Du X, Harris S J, Tetaz T J, Ginsberg M H, Berndt M C
Department of Vascular Biology, Scripps Research Institute, La Jolla, California 92037.
J Biol Chem. 1994 Jul 15;269(28):18287-90.
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.
血小板与内皮下血管性血友病因子的黏附涉及血小板糖蛋白（GP）Ib-IX的受体识别，并启动有助于初级止血的激活信号。我们在此表明，GPIb-IX与一种细胞内29 kDa的蛋白质特异性相关。该蛋白质的物理化学特性和氨基酸序列表明，它与人类ζ-亚型14-3-3蛋白质相同，先前被鉴定为血小板磷脂酶A2（PLA2）。由于PLA2的激活是GPIb-IX介导信号传导中的早期事件，这一结果表明GPIb-IX的配体占据可能直接激活PLA2，从而导致血小板激活。
