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Glycoprotein IIb/IIIa and Membrane Skeleton in Resting and Activated Platelets

  • H. Suzuki
  • K. Tanoue
  • H. Yamazaki
Conference paper

Abstract

When platelets are activated by an appropriate stimulus, they change their shapes from discs to spheres with extending pseudopodia, release the contents of their storage granules, and aggregate with each other. These responses are believed to be mediated by the cytoskeleton, especially as a result of the contractile activity of actin filaments and associated proteins.1,2 The human platelet membrane skeleton has been identified as a membrane-bound actin submembrane structure and that is distinct from the network of cytoplasmic actin filaments.3 In the present study, we examined the cytoskeletal organization in unstimulated and thrombin-activated platelets, focusing on the relationship between membrane GPIIb/IIIa complex, a receptor for fibrinogen, and the membrane skeleton.

Keywords

Gold Particle Amorphous Structure Human Platelet Membrane Skeleton Storage Granule 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Japan 1992

Authors and Affiliations

  • H. Suzuki
    • 1
  • K. Tanoue
    • 1
  • H. Yamazaki
    • 1
    • 2
  1. 1.Department of Cardiovascular ResearchThe Tokyo Metropolitan Institute of Medical ScienceTokyo 113Japan
  2. 2.Jissen Women’s UniversityHino 191Japan

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