A small-molecule compound inhibits a collagen-specific molecular chaperone and could represent a potential remedy for fibrosis.

ABSTRACT: Fibrosis can disrupt tissue structure and integrity and impair organ function. Fibrosis is characterized by abnormal collagen accumulation in the extracellular matrix. Pharmacological inhibition of collagen secretion therefore represents a promising strategy for the management of fibrotic disorders, such as liver and lung fibrosis. Hsp47 is an endoplasmic reticulum (ER)-resident collagen-specific molecular chaperone essential for correct folding of procollagen in the ER. Genetic deletion of Hsp47 or inhibition of its interaction with procollagen interferes with procollagen triple helix production, which vastly reduces procollagen secretion from fibroblasts. Thus, Hsp47 could be a potential and promising target for the management of fibrosis. In this study, we screened small-molecule compou

SUBMITTER: Ito S 

PROVIDER: S-EPMC5723997 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature