Structure and functions of human oxysterol 7alpha-hydroxylase cDNAs and gene CYP7B1.

Structure and functions of human oxysterol 7alpha-hydroxylase cDNAs and gene CYP7B1.

Wu Z; Martin K O; Javitt N B; Chiang J Y

Journal of lipid research

1999

1999-12

Oxysterol 7alpha-hydroxylase has broad substrate specificity for sterol metabolites and may be involved in many metabolic processes including bile acid synthesis and neurosteroid metabolism. The cloned human oxysterol 7alpha-hydroxylase (CYP7B1) cDNA encodes a polypeptide of 506 amino acid residues that shares 40% sequence identity to human cholesterol 7alpha-hydroxylase (CYP7A1), the rate-limiting enzyme in the conversion of cholesterol to bile acids in the liver. In contrast to the liver-specific expression of CYP7A1, CYP7B1 mRNA transcripts were detected in human tissues involved in steroid genesis (brain, testes, ovary, and prostate) and in bile acid synthesis (liver) and reabsorption (colon, kidney, and small intestine). The human oxysterol 7alpha-hydroxylase transiently expressed in 293/T cells was able to catalyze 7alpha-hydroxylation of

Humans; Animals; Mice; Cell Line; Transfection; Base Sequence; Molecular Sequence Data; Chromosome Mapping; Cytochrome P450 Family 7; DNA; Luciferases/genetics; Cytochrome P-450 Enzyme System/*genetics/metabolism; Steroid Hydroxylases/*genetics/metabolism; Hydroxycholesterols/metabolism; Codon; Northern; Blotting; Transcription; Genetic; Cloning; Molecular; Genetic/genetics; Promoter Regions; Nucleic Acid; Complementary/biosynthesis/*isolation & purification; Initiator; Regulatory Sequences

Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).

2195–2203

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