What role do heat-shock proteins play in regulating platelet function and preventing thrombosis?
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Heat-shock proteins (HSPs) play crucial roles in regulating platelet function and preventing thrombosis. HSP70, a member of the HSP family, is highly expressed in platelets and is involved in platelet aggregation, granule secretion, and integrin activation . Inhibition of HSP70 leads to reduced platelet aggregation and integrin activation, hindering thrombus formation. Moreover, extracellular HSP72 promotes platelet aggregation, potentially contributing to thrombus formation in conditions like acute myocardial infarction. HSPs, including HSP70, are essential for maintaining hemostasis and regulating platelet activation through intracellular signaling pathways, highlighting their significance in preventing thrombosis and ensuring proper platelet function. Additionally, HSPs have been implicated in immune responses and have potential applications in cancer therapy and heart disease treatment .
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43 Citations | Not addressed in the paper. |
7 Citations | Heat-shock protein 72 (HSP72) promotes platelet aggregation induced by various activators, potentially contributing to thrombus formation, while anti-HSP72 antibodies may help control HSP72-induced platelet aggregation. |
| Heat shock protein 70 (Hsp70) regulates platelet activation, granule secretion, integrin activation, and aggregation, suggesting a crucial role in maintaining hemostasis and preventing thrombosis. | |
| Heat-shock proteins (HSPs) play roles in protein folding, cell protection, and immune responses, but their specific role in regulating platelet function and preventing thrombosis is not addressed in the paper. | |
01 Jan 2018 5 Citations | Heat shock protein 70 (Hsp70) plays a critical role in regulating platelet function by influencing intracellular signaling events, including integrin conformational changes, which can help prevent thrombosis. |
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