Bazan E, Campbell A K, Rapoport R M
Department of Pharmacology and Cell Biophysics, University of Cincinnati, College of Medicine, OH 45267-0575, USA.
Eur J Pharmacol. 1995 Aug 15;290(3):253-7. doi: 10.1016/0922-4106(95)90001-2.
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.
本研究通过蛋白激酶C从胞质组分向颗粒组分的转位来评估，调查了佛波酯诱导的完整大鼠主动脉收缩速率与蛋白激酶C激活之间的关系。在加入佛波酯之前，将主动脉暴露于无钙生理盐溶液中，以防止在组织匀浆过程中钙诱导的蛋白激酶C转位。早在加入佛波酯后5秒，即收缩开始之前或与之同时，十四酰佛波醇乙酯以及佛波二丁酸酯就降低了胞质蛋白激酶C活性和/或增加了颗粒蛋白激酶C活性。这些结果表明，佛波酯诱导的完整血管平滑肌收缩与蛋白激酶C激活呈时间依赖性相关。
