Regulation of platelet activation and thrombus formation by reactive oxygen species

Jianlin Qiao*, Jane F. Arthur, Elizabeth E. Gardiner, Robert K. Andrews, Lingyu Zeng, Kailin Xu

*Corresponding author for this work

    Research output: Contribution to journalShort surveypeer-review

    180 Citations (Scopus)

    Abstract

    Reactive oxygen species (ROS) are generated within activated platelets and play an important role in regulating platelet responses to collagen and collagen-mediated thrombus formation. As a major collagen receptor, platelet-specific glycoprotein (GP)VI is a member of the immunoglobulin (Ig) superfamily, with two extracellular Ig domains, a mucin domain, a transmembrane domain and a cytoplasmic tail. GPVI forms a functional complex with the Fc receptor γ-chain (FcRγ) that, following receptor dimerization, signals via an intracellular immunoreceptor tyrosine-based activation motif (ITAM), leading to rapid activation of Src family kinase signaling pathways. Our previous studies demonstrated that an unpaired thiol in the cytoplasmic tail of GPVI undergoes rapid oxidation to form GPVI homodimers in response to ligand binding, indicating an oxidative submembranous environment in platelets after GPVI stimulation. Using a redox-sensitive fluorescent dye (H2DCF-DA) in a flow cytometric assay to measure changes in intracellular ROS, we showed generation of ROS downstream of GPVI consists of two distinct phases: an initial Syk-independent burst followed by additional Syk-dependent generation. In this review, we will discuss recent findings on the regulation of platelet function by ROS, focusing on GPVI-dependent platelet activation and thrombus formation.

    Original languageEnglish
    Pages (from-to)126-130
    Number of pages5
    JournalRedox Biology
    Volume14
    DOIs
    Publication statusPublished - Apr 2018

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