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• W50345765 endingPage "e285" @default.
• W50345765 startingPage "e276" @default.
• W50345765 abstract "Background Glycoprotein VI (GPVI) /Fc receptor gamma (FcRγ)-chain complex is one of the collagen receptors in platelets and responsible for the majority of the intracellular signaling events through a similar pathway to immune receptors. Src-like adaptor protein 2 (SLAP-2) is a recently characterized adaptor protein predominantly expressed in hematopoietic cells. In T cells, SLAP-2 was reported to associate with several tyrosine phosphorylated proteins, and function as a negative regulator of signaling downstream of T cell antigen receptor by virtue of its interaction with the ubiquitin ligase c-Cbl. But the data regarding the presence and role of SLAP-2 proteins in platelets is limited. Objectives We describe the characterization of SLAP-2 in human platelets. Methods Human platelets were analyzed by Western blot analysis, immunoprecipitation, and pull down assay, etc. Results Immunoprecipitation revealed the presence of two forms of SLAP-2 with approximately 28kD and 25kD, and following stimulation of GPVI, the additional form with approximately 32kD apppeared. We have found that upon GPVI activation, SLAP-2 translocated from the Triton X-100-soluble fraction to the Triton X-100-insoluble cytoskeleton fraction, with concomitant association with Syk, c-Cbl, and LAT. Conclusions SLAP-2 appears to play a role in regulating signaling pathways by bringing important signaling molecules such as c-Cbl and Syk into proximity of cytoskeletal substrates. In platelets, SLAP-2 may have function as a negative regulator of GPVI-mediated signaling by interacting with c-Cbl, being similar to that reported in T cells." @default.
• W50345765 created "2016-06-24" @default.
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• W50345765 date "2010-10-01" @default.
• W50345765 modified "2023-10-16" @default.
• W50345765 title "Roles of Src-like adaptor protein 2 (SLAP-2) in GPVI-mediated platelet activation" @default.
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• W50345765 doi "https://doi.org/10.1016/j.thromres.2010.07.010" @default.
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