Insulin inhibits the phosphorylation of the membrane cytoskeletal protein spectrin in pig erythrocytes.
Incubation of either ghost membranes with 32P- -ATP or intact erythrocytes with 32P-inorganic phosphate led to phosphorylation of the beta-chain of the major membrane-associated protein spectrin. This phosphorylation was reduced by 30% by insulin (10-100 microU/ml) both in membranes and in intact cells. The results show that the membrane-cytoskeleton is responsive to extracellular signals such as hormone receptor activation.
D000818:Animals; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism; D004912:Erythrocytes / Q000187:drug effects / Q000378:metabolism*; D007328:Insulin / Q000494:pharmacology*; D007700:Kinetics; D010766:Phosphorylation; D013049:Spectrin / Q000378:metabolism*; D013552:Swine
D007328:Insulin; D013049:Spectrin