Background: Changes in integrin αIIbβ3 binding affinity occur in strongly stimulated platelets. Results: Platelet mitochondrial permeability transition pore formation enhances calpain activity, which leads to integrin β3-associated proteolytic cleavage and integrin inactivation. Conclusion: Mitochondrially mediated integrin αIIbβ3 inactivation limits platelet aggregation and thrombus growth. Significance: Modulation of this pathway may offer a novel alternative for the prevention of thrombosis. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
CITATION STYLE
Liu, F., Gamez, G., Myers, D. R., Clemmons, W., Lam, W. A., & Jobe, S. M. (2013). Mitochondrially mediated integrin αiIbβ3 protein inactivation limits thrombus growth. Journal of Biological Chemistry, 288(42), 30672–30681. https://doi.org/10.1074/jbc.M113.472688
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