The reports which follow are taken from a search program called Healthgate, which you can visit at no charge. You can even look at very brief descriptions of any of the 7,000,000 different scientific studies which are included in this database. If you want to examine an "abstract" of one of these studies, you will have to "sign up" and give them a credit card number. Then, when you search, you can look at these abstracts at a cost of $ .25 each. You can get copies of the entire study mailed to you, usually for about $25.00.

These reports are generally considered to be the most authoritative sources of scientific information about diseases, drugs, various substances, etc.

When you search for the word "cysteine" in the Medline database, you find 9,521 items, just since 1992. Since that is so many, you can narrow your search by entering "cysteine and 'heart disease' ", and then you get 23 items. There is actually another search term used to do the research for cysteine as used in Life Glow and Super Life Glow. Read more about that under Cysteine or N Acetyl Cysteine.

I've selected just six of those, and shown them below:

Record 1 from database: MEDLINE

Title

Identification of polymorphic sites of the human bradykinin B2 receptor gene.

Author

Braun A; Kammerer S; BÂohme E; MÂuller B; Roscher AA

Address

Children's Hospital, Department of Clinical Chemistry and Biochemistry, University of Munich, Germany.

Source

Biochem Biophys Res Commun, 1995 Jun 6, 211:1, 234-40

Abstract

The characterization of the genomic organization of the B2 bradykinin receptor gene enabled us to systematically search for polymorphic markers in this gene in a South German cohort (N = 179). We identified at least three polymorphic sites in each of the three exons existing: (i) in exon 1 next to the promoter region, a tandem repeat polymorphism consists of three common alleles, (ii) in exon 2 at nucleotide position 181 of the cDNA a C to T transition leads to an aminoacid substitution from arginine to cysteine in the receptor protein at position 14 (R14C), and (iii) a more complex repeat polymorphism, located in the 3' not-translated region of exon 3, comprises at least two common alleles and two rare variants. These new genetic markers provide valuable tools to elucidate a potential role of a hereditary dysfunction of the B2 bradykinin receptor gene in disorders such as hypertension or ischemic heart disease.

Language of Publication

LA=ENG

Unique Identifier

95298028 GENBANK/X86164 GENBANK/X86165 GENBANK/X86166 GENBANK/X86167 GENBANK/X86168 GENBANK/X86169 GENBANK/X86170 GENBANK/X86171 GENBANK/X86180

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MeSH Heading (Major)

Hominidae|*GE; Polymorphism (Genetics)|*; Receptors, Bradykinin|*GE

MeSH Heading

Alleles; Animal; Base Sequence; Cohort Studies; Comparative Study; DNA Primers; Exons; Gene Frequency; Germany; Human; Molecular Sequence Data; Polymerase Chain Reaction; Repetitive Sequences, Nucleic Acid; Support, Non-U.S. Gov't

Publication Type

JOURNAL ARTICLE

ISSN

0006-291X

Country of Publication

UNITED STATES

CAS Registry/EC Number

0 (bradykinin B2 receptor); 0 (DNA Primers); 0 (Receptors, Bradykinin)

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Record 2 from database: MEDLINE Order full text for this document Title

Mutations of the microsomal triglyceride-transfer-protein gene in abetalipoproteinemia.

Author

Narcisi TM; Shoulders CC; Chester SA; Read J; Brett DJ; Harrison GB; Grantham TT; Fox MF; Povey S; de Bruin TW; et al

Address

MRC Molecular Medicine Group, Royal Postgraduate Medical School, Hammersmith Hospital, London, United Kingdom.

Source

Am J Hum Genet, 1995 Dec, 57:6, 1298-310

Abstract

Elevated plasma levels of apolipoprotein B (apoB)-containing lipoproteins constitute a major risk factor for the development of coronary heart disease. In the rare recessively inherited disorder abetalipoproteinemia (ABL) the production of apoB-containing lipoproteins is abolished, despite no abnormality of the apoB gene. In the current study we have characterized the gene encoding a microsomal triglyceride-transfer protein (MTP), localized to chromosome 4q22-24, and have identified a mutation of the MTP gene in both alleles of all individuals in a cohort of eight patients with classical ABL. Each mutant allele is predicted to encode a truncated form of MTP with a variable number of aberrant amino acids at its C-terminal end. Expression of genetically engineered forms of MTP in Cos-1 cells indicates that the C-terminal portion of MTP is necessary for triglyceride-transfer activity. Deletion of 20 amino acids from the carboxyl terminus of the 894-amino-acid protein and a missense mutation of cysteine 878 to serine both abolished activity. These results establish that defects of the MTP gene are the predominant, if not sole, cause of hereditary ABL and that an intact carboxyl terminus is necessary for activity.

Language of Publication

LA=ENG

Unique Identifier

96065017 GENBANK/X91148

MeSH Heading (Major)

Abetalipoproteinemia|*GE; Carrier Proteins|*GE; Mutation|*

MeSH Heading

Adult; Base Sequence; Chromosome Mapping; Female; Human; Infant; Male; Microsomes|ME; Molecular Sequence Data; Polymerase Chain Reaction; Polymorphism (Genetics)

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Publication Type

JOURNAL ARTICLE

ISSN

0002-9297

Country of Publication

UNITED STATES

CAS Registry/EC Number

0 (cholesterol ester transfer proteins); 0 (Carrier Proteins)

Record 3 from database: MEDLINE

Title

Heterozygosity for apolipoprotein E-4Philadelphia(Glu13----Lys, Arg145----Cys) is associated with incomplete dominance of type III hyperlipoproteinemia.

Author

Lohse P; Rader DJ; Brewer HB Jr

Address

Molecular Disease Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.

Source

J Biol Chem, 1992 Jul 5, 267:19, 13642-6

Abstract

Apolipoprotein (apo) E-4Philadelphia is a double mutant of apoE in which residue 13 of the mature protein, glutamic acid (GAG), is replaced by lysine (AAG) and amino acid 145, arginine (CGT), is converted to cysteine (TGT). These mutations result in two restriction fragment length polymorphisms for the enzymes AvaI and BbvI, a smaller apparent molecular weight of apoE-4Philadelphia on sodium dodecyl polyacrylamide gels, and severe type III hyperlipoproteinemia (HLP) in a 24-year-old homozygous female (Lohse, P., Mann, W. A., Stein, E. A., and Brewer, H. B., Jr. (1991) J. Biol. Chem. 266, 10479-10484). In the current study, we have extended our analysis to include nine additional family members of the Philadelphia kindred spanning four generations. DNA and protein analysis demonstrated that the originally described propositus is a true homozygote for the epsilon-4Philadelphia allele and that six of the nine family members are heterozygous for the mutated allele and the normal epsilon-3 allele or, in one case, the epsilon-4 allele. Heterozygosity for apoE-4Philadelphia leads to the expression of a moderate form of type III HLP without clinical manifestations. These results are consistent with a dominant mode of inheritance of this dyslipoproteinemia. The simultaneous presence of unaffected individuals, heterozygotes, and a homozygote in the Philadelphia kindred makes it possible for the first time to demonstrate that the mutant apoE exhibits an incomplete or partial dominance of type III HLP. Heterozygosity for the normal epsilon-3 allele appears to have an influence on the expression of type III HLP, resulting in a phenotype intermediate between that of the two homozygous states.

Language of Publication

LA=ENG

Unique Identifier

92317096

MeSH Heading (Major)

Apolipoproteins E|*GE/ME; Genes, Dominant|*; Heterozygote|*; Hyperlipoproteinemia Type III|*GE

MeSH Heading

Adolescence; Adult; Aged; Arginine|GE; Child; Cysteine|GE; DNA; Electrophoresis, Polyacrylamide Gel; Female; Glutamates|GE; Homozygote; Human; Lysine|GE; Male; Middle Age; Pedigree; Phenotype; Polymerase Chain Reaction; Polymorphism, Restriction Fragment Length; Support, Non-U.S. Gov't

 

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Publication Type

JOURNAL ARTICLE

ISSN

0021-9258

Country of Publication

UNITED STATES

CAS Registry/EC Number

0 (apolipoprotein E-3); 0 (apolipoprotein E-4 Philadelphia); 0 (Apolipoproteins E); 0 (Glutamates); 4371-52-2 (Cysteine); 56-86-0 (Glutamic Acid); 56-87-1 (Lysine); 7004-12-8 (Arginine); 9007-49-2 (DNA)

Record 4 from database: MEDLINE

Title

Molecular cloning of the amino-terminal region of a rat MUC 2 mucin gene homologue. Evidence for expression in both intestine and airway.

Author

Ohmori H; Dohrman AF; Gallup M; Tsuda T; Kai H; Gum JR Jr; Kim YS; Basbaum CB

Address

Department of Anatomy, University of California, San Francisco 94143.

Source

J Biol Chem, 1994 Jul 8, 269:27, 17833-40

Abstract

To obtain cDNAs for analysis of mucin gene transcription in rat models of human disease, we screened a rat intestinal cDNA library in lambda ZAPII using an upstream non-tandem repeat cDNA fragment of the human MUC 2 gene (Gum, J., Hicks, J., Toribara, N., Rothe, E., Lagace, R., and Y., K. (1992) J. Biol. Chem. 267, 21375-21383). Three cDNAs, 1-1, 8-1, and 21-1, were isolated. A translation start site was found in cDNA 21-1. Combined nucleotide sequence for the three cDNAs contained an open reading frame spanning 4546 base pairs. This amino-terminal sequence contains a non-tandem repeat domain enriched in cysteine (1391 residues) followed by an irregular tandem repeat domain (122 residues). Identity with the human gene is about 80% in the non-tandem repeat domain and about 38% in the irregular tandem repeat domain. Primer extension and S1 nuclease protection analysis indicate a transcription start site at 28 base pairs upstream of translation initiation. Northern analysis showed expression of cognate RNA in the intestine and airway but not heart and spleen. The cDNAs have been used to isolate the gene promoter, the structure of which should yield clues to the regulation of mucin expression in rat models of human disease.

Language of Publication

LA=ENG

Unique Identifier

94299489 GENBANK/U07615

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MeSH Heading (Major)

Intestines|*ME; Mucins|BI/CH/*GE; Trachea|*ME

MeSH Heading

Amino Acid Sequence; Animal; Base Sequence; Blotting, Northern; Cloning, Molecular; DNA; Human; In Situ Hybridization; Male; Molecular Sequence Data; Rats; Rats, Sprague-Dawley; Sequence Homology, Amino Acid; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.; Transcription, Genetic

 

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Publication Type

JOURNAL ARTICLE

ISSN

0021-9258

Country of Publication

UNITED STATES

CAS Registry/EC Number

0 (Muc 2 protein); 0 (Mucins); 9007-49-2 (DNA)

Record 5 from database: MEDLINE

Title

Effects of monocrotaline, a pyrrolizidine alkaloid, on glutathione metabolism in the rat.

Author

Yan CC; Huxtable RJ

Address

Department of Pharmacology, College of Medicine, University of Arizona, Tucson 85724, USA.

Source

Biochem Pharmacol, 1996 Feb 9, 51:3, 375-9

Abstract

Monocrotaline (MONO), a pyrrolizidine alkaloid, causes veno-occlusive disease of the liver, pulmonary arterial hypertension, and right ventricular hypertrophy. Toxicity is due to the hepatic formation of a pyrolic metabolite that can be detoxified by conjugation with glutathione (GSH). We have shown that the GSH content of the liver affects the quantity of the pyrrolic metabolite that is released from the liver. We have now examined whether MONO, in turn, affects GSH metabolism. Twenty-four hours after administration of MONO to rats (65 mg/kg, i.p.), the highest concentration of bound pyrrolic metabolites was found in the liver, followed by the lung and kidney. Heart and brain contained lower concentrations of these metabolites. Significantly higher levels of GSH were found in liver and lungs of MONO-treated rats than in saline-injected control animals. In the liver, activities of the following enzymes were elevated: gamma-glutamylcysteine synthetase, GSH synthetase, gamma-glutamyl transpeptidase, dipeptidase, and microsomal GSH transferase. The same changes were seen in the lung. In the heart, gamma-glutamyl transpeptidase activity was decreased markedly, and cytosolic GSH transferase activity was elevated. In the kidney, the activities of GSH synthetase, gamma-glutamyl transpeptidase, and cytosolic GSH transferase were increased. Our results establish a mutual interaction of MONO and sulfur metabolism. It appears that an early metabolic action of MONO is to modify sulfur amino acid metabolism, diverting cysteine metabolism from oxidation to taurine towards synthesis of GSH.

Language of Publication

LA=ENG

Unique Identifier

96152582

Unique Identifier

93096556

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