Calcium-dependent proteolysis of actin during storage of platelet concentrates.
In an ongoing study of the changes that occur in platelet concentrates during storage, we investigated two 28-26-Kd proteins designated SP-1 and SP-2, respectively, which increase markedly during blood-bank storage of platelet concentrates at room temperature. Formation of SP-1 and SP-2 was inhibited by storage at 4 degrees C as well as by treatment of the concentrates with leupeptin, N-ethylmaleimide, and EDTA; DFP and PPACK had no effect. The calcium ionophore A23187 markedly stimulated production of SP-1 and SP-2. After partial purification, the two proteins were found to be associated with platelet cytoskeletal protein. Two-dimensional peptide mapping and amino acid sequencing identified SP-1 and SP-2 as fragments of actin formed by cleavage on the N-terminal side of residues Thr-106 and Ala-114, respectively. Generation of SP-1 and SP-2 during storage of platelet concentrate is likely attributable to calcium-dependent neutral protease degradation of actin and may have implications for development of the platelet storage lesion.[1]References
- Calcium-dependent proteolysis of actin during storage of platelet concentrates. Snyder, E.L., Horne, W.C., Napychank, P., Heinemann, F.S., Dunn, B. Blood (1989) [Pubmed]
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