HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Adesnik, M. Articles by Bard, E. Search for Related Content PubMed PubMed Citation Articles by Adesnik, M. Articles by Bard, E. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 256, Issue 20, 10340-10345, 10, 1981

Mechanism of induction of cytochrome P-450 by phenobarbital

M Adesnik, S Bar-Nun, F Maschio, M Zunich, A Lippman and E Bard

Treatment of rats with phenobarbital (PB) leads to a substantial increase in the hepatic levels of translatable polysomal poly(A) + cytochrome P-450 mRNA. An enriched fraction of P-450 mRNA was obtained by agarose gel electrophoresis and used to prepare a cDNA probe by differential hybridization to total mRNA from control and PB-treated rats. The majority of the sequences within the probe hybridized to recombinant DNA plasmids which contained a bona fide P-450 cDNA insert identified by positive hybridization selection and in vitro translation. The cDNA probe was used to demonstrate that PB treatment leads to a 30-fold increase in polysomal P-450 mRNA, which is not due to more efficient utilization of previously existing mRNA but to the appearance of new messenger in the cytoplasm. The induction of cytoplasmic P-450 mRNA by PB was rapid, with increases detected within 3 h of PB injection and steady state levels reached in approximately 20 h. The data suggest that the increase in cytoplasmic P-450 protein levels observed after PB treatment may be totally accounted for by an enhanced rate of synthesis resulting from translation of higher cytoplasmic levels of its specific mRNA. The P-450 mRNA was almost exclusively segregated into the membrane-bound polysome compartment was expected for an mRNA coding for an integral membrane protein of the endoplasmic reticulum.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				E. Le Ferrec, G. Ilyin, K. Maheo, C. Bardiau, A. Courtois, A. Guillouzo, and F. Morel Differential effects of oltipraz on CYP1A and CYP2B in rat lung Carcinogenesis, January 1, 2001; 22(1): 49 - 55. [Abstract] [Full Text] [PDF]

				E. LeCluyse, P. Bullock, A. Madan, K. Carroll, and A. Parkinson Influence of Extracellular Matrix Overlay and Medium Formulation on the Induction of Cytochrome P-450 2B Enzymes in Primary Cultures of Rat Hepatocytes Drug Metab. Dispos., August 1, 1999; 27(8): 909 - 915. [Abstract] [Full Text]

				C. Stoltz, M.-H. Vachon, E. Trottier, S. Dubois, Y. Paquet, and A. Anderson The CYP2B2 Phenobarbital Response Unit Contains an Accessory Factor Element and a Putative Glucocorticoid Response Element Essential for Conferring Maximal Phenobarbital Responsiveness J. Biol. Chem., April 3, 1998; 273(14): 8528 - 8536. [Abstract] [Full Text] [PDF]

				Y. Park, H. Li, and B. Kemper Phenobarbital Induction Mediated by a Distal CYP2B2 Sequence in Rat Liver Transiently Transfected in Situ J. Biol. Chem., September 27, 1996; 271(39): 23725 - 23728. [Abstract] [Full Text] [PDF]