Down-regulation of protein kinase C is due to an increased rate of degradation.
The phorbol-ester-induced loss of protein kinase C that has been documented in many cell types appears to be a critical event in the generation of a cellular refractory state. We have investigated here the synthesis and degradation of the protein kinase C polypeptide in order to determine why its steady-state amounts are depleted in response to phorbol esters. These results indicate that depletion is due to an increased rate of degradation, with no change either in mRNA amounts or in rates of polypeptide synthesis.
Young
S
S
Imperial Cancer Research Fund, Lincoln's Inn Fields, London, U.K.
Parker
P J
PJ
Ullrich
A
A
Stabel
S
S
D000818:Animals; D002460:Cell Line; D011232:Chemical Precipitation; D007122:Immunoelectrophoresis; D008715:Methionine / Q000378:metabolism; D010452:Peptide Biosynthesis; D011493:Protein Kinase C / Q000276:immunology / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism; D051381:Rats; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D012333:RNA, Messenger; D008715:Methionine; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate