Data provider:

Icon data provider

The National Agricultural Library is one of four national libraries of the United States, with locations in Beltsville, Maryland and Washington, D.C. It houses one of the world's largest and most accessible agricultural information collections and serves as the nexus for a national network of state land-grant and U.S. Department of Agriculture field libraries. In fiscal year 2011 (Oct 2010 through Sept 2011) NAL delivered more than 100 million direct customer service transactions.

Journal Article

Journal Article

Regulation of CYP1A and CYP3A mRNAs by ascorbic acid in guinea pigs  [1997]

Mori, T.; Itoh, S.; Ohgiya, S.; Ishizaki, K.; et al.

Access the full text

In previous studies, we found that the ascorbic acid (AsA) deficiency caused changes in the amounts of the various forms of cytochrome P450 (P450) in liver microsomes from guinea pigs in a form-specific manner. Thus, the aim of this study was to clarify whether the changes seen in the protein contents of the various forms of P450 were associated with the levels of the expression of their mRNAs. Prior to determining the mRNA level, we isolated four cDNA clones, encoding CYP1A2, CYP3A14, CYP3A15, and CYP3A17, from guinea pig liver cDNA libraries to use them as probes in further experiments. The amino acid sequence of the guinea pig CYP1A2 showed identity ranging from 73 to 77% with those of other mammalian P450s. The amino acid sequences among guinea pig CYP3As had about 94% identities with each other. The AsA deficiency apparently decreased the expression of mRNA for CYP1A1 and CYP1A2. These results were in agreement with the decrease in the content of CYP1A1 and CYP1A2 proteins. The amount of P450 protein(s) immunochemically cross-reactive with antibodies to human CYP3A4 was likely unaffected while that of human CYP3A7 tended to be decreased by the AsA deficiency. It suggested that the expression of each CYP3A isozyme was regulated differently by AsA. In fact, the level of mRNA for CYP3A14 was unaffected by the AsA deficiency, while those for CYP3A15 and CYP3A17 were significantly decreased by the AsA deficiency, clearly indicating that the expression of e
ach isozyme within the CYP3A subfamily is differently regulated by AsA. These results support the idea that the transcription of P450 is regulated by AsA in guinea pigs

Access the full text


Bibliographic information

Journal Article
In AGRIS since:
Start Page:
End Page:
All titles:
" Regulation of CYP1A and CYP3A mRNAs by ascorbic acid in guinea pigs "
" references "

From the journal

Archives of biochemistry and biophysics (USA)

ISSN : 0003-9861