Protein tyrosine phosphorylation in human platelets induced by interaction between glycoprotein Ib and von Willebrand factor

Ozaki, Yukio; Satoh, Kaneo; Yatomi, Yutaka; Miura, S.; Fujimura, Yoshihiro; Kudoh, Shoji

doi:10.1016/0304-4165(94)00178-z

Cited by 50 publications

(46 citation statements)

References 27 publications

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“…Such phosphorylation was not affected by preincubation of intact platelets with control IgG but was almost totally blocked by the anti-Fc␥RIIA mAb IV. 3. Fig.…”

Section: Effect Of the Blockage Of Fc␥riia And Of The Inhibition Of Smentioning

confidence: 99%

“…Under conditions of high shear stress or in the presence of modulators like ristocetin or botrocetin, vWF binds to the platelet membrane GPIb-IX-V and initiates signals leading to platelet activation (1). This process involves the activation of PLC and PLA 2 , the cytoskeleton reorganization and the interaction of several signaling molecules with the actin filaments, the tyrosine phosphorylation of several proteins, the activation of GPIIb-IIIa, and leads to platelet secretion and aggregation (2)(3)(4)(5)(6)(7). Some of these events, such as the activation of PLC, have been demonstrated to be promoted by the secondary action of TxA 2 produced from arachidonic acid through the cyclooxygenase pathway (2).…”

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confidence: 99%

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Platelet Activation by von Willebrand Factor Requires Coordinated Signaling through Thromboxane A2 and FcγIIA Receptor

Canobbio¹,

Bertoni²,

Lova³

et al. 2001

Journal of Biological Chemistry

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“…Such phosphorylation was not affected by preincubation of intact platelets with control IgG but was almost totally blocked by the anti-Fc␥RIIA mAb IV. 3. Fig.…”

Section: Effect Of the Blockage Of Fc␥riia And Of The Inhibition Of Smentioning

confidence: 99%

mentioning

confidence: 99%

Platelet Activation by von Willebrand Factor Requires Coordinated Signaling through Thromboxane A2 and FcγIIA Receptor

Canobbio¹,

Bertoni²,

Lova³

et al. 2001

Journal of Biological Chemistry

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“…However, several studies have examined GPIb-V-IX in vitro using flow-based assay systems (Nesbitt et al, 2002;Yap et al, 2000). GPIb binding is associated with the stimulation of tyrosine kinase signalling (Asazuma et al, 1997;Ozaki et al, 1995;Razdan et al, 1994). Principal players in this pathway include the non-receptor tyrosine kinases Src, Fyn, Lyn and Syk, phospholipase Cγ2 (PLCγ2), and adaptor proteins such as Shc, linker for activation of T cells (LAT) and SLP-76 (Asazuma et al, 1997;Falati et al, 1999;Jackson et al, 1994;Marshall et al, 2002;Torti et al, 1999;Wu et al, 2001).…”

Section: Signalling Through Gpibmentioning

confidence: 99%

Platelet adhesion signalling and the regulation of thrombus formation

Gibbins

2004

Journal of Cell Science

259

232

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Platelets perform a central role in haemostasis and thrombosis. They adhere to subendothelial collagens exposed at sites of blood vessel injury via the glycoprotein (GP) Ib-V-IX receptor complex, GPVI and integrin α2β1. These receptors perform distinct functions in the regulation of cell signalling involving non-receptor tyrosine kinases (e.g. Src, Fyn, Lyn, Syk and Btk), adaptor proteins, phospholipase C and lipid kinases such as phosphoinositide 3-kinase. They are also coupled to an increase in cytosolic calcium levels and protein kinase C activation, leading to the secretion of paracrine/autocrine platelet factors and an increase in integrin receptor affinities. Through the binding of plasma fibrinogen and von Willebrand Factor to integrin αIIbβ3, a platelet thrombus is formed. Although increasing evidence indicates that each of the adhesion receptors GPIb-V-IX and GPVI and integrins α2β1 and αIIbβ3 contribute to the signalling that regulates this process, the individual roles of each are only beginning to be dissected. By contrast, adhesion receptor signalling through platelet endothelial cell adhesion molecule 1 (PECAM-1) is implicated in the inhibition of platelet function and thrombus formation in the healthy circulation. Recent studies indicate that understanding of platelet adhesion signalling mechanisms might enable the development of new strategies to treat and prevent thrombosis.

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“…In activated platelets, vWF can also interact with GP IIb-IIIa through a RGD-containing sequence (15). Binding of soluble vWF to GP Ib-IX-V complex induces platelet activation associated with arachidonic acid release, Ca 2ϩ mobilization, and protein tyrosine phosphorylation (16,17). Moreover, it has been demonstrated that vWF stimulates the association of pp60 src and phosphatidylinositol 3-kinase with the intracellular cytoskeleton through a mechanism independent of GP IIb-IIIa (18).…”

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confidence: 99%

Rap1B and Rap2B Translocation to the Cytoskeleton by von Willebrand Factor Involves FcγII Receptor-mediated Protein Tyrosine Phosphorylation

Torti¹,

Bertoni²,

Canobbio³

et al. 1999

Journal of Biological Chemistry

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Stimulation of human platelets with von Willebrand factor (vWF) induced the translocation of the small GTPases Rap1B and Rap2B to the cytoskeleton. This effect was specifically prevented by an anti-glycoprotein Ib monoclonal antibody or by the omission of stirring, but was not affected by the peptide RGDS, which antagonizes binding of adhesive proteins to platelet integrins. Association of Rap2B with the cytoskeleton was very rapid, while translocation of Rap1B occurred in a later phase of platelet activation and was totally inhibited by cytochalasin D. vWF also induced the rapid tyrosine phosphorylation of several proteins that was prevented by the tyrosine kinases inhibitor genistein and by cAMP-increasing agents. Under these conditions, also the association of Rap1B and Rap2B with the cytoskeleton was prevented. Translocation of Rap proteins to the cytoskeleton induced by vWF, but not by thrombin, was inhibited by a monoclonal antibody against the Fc␥II receptor. The same antibody inhibited vWF-induced tyrosine phosphorylation of selected substrates with molecular masses of about 75, 95, and 150 kDa. Three of these substrates were identified as the tyrosine kinase pp72 syk , the phospholipase C␥2, and the inositol 5-phosphatase SHIP. Our results indicate that translocation of Rap1B and Rap2B to the cytoskeleton is regulated by tyrosine kinases and suggest a novel role for the Fc␥II receptor in the mechanism of platelet activation by vWF.Rap proteins are low molecular weight GTP-binding proteins that share about 50% sequence homology with the product of the ras protooncogene. Human platelets express two members of the Rap family of proteins, Rap1B and Rap2B, which are located at the membrane as a consequence of post-translational modifications, including isoprenylation, proteolysis, and carboxylmethylation (1). The role of Rap1B and Rap2B in platelet function is still poorly understood. Rap1B is phosphorylated by the cAMP-dependent protein kinase A (PKA) 1 (2) and is rapidly activated upon platelet stimulation with extracellular agonists (3, 4). By contrast, Rap2B is not a substrate for PKA (5), and its activation upon cell stimulation has not been reported. In thrombin-treated platelets both Rap1B and Rap2B translocate to the cytoskeleton (6, 7). This actin-based structure is not only responsible for the morphological changes of activated platelets, but also represents a network connecting several molecules involved in signal transduction processes, including protein-tyrosine kinases, lipid metabolizing enzymes, and membrane glycoproteins (8). Translocation of Rap2B to the cytoskeleton in thrombin-stimulated platelets requires cell aggregation and is promoted by secondary signals generated by binding of fibrinogen to the membrane glycoprotein IIb-IIIa (GP IIb-IIIa) (9). Similarly, fibrinogen binding to GP IIb-IIIa strongly supports Rap1B translocation to the cytoskeleton, although a small amount of this protein associates with the actin-based structures, even in activated cells in the absence of aggregation a...

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Protein tyrosine phosphorylation in human platelets induced by interaction between glycoprotein Ib and von Willebrand factor

Cited by 50 publications

References 27 publications

Platelet Activation by von Willebrand Factor Requires Coordinated Signaling through Thromboxane A2 and FcγIIA Receptor

Platelet Activation by von Willebrand Factor Requires Coordinated Signaling through Thromboxane A2 and FcγIIA Receptor

Platelet adhesion signalling and the regulation of thrombus formation

Rap1B and Rap2B Translocation to the Cytoskeleton by von Willebrand Factor Involves FcγII Receptor-mediated Protein Tyrosine Phosphorylation

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