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CYP2E1  -  cytochrome P450, family 2, subfamily E,...

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High impact information on CYP2E1

  • After 4 weeks of ethanol intoxication, although cytochrome CYP2E1 was increased, liver lipid peroxidation remained unchanged when protein carbonyls augmented selectively for high molecular weight with a decrease of the proteasome activities in ethanol rats [1].
  • By contrast, the olfactory monooxygenases associated with CYP2E1 were poorly or not detected, whereas CYP2G1 and a protein immunorelated to CYP1A2 were expressed in the olfactory epithelium [2].
  • 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 [3].
  • Although 4-nitrophenol activity was observed in the rabbit tongue samples, the kinetic parameter K(m) was inconsistent with the involvement of CYP2E1 [4].

References

  1. The effects of acetaldehyde in vitro on proteasome activities and its potential involvement after alcoholization of rats by inhalation of ethanol vapours. Rouach, H., Andraud, E., Aufrère, G., Beaugé, F. Alcohol Alcohol. (2005) [Pubmed]
  2. Xenobiotic-metabolizing enzymes in pig nasal and hepatic tissues. Marini, S., Longo, V., Mazzaccaro, A., Gervasi, P.G. Xenobiotica (1998) [Pubmed]
  3. Phosphorylation of cytochrome P4502E1 (CYP2E1) by calmodulin dependent protein kinase, protein kinase C and cAMP dependent protein kinase. Menez, J.F., Machu, T.K., Song, B.J., Browning, M.D., Deitrich, R.A. Alcohol Alcohol. (1993) [Pubmed]
  4. Cytochrome P450 expression and activities in rat, rabbit and bovine tongue. Yang, S.P., Medling, T., Raner, G.M. Comp. Biochem. Physiol. C Toxicol. Pharmacol. (2003) [Pubmed]
 
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