Structure-function relationship in heart sarcolemma.
Dependence on the membrane lipids of sarcolemmal structure as well as functions was examined by incubating isolated rat heart sarcolemma with phospholipase A, C, or D. Conventional as well as negatively stained electron microscope preparations of the treated membranes revealed structural changes. Ca2+ binding and Na+, K+-ATPase activity were depressed following treatment of the membranes with any of the phospholipases whereas Ca2+-ATPase activity was not affected. Adenylate cyclase activity was increased by low concentration (25 micrograms/mg of protein) of phospholipase A, and a definite inhibition of the enzyme was noticed when the concentration of the phospholipase A was increased to 250 micrograms/mg of protein. Phospholipases C and D had no significant effect on the adenylate cyclase activity. Percentage of phospholipids hydrolyzed was more after phospholipase A treatments. These results provide evidence regarding the involvement of lipids in the membrane structure and functions.
D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000502:physiology; D009206:Myocardium / Q000378:metabolism*; D010739:Phospholipase D / Q000494:pharmacology; D010741:Phospholipases A / Q000494:pharmacology; D010743:Phospholipids; D051381:Rats; D012508:Sarcolemma / Q000201:enzymology / Q000502:physiology* / Q000648:ultrastructure; D010738:Type C Phospholipases / Q000494:pharmacology
D010743:Phospholipids; D010741:Phospholipases A; D010738:Type C Phospholipases; D010739:Phospholipase D; D002118:Calcium