Association of a phospholipase A2 (14-3-3 protein) with the platelet glycoprotein Ib-IX complex.
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.
Mesh Terms:
14-3-3 Proteins, Amino Acid Sequence, Chromatography, Affinity, Electrophoresis, Polyacrylamide Gel, Humans, Immunoblotting, Molecular Sequence Data, Molecular Weight, Nerve Tissue Proteins, Phospholipases A, Phospholipases A2, Platelet Membrane Glycoproteins, Protein Binding, Sequence Homology, Amino Acid, Tyrosine 3-Monooxygenase
14-3-3 Proteins, Amino Acid Sequence, Chromatography, Affinity, Electrophoresis, Polyacrylamide Gel, Humans, Immunoblotting, Molecular Sequence Data, Molecular Weight, Nerve Tissue Proteins, Phospholipases A, Phospholipases A2, Platelet Membrane Glycoproteins, Protein Binding, Sequence Homology, Amino Acid, Tyrosine 3-Monooxygenase
J. Biol. Chem.
Date: Jul. 15, 1994
PubMed ID: 8034572
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