DIFFERENTIAL PHORBOL ESTER GROWTH MODULATION AND PROTEIN-KINASE-C ISOENZYME EXPRESSION IN RAT HEPATOMA-CELLS VS NON NEOPLASTIC RAT HEPATOCYTES

1994 ◽  
Author(s):  
GP PERLETTI ◽  
F PICCININI
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Rat Hepatocytes ◽  
Hepatoma Cells ◽  
Growth Modulation ◽  
Kinase C ◽  
Rat Hepatoma ◽  
Rat Hepatoma Cells

Effect of phorbol esters and diacylglycerol on steroid metabolism in isolated rat hepatocytes

1988 ◽  
Vol 118 (1) ◽  
pp. 19-23 ◽  
Author(s):  
C. J. Allan ◽  
P. Skett
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Phorbol Esters ◽  
Rat Hepatocytes ◽  
Male Rats ◽  
Steroid Metabolism ◽  
Isolated Rat Hepatocytes ◽  
Kinase C ◽  
Activate Protein Kinase

ABSTRACT Hepatocytes, isolated from adult male rats and maintained in serum- and hormone-free medium, were pretreated with phorbol esters known to activate protein kinase C (4β-phorbol-12-myristate-13-acetate) and to be inactive in this respect (4α-phorbol and its 12,13-didecanoate ester). Subsequently the cells were assayed for steroid-metabolizing capacity using androst-4-ene-3,17-dione as substrate. The active phorbol ester was seen to inhibit steroid metabolism markedly after 1 h whereas the inactive derivatives did not show this effect. The endogenous activator of protein kinase C (diacylglycerol) was also seen to inhibit steroid metabolism in a manner similar to the 4β-phorbol ester. Hepatic steroid metabolism is, thus, inhibited by activation of protein kinase C and this may be one of the mechanisms by which the regulatory hormones (e.g. growth hormone) affect steroid metabolism in the liver. J. Endocr. (1988) 118, 19–23

Sign in / Sign up

Export Citation Format

Share Document