Platelet surface thiol isomerases

Platelet thiol-dependent targets refer to a functional group of proteins on the platelet surface that regulate haemostasis and thrombosis through thiol-disulfide exchange reactions. This group primarily includes the thiol isomerase family of enzymes, such as protein disulfide isomerase (PDI), ERp5, and ERp57, which are released from intracellular stores upon platelet activation and relocate to the cell surface. These enzymes catalyze the rearrangement of disulfide bonds in critical surface receptors, including integrin alpha-IIb/beta-3 (GPIIb/IIIa) and the P2Y12 receptor, facilitating their transition to active conformations required for aggregation. Additionally, certain antiplatelet drugs like thienopyridines (e.g., clopidogrel) target these pathways by forming covalent disulfide bonds with cysteine residues on receptors. Modulating the redox state of these platelet surface targets represents a promising therapeutic strategy for treating cardiovascular diseases while potentially offering a wider safety window regarding bleeding risks compared to traditional antiplatelet therapies.

Other names

Platelet thiol-dependent targetsPlatelet surface thiolsPlatelet redox targetsThiol-disulfide exchange proteins

Inhibition of platelet function through the modulation of thiol-disulfide exchange or covalent modification of cysteine residues on the platelet surface.