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Redox control of platelet aggregation.

David W Essex1, Mengru Li

  • 1Department of Medicine, Division of Hematology, University of Texas/Health Science Center at San Antonio, San Antonio, Texas 78229-3900, USA. essex@uthscsa.edu

Biochemistry
|January 8, 2003
PubMed
Summary
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Reduced glutathione (GSH) and blood redox potential regulate platelet aggregation by influencing the alpha IIb beta 3 integrin. This involves sulfhydryl generation in the beta 3 subunit, crucial for platelet activation.

Area of Science:

  • Biochemistry
  • Hematology
  • Cell Biology

Background:

  • Platelet function research is increasingly focused on sulfhydryl and disulfide metabolism.
  • The role of redox balance in platelet activation is not fully understood.

Purpose of the Study:

  • To investigate the effect of redox buffers on platelet aggregation.
  • To determine how reduced glutathione (GSH) and platelet activation impact sulfhydryl exposure in the alpha IIb beta 3 integrin.

Main Methods:

  • Assessing platelet aggregation and secretion in response to agonists and low molecular weight thiols.
  • Measuring sulfhydryl exposure on the beta 3 subunit of alpha IIb beta 3.
  • Evaluating the impact of varying GSH/GSSG ratios on platelet activation.

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Main Results:

  • Physiologic concentrations of GSH stimulated platelet aggregation and secretion, even with subthreshold agonists.
  • GSH generated sulfhydryls in the beta 3 subunit of alpha IIb beta 3.
  • A specific redox potential (GSH/GSSG ratio of 5/1) potentiated aggregation more than GSH alone, indicating a requirement beyond simple reduction.
  • Platelet activation increased sulfhydryl labeling in the beta 3 subunit.
  • Vicinal dithiols on platelet surface proteins are implicated in sulfhydryl-dependent activation pathways.

Conclusions:

  • Blood redox potential regulates alpha IIb beta 3 integrin activation.
  • Disulfide bond cleavage and subsequent sulfhydryl generation in beta 3 are key mechanisms in alpha IIb beta 3 activation and platelet function.