Induction of lauric acid hydroxylation and maintenance of cytochrome P-450 content by clofibrate in primary cultures of rat hepatocytes

Life Sciences ◽  
1983 ◽  
Vol 33 (3) ◽  
pp. 249-254 ◽  
Author(s):  
Brian G. Lake ◽  
Tim J.B. Gray ◽  
Colin R. Stubberfield ◽  
Jenny A. Beamand ◽  
Sharat D. Gangolli
Keyword(s):  
Lauric Acid ◽  
Primary Cultures ◽  
Rat Hepatocytes ◽  
Acid Hydroxylation ◽  
Cytochrome P 450

Comparison of cytochrome P-450 levels in adult rat liver, postnatal rat liver, and primary cultures of postnatal rat hepatocytes

Life Sciences ◽  
1979 ◽  
Vol 25 (16) ◽  
pp. 1413-1418 ◽  
Author(s):  
Daniel Acosta ◽  
David C. Anuforo ◽  
Reagan McMillin ◽  
William H. Soine ◽  
Robert V. Smith
Keyword(s):  
Rat Liver ◽  
Primary Cultures ◽  
Rat Hepatocytes ◽  
Adult Rat ◽  
Cytochrome P 450

Long-term maintenance and induction of cytochrome P-450 in primary cultures of rat hepatocytes

1982 ◽  
Vol 31 (12) ◽  
pp. 2211-2214 ◽  
Author(s):  
Kenneth F. Nelson ◽  
Daniel Acosta ◽  
James V. Bruckner
Keyword(s):  
Primary Cultures ◽  
Rat Hepatocytes ◽  
Cytochrome P 450 ◽  
Term Maintenance

Apparent maintenance of cytochrome P 450 by nicotinamide in primary cultures of rat hepatocytes

Life Sciences ◽  
1979 ◽  
Vol 24 (23) ◽  
pp. 2185-2191 ◽  
Author(s):  
Alan J. Paine ◽  
Lesley J. Williams ◽  
Robert F. Legg
Keyword(s):  
Primary Cultures ◽  
Rat Hepatocytes ◽  
Cytochrome P 450

scholarly journals Induction of cytochrome P-450 in cultured rat hepatocytes. The heterogeneous localization of specific isoenzymes using immunocytochemistry

1989 ◽  
Vol 262 (1) ◽  
pp. 151-158 ◽  
Author(s):  
R G Bars ◽  
A M Mitchell ◽  
C R Wolf ◽  
C R Elcombe
Keyword(s):  
Primary Cultures ◽  
Liver Microsomes ◽  
Rat Hepatocytes ◽  
Clofibric Acid ◽  
Maximal Concentration ◽  
Heterogeneous Distribution ◽  
Cultured Rat Hepatocytes ◽  
Cytochrome P 450

Primary cultures of rat hepatocytes were exposed to phenobarbitone, clofibric acid, beta-naphthoflavone, isosafrole or dexamethasone for 3 days, and the induction of several cytochrome P-450 isoenzymes was demonstrated by increased catalytic activity, by Western blotting and by immunocytochemistry. The profiles of isoenzymes induced in vitro were compared with those induced in liver microsomes of rats dosed with the same agents. Clofibric acid, an agent which has not been thoroughly investigated previously, was shown to induce both in vivo and in vitro several P-450 isoenzymes normally inducible by phenobarbitone (PB1a, PB3a and PB3b) or steroids (PB2c). Immunocytochemical studies demonstrated that the inducible isoenzymes of cytochrome P-450 are not distributed evenly throughout the hepatocyte population, and increasing concentrations of phenobarbitone or beta-naphthoflavone in the medium results in an increasing proportion of ‘induced’ cells. However, whereas maximal concentrations of beta-naphthoflavone resulted in virtually all cells containing induced levels of MC1b, a maximal concentration of phenobarbitone resulted in only 30% of the cells containing induced levels of PB3a/PB3b. These results are discussed in relation to the heterogeneous distribution and induction of cytochrome P-450 in the intact liver.

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