PMID- 10588945
OWN - NLM
STAT- MEDLINE
DCOM- 20000210
LR  - 20190321
IS  - 0022-2275 (Print)
IS  - 0022-2275 (Linking)
VI  - 40
IP  - 12
DP  - 1999 Dec
TI  - Structure and functions of human oxysterol 7alpha-hydroxylase cDNAs and gene
      CYP7B1.
PG  - 2195-203
AB  - 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
      27-hydroxycholesterol and dehydroepiandrosterone (DHEA). The human CYP7A1 and
      CYP7B1 both contain six exons and five introns. However, CYP7B1 spans at least 65
      kb of the genome and is about 6-fold longer than CYP7A1. The transcription start 
      site (+1) was localized 204 bp upstream of the initiation codon. No TATA box-like
      sequence was found near the transcription start site. Transient transfection
      assays of CYP7B1 promoter/luciferase reporter constructs in HepG2 cells revealed 
      that the promoter was highly active. The 5' upstream region from nt -83 to +189
      is the core promoter of the gene.
FAU - Wu, Z
AU  - Wu Z
AD  - Department of Biochemistry and Molecular Pathology, Northeastern Ohio
      Universities College of Medicine, P. O. Box 95, Rootstown, OH 44272, USA.
FAU - Martin, K O
AU  - Martin KO
FAU - Javitt, N B
AU  - Javitt NB
FAU - Chiang, J Y
AU  - Chiang JY
LA  - eng
GR  - R01 DK044442/DK/NIDDK NIH HHS/United States
GR  - R01 DK058379/DK/NIDDK NIH HHS/United States
GR  - DK44442/DK/NIDDK NIH HHS/United States
GR  - GM31584/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Lipid Res
JT  - Journal of lipid research
JID - 0376606
RN  - 0 (Codon, Initiator)
RN  - 0 (DNA, Complementary)
RN  - 0 (Hydroxycholesterols)
RN  - 6T2NA6P5SQ (27-hydroxycholesterol)
RN  - 9035-51-2 (Cytochrome P-450 Enzyme System)
RN  - EC 1.13.12.- (Luciferases)
RN  - EC 1.14.- (Steroid Hydroxylases)
RN  - EC 1.14.13.- (oxysterol 7-alpha-hydroxylase)
RN  - EC 1.14.14.23 (Cytochrome P450 Family 7)
RN  - EC 1.14.14.29 (CYP7B1 protein, human)
SB  - IM
MH  - Animals
MH  - Base Sequence
MH  - Blotting, Northern
MH  - Cell Line
MH  - Chromosome Mapping
MH  - Cloning, Molecular
MH  - Codon, Initiator
MH  - Cytochrome P-450 Enzyme System/*genetics/metabolism
MH  - Cytochrome P450 Family 7
MH  - DNA, Complementary/biosynthesis/*isolation & purification
MH  - Humans
MH  - Hydroxycholesterols/metabolism
MH  - Luciferases/genetics
MH  - Mice
MH  - Molecular Sequence Data
MH  - Promoter Regions, Genetic
MH  - Regulatory Sequences, Nucleic Acid
MH  - Steroid Hydroxylases/*genetics/metabolism
MH  - Transcription, Genetic/genetics
MH  - Transfection
EDAT- 1999/12/10 00:00
MHDA- 1999/12/10 00:01
CRDT- 1999/12/10 00:00
PHST- 1999/12/10 00:00 [pubmed]
PHST- 1999/12/10 00:01 [medline]
PHST- 1999/12/10 00:00 [entrez]
PST - ppublish
SO  - J Lipid Res. 1999 Dec;40(12):2195-203.