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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.

    Du X, Harris SJ, Tetaz TJ, Ginsberg MH, Berndt MC.

    Department 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.

    PMID: 8034572 [PubMed - indexed for MEDLINE]

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