Turnover of membrane proteins: Kinetics of induction and degradation of seven forms of rat liver microsomal cytochrome P-450, NADPH-cytochrome P-450 reductase, and epoxide hydrolase☆
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2019, Journal of Food and Drug AnalysisCitation Excerpt :However, results of immunoblotting analysis of microsomal CYP3A showed that acute SY treatment did not decrease the immunoreactive protein level (supporting information). The mean degradation half-life of rat CYP3A2 was estimated to be 12–27 h [23]. The inactivated CYP might keep immunoreactivity but was not spectrally detected.
Reduction of thyroid hormones triggers down-regulation of hepatic CYP2B through nuclear receptors CAR and TR in a rat model of acute stroke
2014, Biochemical PharmacologyCitation Excerpt :Significant CYP2B1 mRNA changes were observed without large changes in protein levels may be due to the lower rates of protein turnover than mRNA. The in vivo half-life of rat CYP2B1 protein is estimated to be more than 30 h [35]; however, the average half-life of mRNAs is usually 2.6–7 h for mammalian [36]. The time course experiments have shown that the decreases in thyroid hormones occurred before the appearance of the change in hepatic CYP2B1 mRNA and protein expression in the brain I/R-operation rats, while no change in the plasma levels of IL-1β, AST, and ALT was observed at that time point.
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2008, Toxicology and Applied PharmacologyNitric oxide-dependent proteasomal degradation of cytochrome P450 2B proteins
2008, Journal of Biological ChemistryCitation Excerpt :Second, the selective NOS2 inhibitor AG (47) blocked the production of NO. Third, we reported previously that LY83583, which inhibits inducible NOS induction rather than its enzymatic activity, blocked both NO production and CYP2B down-regulation in response to IL-1 (26). The reported constitutive half-life of CYP2B1 varies by 19–25 h (48, 49), and the degradation pathway of CYP2B1 seemed to be in lysosomes based on the presence of CYP2B1 in lysosomal compartments both in the presence or absence of leupeptin treatment of the rats (50, 51). This was supported by genetic evidence in yeast in which transfected rat CYP2B1 was found to be degraded in the vacuolar/lysosomal compartment (52).
Relationship between aryl hydrocarbon receptor-affinity and the induction of EROD activity by 2,3,7,8-tetrachlorinated phenothiazine and derivatives
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2006, Biochemical PharmacologyCitation Excerpt :However, this does not appear to be the mechanism underlying the STIIR-induced reduction in P450 activity, since TIIR nitrates tyrosine of CYP1A1/2 and CYP3A6 in HCONT as well as in HTIIR without loss of activity in the former [50]. On the other hand, direct phosphorylation of serine residues by protein kinase C (PKC) or other kinase will abrogate P450 enzyme catalytic activity [51–53]. Peroxynitrite is capable to activate several kinases, e.g. the phosphoinositide 3-kinase/Akt pathway and Erk1/2 [54,55].
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This research was supported in part by Grants ES 01590 and ES 00267 from the National Institutes of Health.
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On leave from the Institute for Protein Research, Osaka University, 3-2 Yamadoka, Suita, Osaka 565, Japan.
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F.P.G. was the recipient of United States Public Health Service Research Career Development Award ES 00041 (1978–1983).