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Ca2+-dependent cross-linking processes in human platelets.

I Cohen, T Glaser, A Veis

    Biochimica Et Biophysica Acta
    |August 17, 1981
    PubMed
    Summary
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    Calcium-activated platelet transglutaminase, identified as platelet factor XIII, cross-links proteins to form polymers. This process stabilizes platelet membranes during hemostasis.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Hematology

    Background:

    • Platelet activation involves complex protein interactions and structural changes.
    • Calcium ions play a critical role in initiating various cellular responses, including protein cross-linking.

    Purpose of the Study:

    • To investigate the role of calcium-dependent enzymes in platelet protein polymerization.
    • To identify the specific enzyme responsible for cross-linking and its physiological function in platelet aggregation.

    Main Methods:

    • Platelet activation using ionophore A23187 in the presence and absence of protease inhibitors (leupeptin).
    • Analysis of protein and glycoprotein changes using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE).
    • Detection of protein incorporation using radiolabeled histamine ([14C]Histamine).

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    Main Results:

    • Increased cytoplasmic Ca2+ induced polymer formation and disappearance of monomeric proteins.
    • Leupeptin significantly enhanced polymer formation, indicating protease involvement.
    • Histamine inhibited monomer loss and was incorporated into the polymer, identifying transglutaminase activity.

    Conclusions:

    • A Ca2+-dependent transglutaminase, identified as platelet factor XIII, mediates protein cross-linking in platelets.
    • Platelet factor XIII activity leads to polymer formation and stabilization of platelet structure.
    • This cross-linking mechanism is proposed to be crucial for stabilizing platelet membranes in the hemostatic plug.