Sakai K, Taniguchi T, Shimomura R, Asahi M, Kobayashi T, Inazu T, Nakamura S, Yamamura H
Department of Biochemistry, Fukui Medical School, Japan.
Biochem Biophys Res Commun. 1989 Dec 15;165(2):680-4. doi: 10.1016/s0006-291x(89)80019-1.
Effect of membrane phospholipids on the activity of cytosolic protein-tyrosine kinase from porcine spleen (CPTK-40) has been studied. Using poly(Glu Na, Tyr)4:1 as a substrate, phosphatidylethanolamine, phosphatidylcholine and phosphatidylserine had stimulatory effects on that phosphorylation activity, however phosphatidic acid had inhibitory and phosphatidylinositol had no effects. Similar results were obtained using[Val5]angiotensin II as a substrate. On the other hand using basic protein (H2B histone and myelin basic protein) as substrates, phosphatidic acid stimulated the activity of CPTK-40, while phosphatidylinositol inhibited the activity. Phosphatidylethanolamine, phosphatidylcholine and phosphatidylserine caused different effect on the activity of CPTK-40 depending on the substrate employed. However using acidic protein (tubulin and casein) as substrates, the activity of CPTK-40 was neither stimulated nor inhibited by any phospholipids. These results suggest that phospholipids may modulate the activity of CPTK-40.
研究了膜磷脂对猪脾脏胞质蛋白酪氨酸激酶（CPTK - 40）活性的影响。以聚（谷氨酸钠，酪氨酸）4:1为底物时，磷脂酰乙醇胺、磷脂酰胆碱和磷脂酰丝氨酸对该磷酸化活性有刺激作用，而磷脂酸有抑制作用，磷脂酰肌醇则无影响。以[缬氨酸5]血管紧张素II为底物时也得到了类似结果。另一方面，以碱性蛋白（H2B组蛋白和髓鞘碱性蛋白）为底物时，磷脂酸刺激CPTK - 40的活性，而磷脂酰肌醇抑制其活性。磷脂酰乙醇胺、磷脂酰胆碱和磷脂酰丝氨酸根据所使用的底物对CPTK - 40的活性产生不同影响。然而，以酸性蛋白（微管蛋白和酪蛋白）为底物时，任何磷脂均未刺激或抑制CPTK - 40的活性。这些结果表明磷脂可能调节CPTK - 40的活性。
