ArticleJournal of thrombosis and haemostasis : JTH2022
Protein disulfide isomerase-A1 regulates intraplatelet reactive oxygen species-thromboxane A
Article in Journal of thrombosis and haemostasis : JTH, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Donor sex and platelet storage change the therapeutic effects of platelet-derived extracellular vesicles on endothelium.Blood vessels, thrombosis & hemostasis · 2026Article
- The crucial role of thromboxane AFrontiers in pharmacology · 2026Review
- Extracellular PDI in thrombosis and vascular injury.Thrombosis journal · 2025Review
- Anti-Thrombotic Effects ofNutrients · 2025Article
- Platelets welcome a new protein disulfide isomerase family member.Journal of thrombosis and haemostasis : JTH · 2025Article
- Beyond Blood Clotting: The Many Roles of Platelet-Derived Extracellular Vesicles.Biomedicines · 2024Review
- Recent advances in vascular thiol isomerases and redox systems in platelet function and thrombosis.Journal of thrombosis and haemostasis : JTH · 2024Review
- Protein disulfide isomerase A1 regulates fenestration dynamics in primary mouse liver sinusoidal endothelial cells (LSECs).Redox biology · 2024Article
- Sulfenylation links oxidative stress to protein disulfide isomerase oxidase activity and thrombus formation.Journal of thrombosis and haemostasis : JTH · 2023Article
- An Overview of Two Old Friends Associated with Platelet Redox Signaling, the Protein Disulfide Isomerase and NADPH Oxidase.Biomolecules · 2023Article
- Protein disulfide isomerase-A1 regulates intraplatelet reactive oxygen species-thromboxane AJournal of thrombosis and haemostasis : JTH · 2022Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPlatelet-derived protein disulfide isomerase 1 (PDIA1) regulates thrombus formation, but its role in the regulation of platelet function is not fully understood.
aimsThe aim of this study was to characterize the role of PDIA1 in human platelets.
methodsProteomic 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 A
resultsPDIA1 was less abundant compared with PDIA3 in resting platelets and platelets stimulated with TRAP-14, collagen, or ADP. Collagen, but not ADP, induced a significant increase in PDIA1 expression. Bepristat potently inhibited the aggregation of washed platelets induced by collagen or convulxin, but only weakly inhibited platelet aggregation induced by TRAP-14 or thrombin, and had the negligible effect on platelet aggregation induced by arachidonic acid. Inhibition of PDIA1 by bepristat resulted in the reduction of TxA
conclusionsPDIA1 acts as an intraplatelet regulator of the ROS-TxA
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