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Gene Review

CYP2B  -  cytochrome P450, family 2, subfamily B

Homo sapiens

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High impact information on CYP2B

  • There was no significant difference in expression of mEH, CYP2B7, or NADPH OR in smokers compared with nonsmokers [1].
  • CYP2B7 expression was evaluated because, although little is known of its substrate specificity, it is expressed at high levels in human lung tissue [1].
  • New proteins in the rat CYP2B subfamily: presence in liver microsomes of the constitutive CYP2B3 protein and the phenobarbital-inducible protein product of alternatively spliced CYP2B2 mRNA [2].
  • These results demonstrate the existence in rat liver of two new CYP2B proteins: CYP2B3, the major constitutive CYP2B form, and CYP2B2v, which represents a rare case of non-aberrant alternative splicing among xenobiotic-metabolizing P450s [2].
  • Inductions of CYP1A1 and CYP2B in hepatocytes cryopreserved with WPEs were similar to those in fresh hepatocytes [3].
 

Biological context of CYP2B

  • Quantitative structure-activity relationships (QSARs) within cytochromes P450 2B (CYP2B) subfamily enzymes: the importance of lipophilicity for binding and metabolism [4].
  • Although the linear relationships between lipophilicity and CYP2B-related activity point to a major role for desolvation of the enzyme binding site in the overall interaction, it is noted that there may be an optimal log P value displayed by preferred substrates as shown by parabolic relationships with this lipophilic parameter [4].
  • Western blot analyses of scup livers using anti-human CAR antisera revealed the occurrence of a putative CAR homologue in nuclear and cytoplasmic fractions, but no nuclear accumulation of CAR following TCPOBOP treatment, which is a first step regulating the transcriptional activation of CYP2B genes in mouse [5].
 

Associations of CYP2B with chemical compounds

  • The results of qualitative structure-activity relationship (QSAR) analysis are reported for several series of compounds which act as substrates for mammalian CYP2B subfamily enzymes, together with a homologous series of aliphatic primary amines which are known to inhibit CYP2B enzymes [4].
  • The mammalian constitutively active receptor (CAR) is a novel ligand-activated transcription factor that participates in controlling the expression of cytochrome P450 2B (CYP2B) genes in response to pharmaceutical agents (phenobarbital) and halogenated aromatic hydrocarbons (ortho-substituted PCBs) [5].

References

  1. Quantitative RT-PCR measurement of cytochromes p450 1A1, 1B1, and 2B7, microsomal epoxide hydrolase, and NADPH oxidoreductase expression in lung cells of smokers and nonsmokers. Willey, J.C., Coy, E.L., Frampton, M.W., Torres, A., Apostolakos, M.J., Hoehn, G., Schuermann, W.H., Thilly, W.G., Olson, D.E., Hammersley, J.R., Crespi, C.L., Utell, M.J. Am. J. Respir. Cell Mol. Biol. (1997) [Pubmed]
  2. New proteins in the rat CYP2B subfamily: presence in liver microsomes of the constitutive CYP2B3 protein and the phenobarbital-inducible protein product of alternatively spliced CYP2B2 mRNA. Desrochers, M., Christou, M., Jefcoate, C., Belzil, A., Anderson, A. Biochem. Pharmacol. (1996) [Pubmed]
  3. Wheat extracts as an efficient cryoprotective agent for primary cultures of rat hepatocytes. Hamel, F., Grondin, M., Denizeau, F., Averill-Bates, D.A., Sarhan, F. Biotechnol. Bioeng. (2006) [Pubmed]
  4. Quantitative structure-activity relationships (QSARs) within cytochromes P450 2B (CYP2B) subfamily enzymes: the importance of lipophilicity for binding and metabolism. Lewis, D.F., Lake, B.G., Ito, Y., Anzenbacher, P. Drug metabolism and drug interactions. (2006) [Pubmed]
  5. Species-specific responses of constitutively active receptor (CAR)-CYP2B coupling: lack of CYP2B inducer-responsive nuclear translocation of CAR in marine teleost, scup (Stenotomus chrysops). Iwata, H., Yoshinari, K., Negishi, M., Stegeman, J.J. Comp. Biochem. Physiol. C Toxicol. Pharmacol. (2002) [Pubmed]
 
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