The chaperone protein HSP47: a platelet collagen binding protein that contributes to thrombosis and hemostasis.

ABSTRACT: Essentials Heat shock protein 47 (HSP47), a collagen specific chaperone is present on the platelet surface. Collagen mediated platelet function was reduced following blockade or deletion of HSP47. GPVI receptor regulated signalling was reduced in HSP47 deficient platelets. Platelet HSP47 tethers to exposed collagen thus modulating thrombosis and hemostasis.

Summary

Objective Heat shock protein 47 (HSP47) is an intracellular chaperone protein that is vital for collagen biosynthesis in collagen secreting cells. This protein has also been shown to be present on the surface of platelets. 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. Methods and Result

SUBMITTER: Sasikumar P 

PROVIDER: S-EPMC6434988 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature