Regulation of protein kinase C activity by various lipids.
Protein kinase C has recently attracted considerable attention because of its importance in the control of cell division, cell differentiation, and signal transduction across the cell membrane. The activity of this enzyme is altered by several lipids such as diacylglycerol, free fatty acids, lipoxins, gangliosides, and sulfatides. These lipids may interact with protein kinase C either directly or through calcium ions and produce their regulatory effect (activation or inhibition) on the activities of the enzymes phosphorylated by this kinase. These processes widen our perspective of the regulation of intercellular and intracellular communication.
D000818:Animals; D004075:Diglycerides / Q000494:pharmacology / Q000502:physiology; D005227:Fatty Acids / Q000494:pharmacology / Q000502:physiology; D005732:Gangliosides / Q000494:pharmacology / Q000502:physiology; D008055:Lipids / Q000494:pharmacology / Q000502:physiology*; D010703:Phorbol Esters / Q000494:pharmacology / Q000502:physiology; D011493:Protein Kinase C / Q000378:metabolism* / Q000502:physiology; D013433:Sulfoglycosphingolipids / Q000494:pharmacology / Q000502:physiology
D004075:Diglycerides; D005227:Fatty Acids; D005732:Gangliosides; D008055:Lipids; D010703:Phorbol Esters; D013433:Sulfoglycosphingolipids; D011493:Protein Kinase C