Substrate-specific stimulation of protein kinase C by polyvalent anion.
Substrate-specific stimulation of protein kinase C by polyvalent anion.
复制标题
多价阴离子对蛋白激酶 C 的底物特异性刺激。
DOI：
10.1016/s0006-291x(87)80113-4
复制
发表时间：
1987
影响因子：
3.1
通讯作者：
Nelsestuen,GL
中科院分区：
文献类型：
--
作者：
Bazzi,MD;Nelsestuen,GL
蛋白激酶C（PKC）对富含精氨酸的底物的活性被硫酸根和磷酸根极大地刺激，但不是由单价阴离子。这种刺激不需要磷脂，钙，或甘油二酯，并出现模仿磷脂的刺激。阴离子蛋白质，如牛血清白蛋白也促进PKC活性对某些底物，其特征在于无论是高精氨酸或高赖氨酸含量。这两种刺激的机制似乎与底物-PKC复合物的形成有关，该复合物对PKC磷酸化至关重要。多价阴离子结合阳离子底物，并与PKC一起形成允许磷酸化的聚集体。这种刺激的潜在生理相关性进行了讨论。
The activity of protein kinase C (PKC) toward arginine-rich substrates was greatly stimulated by sulfate and phosphate, but not by monovalent anions. This stimulation did not require phospholipid, calcium, or diacylglycerol, and appeared to mimic the stimulation by phospholipid. Anionic proteins such as bovine serum albumin also promoted PKC activity toward certain substrates that were characterized by either high arginine or high lysine content. The mechanism of both of these stimulations appeared to be related to formation of a substrate-PKC complex which is essential to phosphorylation by PKC. Polyvalent anions bind the cationic substrate and, together with PKC, form an aggregate which allows phosphorylation. Potential physiological relevance of this stimulation is discussed.