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J Biol Chem. 1994 Jul 15;269(28):18287-90.

Association of a phospholipase A2 (14-3-3 protein) with the platelet glycoprotein Ib-IX complex.

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  • 1Department of Vascular Biology, Scripps Research Institute, La Jolla, California 92037.


Platelet adhesion to subendothelial von Willebrand factor involves receptor recognition by the platelet glycoprotein (GP) Ib-IX and initiates activation signals that contribute to primary hemostasis. We show here that GPIb-IX is specifically associated with an intracellular 29-kDa protein. The physicochemical characteristics and amino acid sequence of this protein indicate that it is identical to the human zeta-isoform 14-3-3 protein, previously characterized as a platelet phospholipase A2 (PLA2). As activation of PLA2 is an early event in GPIb-IX-mediated signaling, this result suggests that ligand occupancy of GPIb-IX may directly activate PLA2, leading to platelet activation.

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