Modulation of cofactor requirement for the activation of protein kinase C by heparin. Possible effect at the regulatory domain.
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 abolished 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.
Goueli
S A
SA
Cellular and Molecular Biochemistry Laboratory (151), University of Minnesota School of Medicine, Minneapolis.
Hanten
J A
JA
Ahmed
K
K
D000818:Animals; D004789:Enzyme Activation; D006493:Heparin / Q000494:pharmacology*; D006657:Histones / Q000378:metabolism; D008297:Male; D010718:Phosphatidylserines / Q000378:metabolism; D011467:Prostate / Q000201:enzymology; D011479:Protamines / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D014357:Trypsin / Q000494:pharmacology
D006657:Histones; D010718:Phosphatidylserines; D011479:Protamines; D006493:Heparin; D011493:Protein Kinase C; D014357:Trypsin