Calcium-independent activation of protein kinase C by the dianionic form of phosphatidic acid.
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.
Senisterra
G A
GA
Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.
van Gorkom
L C
LC
Epand
R M
RM
D002118:Calcium / Q000494:pharmacology*; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008081:Liposomes; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D010712:Phosphatidic Acids / Q000494:pharmacology*; D010718:Phosphatidylserines / Q000494:pharmacology; D010758:Phosphorus; D011493:Protein Kinase C / Q000378:metabolism*
D008081:Liposomes; D010712:Phosphatidic Acids; D010718:Phosphatidylserines; D010758:Phosphorus; D011493:Protein Kinase C; D002118:Calcium