HPW-RX40 prevents human platelet activation by attenuating cell surface protein disulfide isomerases.

ABSTRACT: Protein disulfide isomerase (PDI) present at platelet surfaces has been considered to play an important role in the conformational change and activation of the integrin glycoprotein IIb/IIIa (GPIIb/IIIa) and thus enhances platelet aggregation. Growing evidences indicated that platelet surface PDI may serve as a potential target for developing of a new class of antithrombotic agents. In the present study, we investigated the effects of HPW-RX40, a chemical derivative of β-nitrostyrene, on platelet activation and PDI activity. HPW-RX40 inhibited platelet aggregation, GPIIb/IIIa activation, and P-selectin expression in human platelets. Moreover, HPW-RX40 reduced thrombus formation in human whole blood under flow conditions, and protects mice from FeCl₃-induced carotid artery occlus

SUBMITTER: Kung PH 

PROVIDER: S-EPMC5466588 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature