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© 1993 Medical Council on Alcohol

research-article

PHOSPHORYLATION OF CYTOCHROME P4502E1 (CYP2E1) BY CALMODULIN DEPENDENT PROTEIN KINASE PROTEIN KINASE C AND cAMP DEPENDENT PROTEIN KINASE

J.-F. MENEZ*,{dagger}, T. K. MACHU*, B.-J. SONG{ddagger}, M. D. BROWNING* and R. A. DEITRICH*

*Pharmacology Department, University of Colorado Health Sciences Center 4200 E 9th Avenue, Denver, CO 80262, U.S.A.
{ddagger}Laboratory of Metabolism and Molecular Biology, National Institute on Alcohol Abuse and Alcoholism 12501 Washington Avenue, Rockville, MD 20892, U.S.A.

{dagger}Author to whom all correspondence should be addressed at: Laboratoire de Biochimie, Faculté de Médecine, 22 Av. Camille Desmoulins, 29285 Brest Cedex, France

Received 5 October 1992; first review notified 27 January 1993; accepted 5 February 1993

Phosphorylation of pure cytochrome P4502E1 (CYP2E1) was achieved in vitro using Ca2+/calmodulin-dependent protein kinase II (CaM kinase II), protein kinase C (PKC) and cAMP-dependent protein kinase (PKA). The stoichiometry and time-course of phosphorylation were determined. CaM kinase II was the most efficient enzyme capable of catalyzing this phosphorylation reaction: the maximum incorporation of 32PO4 was 0.8 mol/mol CYP2E1 in 20 min. PKA phosphorylated a maximum of 0.7 mol of 32PO4/ mol of cytochrome within 60 min. The phosphorylation by PKC reached a maximum of 0.19 mol of 32PO4/mol of cytochrome and this occurred within a few minutes of incubation. Limited digestion by S. aureus V8 protease (SAP) of CYP2E1, which had been phosphorylated by either PKA and PKC, yielded a single major phosphopeptide with an Mr of approximately 18,000. Limited digestion of CYP2E1, that had been phosphorylated by CaM kinase II, yielded phosphorylated polypeptides with Mr of approximately 18,000 and 15,000. These results raise the possibility that these three kinases may be involved in the regulation of CYP2E1.


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