Time course of phorbol ester-induced contraction and protein kinase C activation in rat aorta.
This study investigates the relationship between the rate of phorbol ester-induced contraction of intact rat aorta and protein kinase C activation, as assessed by the translocation of protein kinase C from the cytosolic to the particulate fraction. Aorta was exposed to Ca(2+)-free physiologic salt solution prior to phorbol ester to prevent Ca(2+)-induced protein kinase C translocation during tissue homogenization. Phorbol myristate acetate, as well as phorbol dibutyrate, decreased cytosolic and/or increased particulate protein kinase C activity as early as 5 s following phorbol ester addition, which was prior to, or coincident with, the onset of contraction. These results suggests that phorbol ester-induced contraction of intact vascular smooth muscle is associated in a time-dependent manner with protein kinase C activation.
Bazan
E
E
Department of Pharmacology and Cell Biophysics, University of Cincinnati, College of Medicine, OH 45267-0575, USA.
Campbell
A K
AK
Rapoport
R M
RM
D000818:Animals; D001013:Aorta, Thoracic / Q000187:drug effects* / Q000201:enzymology*; D004789:Enzyme Activation / Q000187:drug effects; D066298:In Vitro Techniques; D008297:Male; D009119:Muscle Contraction / Q000187:drug effects; D009131:Muscle, Smooth, Vascular / Q000187:drug effects* / Q000201:enzymology*; D010703:Phorbol Esters / Q000494:pharmacology*; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley; D013997:Time Factors; D014178:Translocation, Genetic
D010703:Phorbol Esters; D011493:Protein Kinase C