Nakaki T, Wise B C, Chuang D M
Laboratory of Preclinical Pharmacology, National Institute of Mental Health, St. Elizabeths Hospital, Washington, D.C. 20032.
Life Sci. 1988;42(13):1315-21. doi: 10.1016/0024-3205(88)90225-1.
Protein phosphorylation has been studied in a cell free system of rat aorta smooth muscles. Addition of Ca2+ caused phosphorylation of several proteins. The addition of phosphatidylserine or calmodulin together with Ca2+ further increased the phosphorylation of proteins with apparent molecular weights of 20 and 92.5 kilodaltons. The activators of protein kinase C, 12-0-tetradecanoylphorbol-13-acetate and 1,2-diolein, increased phosphorylation of the protein bands of similar molecular weight to those increased by phosphatidylserine in the presence of Ca2+, whereas the biologically inactive phorbol ester, 4 alpha-phorbol-12,13 didecanoate (4 alpha PDD) failed to change the pattern of protein phosphorylation. These results show that proteins present in smooth muscle of rat aorta with molecular weights of 20 and 92.5 kilodaltons are substrates for protein kinase C.
已在大鼠主动脉平滑肌的无细胞体系中研究了蛋白质磷酸化作用。添加Ca2+会导致几种蛋白质发生磷酸化。将磷脂酰丝氨酸或钙调蛋白与Ca2+一起添加，会进一步增加表观分子量为20和92.5千道尔顿的蛋白质的磷酸化。蛋白激酶C的激活剂，12-0-十四酰佛波醇-13-乙酸酯和1,2-二油精，在Ca2+存在的情况下，会增加与磷脂酰丝氨酸增加的分子量相似的蛋白条带的磷酸化，而无生物学活性的佛波酯4α-佛波醇-12,13-二癸酸酯（4αPDD）则无法改变蛋白质磷酸化模式。这些结果表明，大鼠主动脉平滑肌中分子量为20和92.5千道尔顿的蛋白质是蛋白激酶C的底物。
