated for antimicrobial and antiadherence properties. The efficacy of C31G, its two components, and several commercial mouth rinses was determined in assays measuring inhibition of glycolysis, inhibition of bacterial adherence, and MICs. Inhibition of glycolysis was determined by using a saliva sediment model, with glycolytic activity expressed as the change in pH relative to that of a control. Adherence studies were undertaken with Streptococcus sobrinus 6715 to measure inhibition of adherence to nichrome wires. MICs were determined against selected microorganisms by standard methods. C31G demonstrated broad-spectrum antimicrobial properties, with activity against both gram-positive and gram-negative organisms and Candida albicans, a yeast. C31G inhibited both glycolysis by salivary bacteria and adherence of Streptococcus strains to wire mesh. C31G was more effective in the assays conducted than any commercial formulation tested and was as effective as chlorhexidine. A synergistic effect was demonstrated between the individual components of C31G, and no loss of activity was noted when it was formulated into a mouth rinse vehicle.

Language of Publication

English

Unique Identifier

88208370

MeSH Heading (Major)

Anti-Infective Agents|AD/*PD; Bacterial Adhesion|*DE; Betaine|*AA/AD/PD; Fatty Acids, Unsaturated|AD/*PD

MeSH Heading

Bacteria|DE; Glycolysis|DE; Human; Hydrogen-Ion Concentration; Microbial Sensitivity Tests; Mouthwashes; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0066-4804

Country of Publication

UNITED STATES

CAS Registry/EC Number

0 (Anti-Infective Agents); 0 (Fatty Acids, Unsaturated); 0 (Mouthwashes); 107-43-7 (Betaine); 86903-77-7 (C 31G)

Record 11 from database: MEDLINE
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Title

Clinical study of a C31G containing mouthrinse: effect on salivary microorganisms.

Author

Corner AM; Brightman VJ; Cooper S; Yankell SL; Malamud D

Address

University of Pennsylvania School of Dental Medicine.

Source

J Clin Dent, 1990 Fall, 2:2, 34-8

Abstract

In vitro studies have demonstrated the antiplaque properties of C31G, a potent broad spectrum antimicrobial agent consisting of an equimolar mixture of alkyl dimethyl glycine and alkyl dimethyl amine oxide, buffered with citric acid. In this initial clinical study, C31G at concentrations of 0.05%, 0.1%, 0.2% and 0.5%. Listerine, and placebo were tested in a complete crossover design. Twelve subjects were evaluated, with a minimum of 2 days between treatments. Parameters monitored were salivary bacterial counts and saliva glycolysis. The 0.5% and 0.2% C31G mouthrinses significantly reduced total bacterial counts in saliva samples obtained up to and including three hours after rinsing, compared with counts obtained prerinsing or after placebo rinsing. Both 0.5%, and 0.2% C31G significantly inhibited glycolysis of salivary bacteria for up to 6 hours postrinsing, compared with pH values obtained prerinsing. 0.1% and 0.05% C31G exhibited little or no effect in either assay. Listerine showed a significant reduction in bacterial counts for up to 1 hour postrinsing, compared with prerinse counts, but the effect was less sustained. Listerine showed no significant inhibition of glycolysis at any time point. No tooth staining or altered taste sensation was noted with either product.

Language of Publication

English

Unique Identifier

91214535

MeSH Heading (Major)

Anti-Infective Agents|*AD/PD; Betaine|*AA/AD/PD; Dental Plaque|*PC; Fatty Acids, Unsaturated|*AD/PD; Mouthwashes|*AD/PD; Saliva|*MI; Streptococcus|*DE

MeSH Heading

Adult; Analysis of Variance; Bacteria|DE; Comparative Study; Drug Combinations; Glycolysis|DE; Human; Salicylates|AD/PD; Terpenes|AD/PD

Publication Type

CLINICAL TRIAL; CONTROLLED CLINICAL TRIAL; JOURNAL ARTICLE

ISSN

0895-8831

Country of Publication

UNITED STATES

CAS Registry/EC Number

0 (Anti-Infective Agents); 0 (Drug Combinations); 0 (Fatty Acids, Unsaturated); 0 (Mouthwashes); 0 (Salicylates); 0 (Terpenes); 107-43-7 (Betaine); 51273-66-6 (Listerine); 86903-77-7 (C 31G)

Record 12 from database: MEDLINE
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Title

Inositol glycan phosphate derived from human erythrocyte acetylcholinesterase glycolipid anchor and inositol cyclic 1,2-phosphate antagonize glucagon activation of glycogen phosphorylase.

Author

Deeg MA; Brass EP; Rosenberry TL

Address

Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-4965.

Source

Diabetes, 1993 Sep, 42:9, 1318-23

Abstract

In this study we examine the hypothesis that an inositol glycan phosphate can act similarly to insulin on intact cells. The inositol glycan phosphate used in this study (glycan alpha) was isolated previously from the glycoinositol phospholipid anchor of human erythrocyte acetylcholinesterase and was shown to have the structure glycine-ethanolamine-PO4-Man-Man-(N,N-dimethylethanolamine-PO4)Man- (N,N-dimethyl)GlcN-inositol-PO4. The cellular response investigated was the glucagon-stimulated activation of glycogen phosphorylase in rat hepatocytes. When hepatocytes were incubated with 20 nM glucagon for 4 min, the ratio of phosphorylase a activity to total phosphorylase increased from a basal value of 0.49 +/- 0.02 to 0.82 +/- 0.03 (mean +/- SE, n = 15). Inclusion of either 100 nM insulin or 3-10 microM glycan alpha during the glucagon incubation significantly decreased the glucagon-stimulated activity ratio to 0.74 +/- 0.03 for either agent. Furthermore, hepatocyte preparations differed in their response to insulin and were divided into insulin-responsive and -resistant groups. Glycan alpha had a significant effect only in the insulin-responsive group for which the observed activity ratio for 10 microM glycan alpha plus glucagon (0.68 +/- 0.05) compared closely with that for insulin plus glucagon (0.70 +/- 0.04). For the insulin-resistant group, the activity ratio in the presence of 10 microM glycan alpha was 0.81 +/- 0.03, unchanged from the control with glucagon alone. Because glycan alpha contains an inositol phosphate group, the effect of inositol cyclic 1,2-phosphate on the glucagon-stimulated activity ratio was determined.(ABSTRACT TRUNCATED AT 250 WORDS)

Language of Publication

English

Unique Identifier

93351765

MeSH Heading (Major)

Acetylcholinesterase|*CH; Erythrocytes|*EN; Glycogen Phosphorylase|*ME; Glycosylphosphatidylinositols|*CH; Inositol Phosphates|IP/*PH

MeSH Heading

Animal; Enzyme Activation|DE; Human; Liver|CY; Male; Rats; Rats, Sprague-Dawley; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0012-1797

Country of Publication

UNITED STATES

CAS Registry/EC Number

EC 2.4.1.1 (Glycogen Phosphorylase); EC 3.1.1.7 (Acetylcholinesterase); 0 (Glycosylphosphatidylinositols); 0 (Inositol Phosphates); 43119-57-9 (inositol cyclic phosphate)

Record 13 from database: MEDLINE
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Title

Effect of insulin on system A amino acid transport in human skeletal muscle.

Author

Bonadonna RC; Saccomani MP; Cobelli C; DeFronzo RA

Address

Metabolism Unit, University of Pisa, Italy.

Source

J Clin Invest, 1993 Feb, 91:2, 514-21

Abstract

Transmembrane transport of neutral amino acids in skeletal muscle is mediated by at least four different systems (system A, ASC, L, and Nm), and may be an important target for insulin's effects on amino acid and protein metabolism. We have measured net amino acid exchanges and fractional rates of inward (k(in), min-1) and outward (kout, min-1) transmembrane transport of 2-methylaminoisobutyric acid (MeAIB, a nonmetabolizable amino acid analogue, specific for system A amino acid transport) in forearm deep tissues (skeletal muscle), by combining the forearm perfusion technique and a novel dual tracer ([1-H3]-D-mannitol and 2-[1-14C]-methylaminoisobutyric acid) approach for measuring in vivo the activity of system A amino acid transport. Seven healthy lean subjects were studied. After a baseline period, insulin was infused into the brachial artery to achieve local physiologic hyperinsulinemia (76 +/- 8 microU/ml vs 6.4 +/- 1.6 microU/ml in the basal period, P < 0.01) without affecting systemic hormone and substrate concentrations. Insulin switched forearm amino acid exchange from a net output (-2,630 +/- 1,100 nmol/min per kig of forearm tissue) to a net uptake (1,610 +/- 600 nmol/min per kg, P < 0.01 vs baseline). Phenylalanine and tyrosine balances simultaneously shifted from a net output (-146 +/- 47 and -173 +/- 34 nmol/min per kg, respectively) to a zero balance (16.3 +/- 51 for phenylalanine and 15.5 +/- 14.3 nmol/min per kg for tyrosine, P < 0.01 vs baseline for both), showing that protein synthesis and breakdown were in equilibrium during hyperinsulinemia. Net negative balances of alanine, methionine, glycine, threonine and asparagine (typical substrates for system A amino acid transport) also were decreased by insulin, whereas serine (another substrate for system A transport) shifted from a zero balance to net uptake. Insulin increased k(in) of MeAIB from a basal value of 11.8.10(-2) +/- 1.7.10(-2).min-1 to 13.7.10(-2) +/- 2.2.10(-2).min-1 (P < 0.02 vs the postabsorptive value), whereas kout was unchanged. We conclude that physiologic hyperinsulinemia stimulates the activity of system A amino acid transport in human skeletal muscle, and that this effect may play a role in determining the overall concomitant response of muscle amino acid/protein metabolism to insulin.

Language of Publication

English

Unique Identifier

93163344

MeSH Heading (Major)

Amino Acids|*ME; Insulin|*PD; Muscles|*ME

MeSH Heading

beta-Alanine|AA/ME; Adult; Biological Transport|DE; Female; Forearm; Human; Male; Muscle Proteins|ME; Potassium|ME; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0021-9738

Country of Publication

UNITED STATES

CAS Registry/EC Number

0 (Amino Acids); 0 (Muscle Proteins); 107-95-9 (beta-Alanine); 11061-68-0 (Insulin); 19036-43-2 (2,2-dimethyl-beta-alanine); 7440-09-7 (Potassium)

Record 14 from database: MEDLINE
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Title

An approach towards understanding the genesis of sunlight-induced skin cancer.

Author

Chatterjee SN; Agarwal S; Bose B

Address

Biophysics Division, Saha Institute of Nuclear Physics, Calcutta.

Source

Indian J Biochem Biophys, 1990 Aug, 27:4, 254-63

Abstract

The molecular basis of the sunlight-induced skin carcinogenesis has been elucidated. Of the two ultraviolet components of sunlight that reach the earth's surface the UV-B is known to be carcinogenic but the mode of action of UV-A, the predominant component of sunlight, is ill understood. Using the liposomes as a model system, it has been shown here that UV-A causes dose-dependent lipid peroxidation as estimated by measurements of conjugated dienes, lipid hydroperoxides, malondialdehydes and the fluorescent adducts (Schiff bases) produced by the reaction of MDA with glycine. Direct exposure to sunlight has also been shown to cause dose-dependent lipid peroxidation. The UV-A induced lipid peroxidation has also been shown to be dependent on dose rate. While the sodium formate, dimethyl sulphoxide, superoxide dismutase and EDTA do not have any significant effect, sodium azide, histidine, beta-carotene and dimethylfuran were shown to inhibit significantly the UV-A induced lipid peroxidation, thereby providing significant evidence of the involvement of singlet oxygen (1O2) as the initiating agent. The use of D2O in place of H2O as the liposome dispersing medium enhanced to great extent the UV-A induced lipid peroxidation, thereby lending additional support to the finding that singlet oxygen was the initiating agent. The possible mode of formation of 1O2 on exposure to UV-A was discussed. This study also highlighted the role of environmental factors on the sunlight-induced cutaneous damage. Finally, the relation between lipid peroxidation, DNA damage and carcinogenesis has been discussed in a way to suggest the possible link between sunlight exposure and causation of skin cancer.

Language of Publication

English

Unique Identifier

91139161

MeSH Heading (Major)

Skin Neoplasms|*ET; Sunlight|*AE

MeSH Heading

Human; Lipid Peroxidation|RE; Liposomes; Models, Biological; Neoplasms, Radiation-Induced|ET; Ultraviolet Rays|AE

Publication Type

JOURNAL ARTICLE

ISSN

0301-1208

Country of Publication

INDIA

CAS Registry/EC Number

0 (Liposomes)

Record 15 from database: MEDLINE
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Title

Effects of iron chelates on the transferrin-free culture of rat dermal fibroblasts through active oxygen generation.

Author

Yabe N; Matsui H

Address

Department of Hygiene, Dokkyo University School of Medicine, Tochigi, Japan.

Source

In Vitro Cell Dev Biol Anim, 1997 Jul, 33:7, 527-35

Abstract

Effects of nonchelating and chelating agents at 10 mM on the serum-free culture of rat dermal fibroblasts were investigated. A strong iron-chelating agent, iminodiacetic acid (IDA), and a weak one, dihydroxyethylglycine (DHEG), decreased iron permeation into preconfluent fibroblasts. A weak iron-chelating agent, glycylglycine (GG), a nonchelating agent, N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid (HEPES), and human apotransferrin (10 micrograms/ml) increased the permeation with time. Iron may be essential for survival of fibroblasts because subconfluent fibroblasts exposed to 100 microM FeSO4 in combination with transferrin, HEPES, or GG significantly decreased to release lactate dehydrogenase into the medium. Superoxide dismutase and dimethyl sulfoxide blocked the enzyme release, suggesting that superoxide and hydroxyl radical induce cellular damage but hydrogen peroxide (H2O2) generated by superoxide dismutation does not. GG significantly reduced H2O2 cytotoxicity. DHEG acted as a potent promoter of the iron-stimulated cellular damage if ascorbate or H2O2 was added to the medium. FeSO4 and FeCl3 (50 to 100 microM) individually combined with IDA maximally promoted fibroblast proliferation. Ascorbate increased formation of thiobarbituric acid-reactive substances from deoxyribose in the medium supplemented with FeSO4 and either IDA or DHEG. Conversely, ascorbate decreased the formation in the medium with FeSO4 and with or without other agents. Fibroblast proliferation may thus be stimulated through the active oxygen generation mediated by a redox-cycling between Fe3+ and Fe2+, which are dissolved in the medium at a high concentration, rather than through delivery of iron into the cells.

Language of Publication

English

Unique Identifier

97427281

MeSH Heading (Major)

Fibroblasts|*DE/*ME; Iron Chelating Agents|*PD; Oxygen|*ME; Transferrin|PD/*PH

MeSH Heading

Animal; Antioxidants|PD; Apoproteins|PD; Cell Division|DE; Cells, Cultured; Dimethyl Sulfoxide|PD; Ferrous Compounds|PD; Glycine|AA/PD; Glycylglycine|PD; Human; Hydrogen Peroxide|ME/PD; Imino Acids|PD; Lactate Dehydrogenase|SE; Male; Rats; Rats, Wistar; Superoxide Dismutase|PD; Thiobarbituric Acid Reactive Substances|ME

Publication Type

JOURNAL ARTICLE

ISSN

1071-2690

Country of Publication

UNITED STATES

Record 16 from database: MEDLINE
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Title

Assessment of the anti-microbial agent C31G as a spermicide: comparison with nonoxynol-9.

Author

Thompson KA; Malamud D; Storey BT

Address

Department of Obstetrics and Gynecology, School of Medicine, University of Pennsylvania, Philadelphia, USA.

Source

Contraception, 1996 May, 53:5, 313-8

Abstract

The broad-spectrum anti-microbial agent, C31G, containing an equimolar mixture of n-dodecyl-dimethylamine-N-oxide (C12-N-O) and N-(n-dodecyl), N-dimethyl-glycine (C12-betaine), was tested for spermicidal activity in comparison with the currently used spermicide, nonoxynol-9 (N-9). The rate of sperm cell permeabilization by the spermicides, as assayed with the fluorescent probe, TO-PRO-1, increased as the cube of the C31G concentration, while the rate increase was linear with N-9 concentration. At 0.04%, the rate of sperm cell permeabilization with both spermicides is at the limit of rapid measurement. C31G diffuses through cervical mucus at a more rapid rate than does N-9. C31G has long been known to aid wound healing and reduce inflammation, whereas N-9 has been reported to induce vaginal irritation. C31G would, thus, seem to have the spermicidal efficacy, the broad range of anti-microbial activity, and the lack of inflammatory activity that is sought in the ideal vaginal spermicide.

Language of Publication

English

Unique Identifier

96315389

MeSH Heading (Major)

Anti-Infective Agents|*; Betaine|*AA/AE/ME; Fatty Acids, Unsaturated|*/AE/ME; Nonoxynol|*/AE; Spermatocidal Agents|*

MeSH Heading

Adult; Cell Membrane Permeability|DE; Cervix Mucus|ME; Comparative Study; Fluorescent Dyes; Human; Male; Spermatozoa|DE; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0010-7824

Country of Publication

UNITED STATES

Record 17 from database: MEDLINE
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Title

Design, synthesis, and evaluation of mitomycin-tethered phosphorothioate oligodeoxynucleotides.

Author

Huh N; Rege AA; Yoo B; Kogan TP; Kohn H

Address

Department of Chemistry, University of Houston, Texas 77204-5641, USA.

Source

Bioconjug Chem, 1996 Nov, 7:6, 659-69

Abstract

Mitomycin C (1) is the prototypical bioreductive alkylating agent. Studies have shown that mitomycin C and its derivatives selectively alkylate guanine residues within di- and trinucleotide DNA sequences. This investigation sought to improve the selective DNA bonding properties of the mitomycins by coupling them with antisense oligodeoxynucleotides. Two procedures were developed that allowed the attachment of a phosphorothioate oligodeoxynucleotide containing a hexylamino spacer at the 5' terminus with a C(10)-activated mitomycin. In the first procedure, decarbamoylation of 1 (NaOCH3/ benzene) afforded 10-decarbamoylmitomycin C (10), which was treated with either dimethyl sulfate or methylthiochloroformate and base to yield 10-decarbamoylporfiromycin (11) and N(1a)-[(methylthio)-carbonyl]-10-decarbamoylmitomycin C (12), respectively. Activation of the C(10) site in 11 and 12 with 1,1'-carbonyldiimidazole or with 1,1'-thiocarbonyldiimidazole provided the N(1a)-substituted mitomycin 10-decarbamoyl-10-O-carbonylimidazoles (5, 7) and 10-decarbamoyl-10-O-thiocarbonylimidazoles (6, 8), respectively. Compounds 5-8 were reacted with glycine methyl ester hydrochloride (17) and base in both methylene chloride and aqueous buffered solutions to determine the ease and efficiency in which these C(10)-activated mitomycin derivatives coupled to amines. It was found that 5-8 all reacted with 17 in methylene chloride to give the coupled products 18-21 but that improved amine coupling yields in water were observed for the 10-decarbamoyl-10-O-thiocarbonylimidazoles 6 and 8 as compared with the 10-decarbamoyl-10-O-carbonylimidazoles 5 and 7. This finding led to the coupling of the phosphorothioate oligodeoxynucleotide, H2N(CH2)6-P(S)(OH)-GGCCCCGTG-GTGGCTCCAT (22) to 8. Compound 22 complemented a 19-base sequence in the translation initiation region of the human A-raf-1 gene. Use of excess 8 (28 equiv) with 22 gave only a 36% yield of the coupled product 23, which proved difficult to separate from 22. In the second procedure, phosphorothioate oligodexynucleotides that contained a hexylamino spacer at the 5'termini were coupled to 10-des(carbamoyloxy)-10-isothiocyanatoporfiromycin (9). Compound 9 was prepared in four steps from 11. Mesylation (methanesulfonyl chloride/pyridine) of 11 gave the C(10) mesylate 13, which was then treated with NaN3 (dimethylformamide, 90 degrees C) to give 10-des(carbamoyloxy)-10-azidoporfiromycin (14). Catalytic reduction (PtO2, H2) of 14 in pyridine afforded C(10) amine 15. Treatment of 15 with di-2-pyridyl thionocarbonate provided the desired 10-des(carbamoyloxy)-10-isothiocyanatoporfiromycin (9). Compound 9 readily coupled with 17 and base in both methylene chloride and aqueous buffered solutions to give 25. Use of the 5'hexylaminophosphorothioate oligodeoxynucleotides 32-35 in place of 17 gave the conjugated adducts 28-31, respectively, in a 12% to near-quantitative yield. The products were purified by semipreparative HPLC. Antisense agents 28-31 were designed to target a 30-base-long region from the coding region of the human FGFR1 gene. One adduct, 29, reduced the number of FGFR1 receptors in human aortic smooth cells for bFGF on the cell surface, which suggested down-regulation of FGFR1 gene expression. Further, 29 inhibited cultured human aortic smooth muscle cell proliferation and was less cytotoxic than porfiromycin (2). The biological assay data suggest that the phosphorothioate oligodexynucleotide porfiromycin conjugates may be more target selective and less toxic than either mitomycin or porfiromycin and thus be promising therapeutic agents.

Language of Publication

English

Unique Identifier

97107759

MeSH Heading (Major)

Mitomycin C|*AA/CH; Oligonucleotides|*CS; Organothiophosphorus Compounds|CH/*CS; Porfiromycin|*AA/CH/PD

MeSH Heading

Chromatography, High Pressure Liquid; Human; Muscle, Smooth, Vascular|DE/ME; Nuclear Magnetic Resonance; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

1043-1802

Country of Publication

UNITED STATES

Record 18 from database: MEDLINE
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Title

Inhibition of redox cycling of methoxatin (PQQ), and of superoxide release by phagocytic white cells.

Author

Bishop A; Paz MA; Gallop PM; Karnovsky ML

Address

Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.

Source

Free Radic Biol Med, 1995 Mar, 18:3, 617-20

Abstract

The iodonium compounds diphenyleneiodonium and diphenyliodonium, and the amine compounds, 4,5-dimethyl phenylene diamine, N,N-dimethyl 1,4-phenylene diamine, 1,2-diamino-4,5-methyleneoxybenzene, and aminomalononitrile inhibit methoxatin's (PQQ's) redox activity in vitro, that is, the methoxatin-coupled oxidation of glycine and reduction of nitroblue tetrazolium to formazan. The compounds mentioned above also inhibit phorbol myristate acetate (PMA) stimulated superoxide release by phagocytic white cells--determined mainly as the superoxide dismutase sensitive reduction of ferricytochrome C. Related compounds, 3,4-diaminopyridine and 4-dimethylamino-benzylamine, did not inhibit redox activity of PQQ in vitro, nor did they inhibit PMA stimulated superoxide production in monocytes or neutrophils. Thus, there is a correlation between an agent's ability to inhibit PQQ redox cycling and its ability to inhibit superoxide release by phagocytes. The findings are a further indication that PQQ is involved in the respiratory burst of phagocytic cells.

Language of Publication

English

Unique Identifier

97255925

MeSH Heading (Major)

Coenzymes|*ME; Phagocytes|DE/*ME; Quinolones|*ME; Superoxides|*ME

MeSH Heading

Amines|PD; Animal; Biphenyl Compounds|PD; Free Radicals|ME; Guinea Pigs; Human; In Vitro; Onium Compounds|PD; Oxidation-Reduction; Respiratory Burst; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0891-5849

Country of Publication

UNITED STATES

Record 19 from database: MEDLINE
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Title

Inositol glycan phosphate derived from human erythrocyte acetylcholinesterase glycolipid anchor and inositol cyclic 1,2-phosphate antagonize glucagon activation of glycogen phosphorylase.

Author

Deeg MA; Brass EP; Rosenberry TL

Address

Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-4965.

Source

Diabetes, 1993 Sep, 42:9, 1318-23

Abstract

In this study we examine the hypothesis that an inositol glycan phosphate can act similarly to insulin on intact cells. The inositol glycan phosphate used in this study (glycan alpha) was isolated previously from the glycoinositol phospholipid anchor of human erythrocyte acetylcholinesterase and was shown to have the structure glycine-ethanolamine-PO4-Man-Man-(N,N-dimethylethanolamine-PO4)Man- (N,N-dimethyl)GlcN-inositol-PO4. The cellular response investigated was the glucagon-stimulated activation of glycogen phosphorylase in rat hepatocytes. When hepatocytes were incubated with 20 nM glucagon for 4 min, the ratio of phosphorylase a activity to total phosphorylase increased from a basal value of 0.49 +/- 0.02 to 0.82 +/- 0.03 (mean +/- SE, n = 15). Inclusion of either 100 nM insulin or 3-10 microM glycan alpha during the glucagon incubation significantly decreased the glucagon-stimulated activity ratio to 0.74 +/- 0.03 for either agent. Furthermore, hepatocyte preparations differed in their response to insulin and were divided into insulin-responsive and -resistant groups. Glycan alpha had a significant effect only in the insulin-responsive group for which the observed activity ratio for 10 microM glycan alpha plus glucagon (0.68 +/- 0.05) compared closely with that for insulin plus glucagon (0.70 +/- 0.04). For the insulin-resistant group, the activity ratio in the presence of 10 microM glycan alpha was 0.81 +/- 0.03, unchanged from the control with glucagon alone. Because glycan alpha contains an inositol phosphate group, the effect of inositol cyclic 1,2-phosphate on the glucagon-stimulated activity ratio was determined.(ABSTRACT TRUNCATED AT 250 WORDS)

Language of Publication

English

Unique Identifier

93351765

MeSH Heading (Major)

Acetylcholinesterase|*CH; Erythrocytes|*EN; Glycogen Phosphorylase|*ME; Glycosylphosphatidylinositols|*CH; Inositol Phosphates|IP/*PH

MeSH Heading

Animal; Enzyme Activation|DE; Human; Liver|CY; Male; Rats; Rats, Sprague-Dawley; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0012-1797

Country of Publication

UNITED STATES

CAS Registry/EC Number

EC 2.4.1.1 (Glycogen Phosphorylase); EC 3.1.1.7 (Acetylcholinesterase); 0 (Glycosylphosphatidylinositols); 0 (Inositol Phosphates); 43119-57-9 (inositol cyclic phosphate)

Record 20 from database: MEDLINE
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Title

Inhibition of human leukocyte elastase by N-substituted tripeptide trifluoromethyl ketones.

Author

Skiles JW; Fuchs V; Chow G; Skoog M

Address

Department of Biochemistry, Boehringer Ingelheim Pharmaceuticals Inc., Ridgefield, CT 06877.

Source

Res Commun Chem Pathol Pharmacol, 1990 Jun, 68:3, 365-74

Abstract

Several tripeptide trifluoromethyl ketones containing non-naturally occurring N-substituted glycine residues at the P2-position are effective human leukocyte elastase (HLE) inhibitors in vitro and possess IC50 values in the submicromolar range. Deletion of the amino acid at the P3-subsite region affords inactive compounds. The trifluoromethyl ketone derivative of valine is the preferred residue at the P1-position; whereas, the corresponding glycine or alpha, alpha-dimethyl glycine analogs result in inactive compounds.

Language of Publication

English

Unique Identifier

90349916

MeSH Heading (Major)

Ketones|*PD; Leukocytes|*EN; Oligopeptides|*PD; Pancreatopeptidase|*AI

MeSH Heading

Amino Acid Sequence; Binding Sites; Human; In Vitro; Molecular Sequence Data; Structure-Activity Relationship; Substrate Specificity

Publication Type

JOURNAL ARTICLE

ISSN

0034-5164

Country of Publication

UNITED STATES

CAS Registry/EC Number

EC 3.4.21.36 (Pancreatopeptidase); 0 (Ketones); 0 (Oligopeptides)

Record 21 from database: MEDLINE
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Title

NADPH-cytochrome c reductase from human neutrophil membranes: purification, characterization and localization.

Author

Nisimoto Y; Otsuka Murakami H; Iwata S

Address

Department of Biochemistry, Aichi Medical University, Japan.

Source

Biochem J, 1994 Feb, 297 ( Pt 3):, 585-93

Abstract

Neutrophil-membrane-associated NADPH-cytochrome c reductase and cytochrome b558 were separately eluted and highly purified by a combination of ion-exchange Sepharose, N-amino-octylagarose, 2',5'-ADP-Sepharose and heparin-Sepharose column chromatographies. The purified cytochrome c reductase with an apparent molecular mass of 68 kDa contained FMN and FAD (FMN/FAD approx. 1). Cytochrome b558 prepared in the presence of phospholipids and FAD showed marked O2-.-producing activity (Vmax., 8.53 mumol of O2-./min per mg of cytochrome; Km for NADPH 58.8 microM) in a cell-free assay system consisting of cytosol, arachidonate and GTP[S]. However, when it was obtained without FAD added to the purification process, it had negligible FAD and little or no O2-.-forming activity in the reconstituted system. The NADPH oxidase activity was not markedly stimulated on incubation of the purified reductase with either flavinated or flavin-depleted cytochrome b558 in the cell-free system, suggesting that the reductase is not likely to be involved in neutrophil O2-. generation. The purified reductase cross-reacted with polyclonal antibodies against both hepatic NADPH-cytochrome P-450 reductase and a synthetic peptide, ILVGPGTGIAPFRSF, which indicates residues 529-543 located in the glycine-rich NADPH-binding domain of the P-450 reductase, but cytochrome b558 did not produce any immunoreactive bands to these antibodies. These antibodies also produced a positive reaction with a 76 kDa protein from dimethyl sulphoxide-induced HL-60-cell microsomes. After solubilization of the microsomal membranes, the 76 kDa protein was readily converted into a partially proteolysed form (68 kDa) even in the presence of antiproteases. In addition, the microsomal fraction shows a CO difference spectrum with a peak at about 454 nm and a trough at 476 nm in the presence of dithionite, indicating the presence of a cytochrome P-450-like haemoprotein.

Language of Publication

English

Unique Identifier

94153334

MeSH Heading (Major)

Neutrophils|*EN; NADPH-Ferrihemoprotein Reductase|*IP/ME

MeSH Heading

Amino Acid Sequence; Blotting, Western; Carbon Monoxide; Catalysis; Cell Membrane|EN; Chromatography, Affinity; Chromatography, Gel; Chromatography, Ion Exchange; Cytochrome b|IP/ME; Electrophoresis, Polyacrylamide Gel; Human; Microsomes|EN; Molecular Sequence Data

Publication Type

JOURNAL ARTICLE

ISSN

0264-6021

Country of Publication

ENGLAND

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