Modulation of cofactor requirement for the activation of protein kinase C by heparin Possible effect at the regulatory domain

FEBS Letters

Ahmed, Khalil¹  Hanten, John A.¹  Goueli, Said A.¹ 

[1] Cellular and Molecular Biochemistry Laboratory (151) and Department of Laboratory Medicine and Pathology, University of Minnesota School of Medicine, USA

关键词: Protein kinase C;    Heparin;    Phosphorylation;    Regulatory domain;   

DOI  :  10.1016/0014-5793(91)80533-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Heparin was found to stimulate the phosphorylation of histone H1 but not protamine sulfate catalyzed by Ca²⁺/phospholipid-dependent protein kinase (protein kinase C or PKC). The effect of heparin on histone H1 phosphorylation appeared to be due to an increase in phosphatidylserine affinity for PKC activation in the presence of heparin. This effect of heparin was abolisched when trypsinized, cofactor-independent, PKC was employed to phosphorylate histone H1. These studies suggest that heparin acts at the regulatory domain of PKC, and emphasize the importance of the negative charge in influencing the accessibility of the substrate to PKC action

【 授权许可】

Unknown