Role of heat shock protein 47 in platelet glycoprotein VI dimerization and signaling.

ABSTRACT:

Background

Heat shock protein 47 (HSP47) is an intracellular chaperone protein with an indispensable role in collagen biosynthesis in collagen-secreting cells. This chaperone has also been shown to be released and present on the surface of platelets. The inhibition of HSP47 in human platelets or its ablation in mouse platelets reduces platelet function in response to collagen and the glycoprotein (GP) VI collagen receptor agonist CRP-XL.

Objectives

In this study, we sought, through experiments, to explore cellular distribution, trafficking, and influence on GPVI interactions to understand how HSP47 modulates collagen receptor signaling.

Methods

HSP47-deficient mouse platelets and SMIH- treated human platelets were used to study the role of HSP47 in collagen mediated r

SUBMITTER: AlOuda SK 

PROVIDER: S-EPMC10520510 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature