Gavrilova N J, Petkova D H
Central Laboratory of Biophysics, Bulgarian Academy of Sciences, Sofia.
J Lipid Mediat Cell Signal. 1995 May;11(3):241-52. doi: 10.1016/0929-7855(94)00041-a.
The role of rat liver plasma membrane phospholipids in the regulation of protein kinase A, protein kinase C and tyrosine kinase activities was investigated. Plasma membrane composition was modified by phospholipase A2, phospholipase C and phospholipase D treatment and subsequent incorporation of various phospholipids. Phospholipase A2 deactivated the three types of protein kinases, while phospholipase C and D affected the enzymes in a different manner. Phosphatidylcholine and sphingomyelin were found to be the most effective activators of protein kinase A and tyrosine kinase. Incorporation of sphingomyelin and phosphatidylserine into partially delipidated plasma membranes resulted in a significant stimulation of protein kinase C activity. Since sphingomyelin appeared to be a specific effector of the three types of protein kinases under investigation, one might suggest that its role in cellular signaling could be manifested via regulation of protein kinase C as well as via modulation of protein kinase A and tyrosine kinase activities.
