The Role of HSP47 in Thrombotic Disorders: Molecular Mechanism and Therapeutic Potential.

This review aims to analyze the role of heat shock protein 47 (HSP47) in thrombosis and evaluate its potential as a therapeutic target for deep vein thrombosis (DVT). A systematic literature review was conducted using PubMed, Scopus, and Web of Science to identify studies on HSP47, thrombosis, and collagen, selecting only relevant and methodologically rigorous articles. HSP47 regulates platelet function and collagen interaction, playing a key role in deep vein thrombosis (DVT). HSP47, known for stabilizing collagen, also improves platelet-collagen binding and thrombus formation. In addition, reduced HSP47 levels reduce platelet adhesion, resulting in reduced thrombus formation, while inhibitors that target HSP47 decrease platelet aggregation in animal models. Naturally low levels of HSP47 during prolonged immobility are also found in hibernating mammals, such as bears, and are associated with reduced formation of thrombi, indicating a possible natural mechanism of thrombo-protection. This observation could inform new therapeutic approaches. Current studies use in vitro platelet aggregation assays, flow chamber assays, and collagen binding studies to investigate the role of HSP47 in clotting. This review aims to synthesize existing evidence to better understand HSP47's role in clot formation and explore its potential as a target for novel DVT therapies.