| Cloning and expression analysis of a new member of the cytochrome P450, CYP2A15 from the Chinese hamster, encoding testosterone 7alpha-hydroxylase. | |
| | |
MedLine Citation:
|
PMID: 10545214 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
We cloned a new cytochrome P450 cDNA encoding testosterone 7alpha-hydroxylase in the Chinese hamster, designated CYP2A15 which shares significant amino acid sequence homology with members of the CYP2A subfamily. The CYP2A15 cDNA was isolated by screening a liver cDNA library and the sequence contains an open reading frame of 1482 nucleotides encoding a polypeptide of 493 amino acids with a calculated molecular mass of 56,295 Da. This is flanked by a 5'-untranslated region of 2 bp and a 3' untranslated region of 191 bp including the poly(A) tail. We determined the catalytic activity of CYP2A15 using microsomes obtained by transient expression of its cDNA in transfected COS-7 cells. The heterologously expressed CYP2A15 was found to hydroxylate testosterone at position 7alpha in a reconstituted system. RT-PCR experiments revealed that the mRNA of CYP2A15 was expressed in liver, but not detected in kidney, lung, or small intestine. The expression of CYP2A15 mRNA was slightly induced by treatment with either rifampicin or 3-methylcholanthrene. |
| | |
Authors:
|
K Kurose; E Isozaki; M Tohkin; M Fukuhara |
Related Documents
:
|
21349564 - Cdna cloning and recombinant expression of a proliferation inducing ligand (april) from... 3190674 - Four species of cdnas for cytochrome p450 isozymes immunorelated to p450c-m/f encode fo... 20153434 - Identification, characterization and genetic mapping of tlr1 loci in rainbow trout (onc... 20730594 - Component identification of electron transport chains in curdlan-producing agrobacteriu... 6310494 - The genes coding for histone h3 and h4 in neurospora crassa are unique and contain inte... 15865984 - Detecting differential expression of parental or progenitor alleles in genetic hybrids ... |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
|
Title: Archives of biochemistry and biophysics Volume: 371 ISSN: 0003-9861 ISO Abbreviation: Arch. Biochem. Biophys. Publication Date: 1999 Nov |
Date Detail:
|
Created Date: 1999-12-21 Completed Date: 1999-12-21 Revised Date: 2006-11-15 |
Medline Journal Info:
|
Nlm Unique ID: 0372430 Medline TA: Arch Biochem Biophys Country: UNITED STATES |
Other Details:
|
Languages: eng Pagination: 270-6 Citation Subset: IM |
Copyright Information:
|
Copyright 1999 Academic Press. |
Affiliation:
|
Department of Pharmaceutical Sciences, National Institute of Public Health, 4-6-1 Shirokanedai, Minato-ku, Tokyo, 108-8638, Japan. kurose@iph.go.jp |
| Data Bank Information | |
Bank Name/Acc. No.:
|
GENBANK/AB022916 |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Amino Acid Sequence Animals Aryl Hydrocarbon Hydroxylases* Base Sequence Cloning, Molecular Cricetinae Cytochrome P-450 Enzyme System / genetics*, metabolism DNA, Complementary / genetics Female Gene Expression Hydroxylation Isoenzymes / genetics, metabolism Liver / drug effects, enzymology Male Methylcholanthrene / pharmacology Microsomes / enzymology Molecular Sequence Data Phenobarbital / pharmacology Phylogeny Recombinant Proteins / metabolism Rifampin / pharmacology Steroid Hydroxylases / genetics*, metabolism Testosterone / metabolism* Tissue Distribution |
| Chemical | |
Reg. No./Substance:
|
0/DNA, Complementary; 0/Isoenzymes; 0/Recombinant Proteins; 13292-46-1/Rifampin; 50-06-6/Phenobarbital; 56-49-5/Methylcholanthrene; 58-22-0/Testosterone; 9035-51-2/Cytochrome P-450 Enzyme System; EC 1.14.-/Steroid Hydroxylases; EC 1.14.14.1/Aryl Hydrocarbon Hydroxylases; EC 1.14.14.1/steroid hormone 6-beta-hydroxylase; EC 1.14.14.1/testosterone 7-alpha-hydroxylase, hamster |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Overexpression of Mn-containing superoxide dismutase in transgenic Drosophila melanogaster.
Next Document: Comparative study of the inhibition of alpha-glucosidase, alpha-amylase, and cyclomaltodextrin gluca...