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Oesch-Bartlomowicz, B. and Oesch, F. (2004) Modulation of mutagenicity by phosphorylation of mutagenmetabolizing enzymes. Archives of Biochemistry and Biophysics, 423, 31-36. doi:10.1016/j.abb.2003.11.020

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• TITLE: In vivo effects of genistein, herbimycin a and geldanamycin on rat hepatic cytochrome P4501A

  AUTHORS: Maria L. Perepechaeva, Alevtina Y. Grishanova

  KEYWORDS: Protein-Tyrosine Kinase; Aryl Hydrocarbon Receptor; Cytochromes P450 1A Regulation

  JOURNAL NAME: Journal of Biophysical Chemistry, Vol.3 No.4, November 29, 2012

  ABSTRACT: Cytochrome P4501A (the CYP1A1 and CYP1A2 enzymes) are regulated through the aryl hydrocarbon receptor (AhR)-dependent signal transduction pathway and are generally known as enzymes which metabolize anthropogenic xenobiotics such as dioxin to carcinogenic and mutagenic compounds. However, recently the facts of CYP1A activation under physiological conditions or under action of non-dioxin-like compounds appear. In the present study we show that genistein, herbimycin A and geldanamycin (the protein-tyrosine kinase inhibitors) affect in vivo to CYP1A1 activity, the CYP1A1 mRNA level and the CYP1A1 protein level. These data provide insight into the role of protein kinases in CYP1A regulation may facilitate the understanding of CYP1A regulation.