The activation of platelets – to stop bleeding by clotting blood vessel injuries – initiates a cascade of signaling inside the platelet that results in the generation of malondialdehyde (MDA). MDA is a reactive molecule that can modify protein structure in vitro, but it was not known if this reaction occurs in platelets.
Olivier Boutaud, Ph.D., and colleagues have now developed a novel chromatography-mass spectrometry method to analyze MDA products. They reported in the Journal of Lipid Research that platelet activation results in the formation of MDA-protein cross-links.
The investigators also demonstrated that these protein modifications are increased in diseases associated with platelet activation, including metabolic syndrome and sickle cell disease. Salicylamine and its analogs – compounds that “scavenge” MDA – prevented the MDA-protein cross-links.
The findings support further study of the contribution of MDA-induced protein modifications to platelet function and suggest the possibility that analysis of MDA-protein cross-links could provide a biomarker for in vivo platelet dysfunction.
This research was supported in part by the Specialized Centers of Clinically Oriented Research in Hemostatic and Thrombotic Diseases (National Institutes of Health grants HL081009, GM087603).
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