磷脂酸的双阴离子形式对蛋白激酶C的非钙依赖性激活。
Calcium-independent activation of protein kinase C by the dianionic form of phosphatidic acid.
作者信息
Senisterra G A, van Gorkom L C, Epand R M
机构信息
Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.
出版信息
Biochem Biophys Res Commun. 1993 Jan 15;190(1):33-6. doi: 10.1006/bbrc.1993.1006.
PMID:8422258
Abstract
Phosphatidic acid in the form of small unilamellar vesicles has a dissociation constant of about 8.3 as determined by 31P nuclear magnetic resonance (NMR) spectroscopy. The activation of protein kinase C (PKC) by monovalent phosphatidic acid or phosphatidylserine occurs only in the presence of Ca2+. However, PKC activity on membranes of divalent anionic phosphatidic acid is independent of Ca2+ concentration.
摘要
通过31P核磁共振（NMR）光谱测定，小单层囊泡形式的磷脂酸解离常数约为8.3。单价磷脂酸或磷脂酰丝氨酸对蛋白激酶C（PKC）的激活仅在Ca2+存在时发生。然而，二价阴离子磷脂酸膜上的PKC活性与Ca2+浓度无关。
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