E-NTPase/E-NTPDase: a potential regulatory role in E-kinase/PKA-mediated CD36 activation.
CD36 is a platelet surface receptor protein that plays a major role in platelet aggregation and accumulation that is mediated by parasitic attachment. The CD36 receptor is constitutively phosphorylated by E-kinase/PKA, resulting in increased affinity for collagen, but preventing spontaneous platelet aggregation. Dephosphorylation of CD36 by protein phosphatase 2A (PP2A) leads to increased affinity for thrombospondin at a different rate than that of collagen-mediated platelet aggregation. Depletion of the E-kinase/PKA substrate [ATP](0)by E-NTPase-mediated hydrolysis, in conjunction with inhibition of PP2A by okadaic acid, could prove to be a valuable tool in inhibiting CD36 activation, thus preventing platelet aggregation and thrombus formation.
Kannan
Subburaj
S
Department of Medicine, Division of Gastroenterology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6145, USA. sukannan@utmb.edu
D017766:Acid Anhydride Hydrolases / Q000502:physiology*; D000818:Animals; D018955:CD36 Antigens / Q000378:metabolism*; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D043583:Nucleoside-Triphosphatase; D010974:Platelet Aggregation / Q000502:physiology
D018955:CD36 Antigens; D017868:Cyclic AMP-Dependent Protein Kinases; D017766:Acid Anhydride Hydrolases; D043583:Nucleoside-Triphosphatase