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Induction of drug metabolizing enzymes in human liver cell line Hep G2
Author(s) -
Dawson J.R.,
Adams D.J.,
Wolf C.R.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80780-8
Subject(s) - phenobarbital , glucuronidation , enzyme inducer , methylcholanthrene , cytochrome p450 , hep g2 , chemistry , biochemistry , cell culture , enzyme , cytochrome , liver cell , microsome , isozyme , glucuronosyltransferase , cell , microbiology and biotechnology , pharmacology , biology , carcinogen , medicine , in vitro , genetics
Human cytochrome P‐450, UDP‐glucuronosyltransferase and sulphotransferase activities have been measured in the cell line Hep G2 following treatment of cells with 3‐methylcholanthrene or phenobarbital. 3‐Methylcholanthrene treatment caused a 20–30‐fold increase in the O‐deethylation of 7‐ethoxycoumarin. The glucuronidation and sulphation of the product 7‐hydroxycoumarin were increased 36 and 7 fold, respectively. In comparison, phenobarbital treatment did not increase these activities significantly. However, phenobarbital‐inducible proteins were identified on ‘Western blots’ using antibodies to a rat liver phenobarbital inducible P‐450 form. The molecular masses of the proteins did not coincide with those expected for cytochromes P‐450. However, characteristic of P‐450 forms, the synthesis of these proteins was suppressed by 3‐methylcholanthrene treatment. The Hep G2 cell line represents a potentially useful model for studying the regulation of human P‐450 genes.