Calcium-induced proteolysis of spectrin and band 3 protein in rat erythrocyte membranes.
Calcium-dependent protease activity capable of degrading a number of endogenous proteins was found in rat red blood cell membranes. This protease activity, like that found in human red blood cells, was activated by low concentrations of calcium, but in the rat red blood cells, unlike the human red blood cells, calcium-activated protease activity was membrane-bound. A number of endogenous membrane-bound proteins were degraded after the addition of calcium to the membranes. These included spectrin bands 1 and 2 as well as bands 3, 2.1, and 2.2. No calcium-induced aggregation (transglutaminase activity) was noted in the rat red blood cell membranes.
D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism*; D002118:Calcium / Q000494:pharmacology*; D002154:Calpain; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000097:blood; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D013049:Spectrin / Q000378:metabolism*; D013997:Time Factors
D001457:Anion Exchange Protein 1, Erythrocyte; D013049:Spectrin; D010450:Endopeptidases; D002154:Calpain; D002118:Calcium