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rdf:type |
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lifeskim:mentions |
umls-concept:C0001675,
umls-concept:C0006556,
umls-concept:C0009015,
umls-concept:C0017262,
umls-concept:C0085180,
umls-concept:C0332325,
umls-concept:C0521457,
umls-concept:C0538775,
umls-concept:C0679058,
umls-concept:C1171362,
umls-concept:C1305923,
umls-concept:C1515670,
umls-concept:C1547699,
umls-concept:C1711351,
umls-concept:C1882726,
umls-concept:C2700640
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pubmed:issue |
32
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pubmed:dateCreated |
1994-9-6
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pubmed:databankReference |
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pubmed:abstractText |
Fetal rat liver possesses substantial levels of glutathione S-transferase (GST) activity toward aflatoxin B1-8,9-epoxide. The enzyme responsible for this activity is an Alpha-class GST heterodimer comprising Yc1 and Yc2 subunits. The cDNAs encoding these polypeptides have been cloned and shown to share approximately 91% identity over 920 base pairs, extending from nucleotide -23 to the AATAAA polyadenylation signal. GST Yc2Yc2 expressed in Escherichia coli was found to exhibit 150-fold greater activity toward aflatoxin B1-8,9-epoxide than GST Yc1Yc1. Comparison between the structures of Alpha-class GST suggests that tyrosine at residue 108 and/or aspartate at residue 208 is responsible for the high aflatoxin B1 detoxication capacity of Yc2. Immunoblotting and enzyme assays have shown that liver from adult female rats contains about 10-fold greater levels of Yc2 than is found in liver from adult male rats. This sex-specific expression of Yc2 in adult rat liver may contribute to the relative insensitivity of female rats to aflatoxin B1. Dietary administration of oltipraz, a synthetic antioxidant which protects against aflatoxin-hepatocarcinogenesis, serves as an inducer of GST Yc2.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
269
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20707-17
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8051171-Aflatoxin B1,
pubmed-meshheading:8051171-Amino Acid Sequence,
pubmed-meshheading:8051171-Animals,
pubmed-meshheading:8051171-Base Sequence,
pubmed-meshheading:8051171-Carcinogens,
pubmed-meshheading:8051171-Cloning, Molecular,
pubmed-meshheading:8051171-DNA, Complementary,
pubmed-meshheading:8051171-Drug Resistance,
pubmed-meshheading:8051171-Enzyme Induction,
pubmed-meshheading:8051171-Escherichia coli,
pubmed-meshheading:8051171-Female,
pubmed-meshheading:8051171-Glutathione Transferase,
pubmed-meshheading:8051171-Humans,
pubmed-meshheading:8051171-Liver,
pubmed-meshheading:8051171-Male,
pubmed-meshheading:8051171-Metabolic Detoxication, Drug,
pubmed-meshheading:8051171-Molecular Sequence Data,
pubmed-meshheading:8051171-Peptide Fragments,
pubmed-meshheading:8051171-Rats,
pubmed-meshheading:8051171-Rats, Inbred F344,
pubmed-meshheading:8051171-Sequence Homology, Amino Acid
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pubmed:year |
1994
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pubmed:articleTitle |
Cloning of cDNAs from fetal rat liver encoding glutathione S-transferase Yc polypeptides. The Yc2 subunit is expressed in adult rat liver resistant to the hepatocarcinogen aflatoxin B1.
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pubmed:affiliation |
Biomedical Research Centre, Ninewells Hospital and Medical School, University of Dundee, Scotland, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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