Abstract
Ca 2+-ATPase activity in human erythrocytes is increased by the enzymatic methylation of membrane phospholipids. Erythrocyte membranes incubated in the presence of the methyl donor, S-adenosyl-L-methionine, demonstrate increased Ca 2+ stimulated ATP hydrolysis, increased [ 45Ca 2+] efflux from erythrocyte ghosts and synthesis of phosphatidyl-N-monomethylethanolamine. The increase in Ca 2+-ATPase activity is due to an increase in Vmax, and not due to changes in affinity for ATP or Ca 2+. The concentration of S-adenosyl-L-methionine needed to stimulate Ca 2+-ATPase closely matches that needed for the methylation of phosphatidylethanolamine. Both the stimulation of Ca 2+-ATPase and the methylation of phospholipids are inhibited by the methyltransferase inhibitor, S-adenosyl-L-homocysteine. Membrane fluidity is increased by phospholipid methylation, which may be the mechanism for Ca 2+-ATPase stimulation.
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