Liu Q Y, Karpinski E, Pang P K
Department of Physiology, University of Alberta, Edmonton, Canada.
Biochem Biophys Res Commun. 1993 Mar 31;191(3):796-801. doi: 10.1006/bbrc.1993.1287.
Ca2+ channels can be modulated by protein kinase C which phosphorylates Ca2+ channel proteins. Two protein kinase C activators, 4 beta-phorbol 12-myristate 13-acetate (PMA) and 1-oleyl-2-acetyl-rac-glycerol (OAG), were used to investigate the effect of protein kinase C activation on dihydropyridine-sensitive Ca2+ channel currents (L-type) in neonatal rat ventricular myocytes using the whole cell version of the patch clamp technique. The results show that both of the activators increased the Ca2+ channel current in myocytes. However, these increases in Ca2+ channel current were different as function of time. Therefore, our results suggest that the temporal factor should be considered when the protein kinase C activators are used in studies of channel modulation.
蛋白激酶C可通过使Ca2+通道蛋白磷酸化来调节Ca2+通道。使用两种蛋白激酶C激活剂,即4β-佛波醇12-肉豆蔻酸酯13-乙酸酯(PMA)和1-油酰基-2-乙酰基-rac-甘油(OAG),采用膜片钳技术的全细胞模式,研究蛋白激酶C激活对新生大鼠心室肌细胞中二氢吡啶敏感的Ca2+通道电流(L型)的影响。结果表明,两种激活剂均增加了心肌细胞中的Ca2+通道电流。然而,这些Ca2+通道电流的增加随时间变化有所不同。因此,我们的结果表明,在使用蛋白激酶C激活剂进行通道调节研究时,应考虑时间因素。