Chaperone proteins3/30/2023 The presence of HSP47 on the surface of primary megakaryocytes isolated from mouse bone marrow was demonstrated using epi‐fluorescence microscopy under non‐permeabilizing conditions using rabbit monoclonal anti‐ HSP47 antibody. HSP47 is present on the surface of platelet progenitor primary megakaryocytes and platelets. on behalf of International Society on Thrombosis and Haemostasis. Journal of Thrombosis and Haemostasis published by Wiley Periodicals, Inc. HSP47 chaperone hemostasis platelets thrombosis. Conclusions Our study demonstrates the presence of HSP47 on the platelet surface, where it interacts with collagen, stabilizes platelet adhesion and increases collagen-mediated signalling and therefore thrombus formation and hemostasis. ![]() Laser-induced thrombosis in cremaster muscle arterioles was reduced and bleeding time was prolonged in HSP47-deficient mice or following inhibition of HSP47. Platelet adhesion under flow to von Willebrand factor was unaltered following HSP47 inhibition. Thrombus formation on collagen, under arterial flow conditions, was also decreased following the inhibition or deletion of HSP47, in the presence or absence of eptifibatide, consistent with a role for HSP47 in enhancing platelet adhesion to collagen. In the absence of functional HSP47, the interaction of collagen with platelets was reduced, and this was associated with reduced GPVI-collagen binding, signalling and platelet activation. Methods and Results The deletion of HSP47 in mouse platelets or its inhibition in human platelets reduced their function in response to collagen and the GPVI agonist (CRP-XL), but responses to thrombin were unaltered. Given the importance of collagen and its interactions with platelets in triggering hemostasis and thrombosis, in this study we sought to characterize the role of HSP47 in these cells. This protein has also been shown to be present on the surface of platelets. Objective Heat shock protein 47 (HSP47) is an intracellular chaperone protein that is vital for collagen biosynthesis in collagen secreting cells. Platelet HSP47 tethers to exposed collagen thus modulating thrombosis and hemostasis. GPVI receptor regulated signalling was reduced in HSP47 deficient platelets. Collagen mediated platelet function was reduced following blockade or deletion of HSP47. We suggest that these findings provide the rationale for the mechanism of how these proteins avert the adverse effects of dehydration stresses.Essentials Heat shock protein 47 (HSP47), a collagen specific chaperone is present on the platelet surface. ![]() Our results show that these intrinsically disordered proteins have chaperone activity of rather wide substrate specificity and that they interact with phospholipid vesicles through electrostatic forces. Membrane binding is strongly influenced by ionic strength. It is also demonstrated that ERD10 and ERD14 bind to acidic phospholipid vesicles without significantly affecting membrane fluidity. ![]() ERD10 and ERD14 are able to prevent the heat-induced aggregation and/or inactivation of various substrates, such as lysozyme, alcohol dehydrogenase, firefly luciferase, and citrate synthase. Here, detailed evidence is provided that ERD10 and ERD14 belong to the family of intrinsically disordered proteins, and it is shown in various assays that they act as chaperones in vitro. Whereas these proteins protect cells against the consequences of dehydration, the exact mode(s) of their action remains poorly understood. ERD10 and ERD14 (for early response to dehydration) proteins are members of the dehydrin family that accumulate in response to abiotic environmental stresses, such as high salinity, drought, and low temperature, in Arabidopsis (Arabidopsis thaliana).
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