TY - JOUR
T1 - Potentiation of diacylglycerol-activated protein kinase C by acyl-coenzyme a thioesters of hypolipidaemic drugs
AU - Bronfman, Miguel
AU - Orellana, Ariel
AU - Morales, M. Nelly
AU - Bieri, Francoise
AU - Waechter, Felix
AU - Stäubli, Willy
AU - Bentley, Philip
N1 - Funding Information:
This work was partially supported by the Direction de Investigation de la P.Universidad Catolica de Chile (DIUC 82/86), and Fondo National de Ciencias (Fondecyt 390/88). We thank Dr. N.C. Inestrosa and Dr. A.Gonzalez for valuable discussion and suggestions.
PY - 1989/3/31
Y1 - 1989/3/31
N2 - Acyl-Coenzyme A thioesters of the hypolipidaemic and cancerinogenic peroxisome proliferators clofibric acid, nafenopin, ciprofibrate, bezafibrate and tibric acid were found to greatly increase the activity of rat brain protein kinase C. Maximal activation required the simultaneous presence of Ca+2, phosphatidylserine and diolein, thus differentiating their action from that of other tumor promoters such as phorbol esters. Under similar conditions the unesterified drugs were comparatively ineffective. Similar results were obtained using the rat liver enzyme. The data suggest that acyl-coenzyme A thioesters of hypolipidaemic drugs, may play a role in the induction of liver tumors by these compounds, through the potentiation of protein kinase C.
AB - Acyl-Coenzyme A thioesters of the hypolipidaemic and cancerinogenic peroxisome proliferators clofibric acid, nafenopin, ciprofibrate, bezafibrate and tibric acid were found to greatly increase the activity of rat brain protein kinase C. Maximal activation required the simultaneous presence of Ca+2, phosphatidylserine and diolein, thus differentiating their action from that of other tumor promoters such as phorbol esters. Under similar conditions the unesterified drugs were comparatively ineffective. Similar results were obtained using the rat liver enzyme. The data suggest that acyl-coenzyme A thioesters of hypolipidaemic drugs, may play a role in the induction of liver tumors by these compounds, through the potentiation of protein kinase C.
UR - http://www.scopus.com/inward/record.url?scp=0024560991&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(89)92211-0
DO - 10.1016/0006-291X(89)92211-0
M3 - Article
C2 - 2930549
AN - SCOPUS:0024560991
SN - 0006-291X
VL - 159
SP - 1026
EP - 1031
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -
