RGD Reference Report - Identification of a rat adrenal cytochrome P450 active in polycyclic hydrocarbon metabolism as rat CYP1B1. Demonstration of a unique tissue-specific pattern of hormonal and aryl hydrocarbon receptor-linked regulation. - Rat Genome Database

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Identification of a rat adrenal cytochrome P450 active in polycyclic hydrocarbon metabolism as rat CYP1B1. Demonstration of a unique tissue-specific pattern of hormonal and aryl hydrocarbon receptor-linked regulation.

Authors: Bhattacharyya, KK  Brake, P B  Eltom, S E  Otto, S A  Jefcoate, C R 
Citation: Bhattacharyya KK, etal., J Biol Chem 1995 May 12;270(19):11595-602.
RGD ID: 728267
Pubmed: PMID:7744798   (View Abstract at PubMed)

Antibodies against a novel adrenocorticotropic hormone-inducible cytochrome P450 (P450RAP), responsible for polycyclic aromatic hydrocarbon metabolism in rat adrenal microsomes (Otto, S., Bhattacharyya, K.K., and Jefcoate, C.R. (1992) Endocrinology 131, 3067-3076), identified a cDNA clone encoding a partial cytochrome P450 sequence from a rat adrenal cDNA library. Rescreening a second cDNA library yielded several clones up to 5.0 kilobases (kb) encoding a 1629-base pair open reading frame. The deduced amino acid sequence (543 residues) matched completely with five peptides cleaved from P450RAP. The amino acid sequence of P450RAP is 92% identical to a 2,3,7,8-tetrachlorodibenzo-p-dioxin-inducible CYP1B1, cloned from mouse C3H10T1/2 (10T1/2) embryo fibroblast cells (Savas, U., Bhattacharyya, K. K., Christou, M., Alexander, D.L., and Jefcoate, C. R. (1994) J. Biol. Chem. 269, 14905-14911), which shows nearly the same characteristics in polycyclic aromatic hydrocarbon metabolism. The available 5'- and 3'-noncoding regions show, respectively, 93 and 83% sequence identity. We conclude that P450RAP protein is encoded by a rat CYP1B1 gene orthologous to the mouse CYP1B1 gene. Alignment of rat CYP1B1 amino acid sequences with rat CYP1A1 (39% identical) indicated eight regions of high identity for each (60-78%), interspersed by extensive regions of less than 30% similarity. The CYP1B1 cDNAs hybridize a 5.2-kb mRNA in rat adrenals, consistent with the length of the longest clones and the mRNA recognized in 10T1/2 cells. CYP1B1 mRNA was elevated by a 2-day adrenocorticotropic hormone treatment but much less than CYP11A1 (cytochrome P450 side chain cleavage) mRNA (2-fold versus 4-fold). The lower levels of the 5.2-kb mRNA in other steroidogenic cells (ovary) was consistent with the amount of immunodetectable CYP1B1 protein and, unlike the adrenal, expression in the ovary was stimulated 5-fold by beta-naphthoflavone, an aryl hydrocarbon receptor agonist, in parallel with CYP1A1 induction. In several other tissues (liver > lung > uterus >> kidney), CYP1B1 mRNA and protein were constitutively undetectable but highly induced by beta-naphthoflavone, although at much lower levels than CYP1A1. Rat CYP1B1, therefore, exhibits regulation through hormonal signaling and the aryl hydrocarbon receptor in a cell-specific manner.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
response to organic cyclic compound  IEP 728267beta-naphthoflavoneRGD 

Molecular Pathway Annotations    Click to see Annotation Detail View

RGD Manual Annotations

Objects Annotated

Genes (Rattus norvegicus)
Cyp1b1  (cytochrome P450, family 1, subfamily b, polypeptide 1)

Genes (Mus musculus)
Cyp1b1  (cytochrome P450, family 1, subfamily b, polypeptide 1)

Genes (Homo sapiens)
CYP1B1  (cytochrome P450 family 1 subfamily B member 1)


Additional Information