Open AccessNuclear ADP‐ribosyl transferase activity correlates with induction of P‐450 monooxygenases by phenobarbital in rat liver microsomes
Author(s) -
LECHNER Maria Celeste,
BRÁZ Judite
Publication year - 1985
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1985.tb09149.x
Subject(s) - phenobarbital , microsome , transferase , chemistry , monooxygenase , cytochrome p450 , cytochrome , enzyme inducer , enzyme , biochemistry , in vivo , isozyme , biology , endocrinology , genetics
The effect of phenobarbital treatment on the nuclear ADP‐ribosyl transferase activity has been studied in parallel with microsomal cytochrome P‐450 concentration and related mono‐oxygenase activities, in rat liver. A marked activation of the ADP‐ribosyl transferase was observed 24 h after phenobarbital administration. The chronological study performed between 0–6 days after phenobarbital treatment showed a sharp increase in this nuclear enzyme activity, to ∼ 270% of the control value produced in 48 h. The administration of 5′‐methylnicotinamide in vivo , an inhibitor of ADP‐riboyl transferase activity in vitro , produced a decrease both of the induction of liver microsomal cytochrome P‐450 mono‐oxygenases and nuclear ADP‐ribosyl transferase activity. The role of nuclear ADP‐ribosyl transferase in the adaptative response of the liver cell to phenobarbital is discussed.