Protein disulfide isomerase-A1 regulates intraplatelet reactive oxygen species-thromboxane A₂ -dependent pathway in human platelets.

ABSTRACT:

Background

Platelet-derived protein disulfide isomerase 1 (PDIA1) regulates thrombus formation, but its role in the regulation of platelet function is not fully understood.

Aims

The aim of this study was to characterize the role of PDIA1 in human platelets.

Methods

Proteomic analysis of PDI isoforms in platelets was performed using liquid chromatography tandem mass spectometry, and the expression of PDIs on platelets in response to collagen, TRAP-14, or ADP was measured with flow cytometry. The effects of bepristat, a selective PDIA1 inhibitor, on platelet aggregation, expression of platelet surface activation markers, thromboxane A₂ (TxA₂ ), and reactive oxygen species (ROS) generation were evaluated by optical aggregometry, flow cytometry, ELIS

SUBMITTER: Przyborowski K 

PROVIDER: S-EPMC9292974 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature