Syk interacts with tyrosine-phosphorylated proteins in human platelets activated by collagen and cross-linking of the Fc<i>γ</i>-IIA receptor

Yanaga, Fumi; Poole, Alastair W.; Asselin, J; Blake, Robert A.; Schieven, Gary L.; Clark, Edward A.; Law, Che‐Leung; Watson, S. P.

doi:10.1042/bj3131047

Cited by 43 publications

(53 citation statements)

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“…Analogous cellular activation events are initiated upon FcγR cross-linking in other FcγR-expressing cell types, such as platelets. Indeed, engagement of platelet FcγRIIa by IgG immune complexes triggers platelet activation and degranulation, leading to platelet aggregation and the activation of pro-thrombotic pathways (27,75,76).…”

Section: Diversity Of Fc Effector Functionsmentioning

confidence: 99%

“…In particular, activating Type I FcγR interactions with multivalent IgG immune complexes induce receptor clustering and aggregation that subsequently lead to the recruitment of Syk and Src family kinases at their intracellular domains (17,19,22,26,27). Interactions of these kinases with the ITAMs of activating Type I FcγRs trigger their phosphorylation and the activation of several pro-inflammatory signaling pathways that involve the phosphorylation of diverse families of kinases, actin remodeling, Ca 2+ influx and the up-regulation of genes with pro-inflammatory and pro-survival properties (18,24,(28)(29)(30)(31).…”

Section: Type I and Type Ii Fcγrs: Structural Properties And Functionmentioning

confidence: 99%

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Diversification of IgG effector functions

Bournazos

Ravetch

2017

International Immunology

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Section: Diversity Of Fc Effector Functionsmentioning

confidence: 99%

Section: Type I and Type Ii Fcγrs: Structural Properties And Functionmentioning

confidence: 99%

Diversification of IgG effector functions

Bournazos

Ravetch

2017

International Immunology

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“…65,66 PKC-independent tyrosine phosphorylation of p72 syk has also been observed during platelet aggregation stimulated by fibrillar collagen. 27 Previously, we found that rapid adhesion to collagen under flow conditions primarily mediated by the ␣ 2 ␤ 1 -integrin and in the absence of ␣ IIb ␤ 3 -dependent aggregation was associated with tyrosine phosphorylation of p125 FAK . 25 In the present study, we show that rapid adhesion also resulted in tyrosine phosphorylation of p72 syk .…”

Section: Discussion Platelet Adhesion To Collagen: Activation Of Pkc mentioning

confidence: 99%

“…25,26 Signaling molecules that have been shown to be activated during collagen stimulation include the p72 syk tyrosine kinase. 27 The initial phase of protein tyrosine phosphorylation of several tyrosine kinases depends on prior PKC activation, 28 and it has been proposed that protein tyrosine phosphorylation in platelets occurs after activation of PKC. 29 This suggests that PKC activation may also influence the initial stage of tyrosine phosphorylation of p125 FAK and p72 syk after platelet adhesion.…”

mentioning

confidence: 99%

Activation of Protein Kinase C Is Required for the Stable Attachment of Adherent Platelets to Collagen but Is Not Needed for the Initial Rapid Adhesion Under Flow Conditions

Polanowska-Grabowska

Gear

1999

ATVB

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Abstract-We have investigated the role of protein kinase C (PKC) in the initial events of ␣ 2 ␤ 1 -integrin-mediated platelet adhesion to collagen under flow conditions. Although adhesion caused activation of PKC, as evidenced by pleckstrin phosphorylation, the PKC inhibitors GF 109203X and Gö 6976 had no effect on adhesion, even though they prevented pleckstrin phosphorylation. The initial kinetics and extent of platelet adhesion to collagen (Ͻ5 seconds) and tyrosine phosphorylation of p125 FAK and p72 syk were not influenced by the PKC inhibitors, whereas adhesion to polylysine was prevented. These results indicate that adhesion to collagen and polylysine involve different mechanisms and requirements for PKC activation. Pretreatment with GF 109203X destabilized collagen-adherent platelets, accelerating their detachment, which was associated with tyrosine dephosphorylation of p125 FAK . Thus, although PKC activation was not required for rapid platelet adhesion to collagen, it appears to play an important role in stabilizing the attachment of adherent platelets to collagen. We also examined the effect of PKC activation by the phorbol ester phorbol 12-myristate 13-acetate (PMA) on platelet adhesion to collagen. PMA at 100 nmol/L strongly potentiated adhesion and tyrosine phosphorylation of p125 FAK and p72 syk and activated ␤ 1 -integrins, as determined by increased exposure of the 15/7 epitope. The PMA-stimulated adhesion was partially blocked by an anti-␣ 2 ␤ 1 antibody, was completely inhibited by GF 109203X, and was not correlated with the extent of pleckstrin phosphorylation. Therefore, strong PKC activation may lead to inside-out signaling, enhancing the role of ␤ 1 -integrins in adhesion. Pleckstrin phosphorylation does not appear to be involved in the initial phase of basic or PMA-stimulated adhesion but may help stabilize the adherent platelets. Key Words: platelets Ⅲ adhesion Ⅲ collagen Ⅲ PKC Ⅲ p125 FAK Ⅲ p72 syk P rotein kinase C (PKC) was initially identified as a threonine/serine protein kinase dependent on calcium and phospholipids and known to be activated during the earliest events of signal transduction, tumor promotion, and cell regulation. 1-4 Activation of PKC has been linked to reorganization of the actin cytoskeleton, cell motility, adhesion, and the formation of focal contacts. [5][6][7] The involvement of PKC in cell adhesion to extracellular matrix (ECM) proteins has long been proposed from the observations that direct stimulation of PKC by phorbol esters can activate integrins, potentiating adhesion and spreading, and that inhibitors of PKC prevent adhesion. 8 -13 There is also evidence that direct integrin binding to ECM proteins leads to PKC activation. 9,14 Although stimulation of PKC by phorbol esters can mediate integrin activation and enhance adhesion, there is little evidence that PKC directly regulates these events.Platelets are a good model to study signal transduction events during attachment of cells to ECM proteins or for cell-cell interactions. 15 Several studies suggest th...

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“…GPVI forms a complex with the Fc receptor γ-chain (4,5). Activated GPVI induces the activation of various intracellular molecules, including phospholipase Cγ2 and tyrosine kinase Syk (6,7), resulting in the upregulation of integrin activity (8) and the enhancement of granule secretion (2). Platelet-derived growth factor (PDGF)-AB, which is stored in α-granules of human platelets and is known to exert potent proliferative effects on a variety of cells, is released from activated platelets and has a pivotal role in atherosclerosis via the proliferation of connective tissue, including vascular smooth muscle cells (1).…”

Section: Introductionmentioning

confidence: 99%

AICAR reduces the collagen-stimulated secretion of PDGF-AB and release of soluble CD40 ligand from human platelets: Suppression of HSP27 phosphorylation via p44/p42 MAP kinase

Tsujimoto

Tokuda

Kuroyanagi

et al. 2016

Experimental and Therapeutic Medicine

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Abstract.We have previously reported that collagen-induced phosphorylation of heat shock protein (HSP) 27 via p44/p42 mitogen-activated protein (MAP) kinase in human platelets is sufficient to induce the secretion of platelet-derived growth factor (PDGF)-AB and the release of soluble cluster of differentiation 40 ligand (sCD40L). Adenosine monophosphate-activated protein kinase (AMPK), which is known to regulate energy homeostasis, has a crucial role as an energy sensor in various eukaryotic cells. The present study investigated the effects of 5-aminoimidazole-4-carbox amide-1-β-d-ribofuranosyl 5'-monophosphate (AICAR), which is an activator of AMPK, on the collagen-induced activation of human platelets. It was demonstrated that AICAR dose-dependently reduced collagen-stimulated platelet aggregation up to 1.0 µM. Analysis of the size of platelet aggregates demonstrated that AICAR decreased the ratio of large aggregates (50-70 µm), whereas the ratio of small aggregates (9-25 µm) was increased by AICAR administration. AICAR markedly attenuated the phosphorylation levels of p44/p42 MAP kinase and HSP27, which are induced by collagen.Furthermore, AICAR significantly decreased the secretion of PDGF-AB and the collagen-induced release of sCD40L. These results indicated that AICAR-activated AMPK may reduce the secretion of PDGF-AB and the collagen-induced release of sCD40L by inhibiting HSP27 phosphorylation via p44/p42 MAP kinase in human platelets.

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Syk interacts with tyrosine-phosphorylated proteins in human platelets activated by collagen and cross-linking of the Fcγ-IIA receptor

Cited by 43 publications

References 0 publications

Diversification of IgG effector functions

Diversification of IgG effector functions

Activation of Protein Kinase C Is Required for the Stable Attachment of Adherent Platelets to Collagen but Is Not Needed for the Initial Rapid Adhesion Under Flow Conditions

AICAR reduces the collagen-stimulated secretion of PDGF-AB and release of soluble CD40 ligand from human platelets: Suppression of HSP27 phosphorylation via p44/p42 MAP kinase

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