Activation of Ca2+-stimulated ATPase by phospholipid N-methylation in cardiac sarcoplasmic reticulum.
Incubation of cardiac sarcoplasmic reticulum (SR) in the presence of S-adenosyl-L-methionine, a methyl donor for the enzymatic N-methylation of phosphatidylethanolamine, increased Ca2+-stimulated ATPase activity. The increase in Ca2+-ATPase activity was not due to changes in the affinity for Ca2+ and was prevented by methyl acetimidate, an inhibitor of phospholipid N-methylation. The results suggest a possible regulatory role of phospholipid N-methylation in SR Ca2+-pump mechanism.
Ganguly
P K
PK
Panagia
V
V
Okumura
K
K
Dhalla
N S
NS
D000818:Animals; D001693:Biological Transport, Active; D002118:Calcium / Q000378:metabolism; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D002474:Cell-Free System; D004789:Enzyme Activation; D007096:Imidoesters / Q000494:pharmacology; D008563:Membrane Lipids / Q000378:metabolism; D008745:Methylation; D009206:Myocardium / Q000201:enzymology*; D010713:Phosphatidylcholines / Q000378:metabolism*; D010714:Phosphatidylethanolamines / Q000378:metabolism*; D051381:Rats; D012436:S-Adenosylmethionine / Q000378:metabolism; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*
D007096:Imidoesters; D008563:Membrane Lipids; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D012436:S-Adenosylmethionine; C010222:methyl acetimidate; D000252:Calcium-Transporting ATPases; D002118:Calcium