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Related Experiment Videos

Collagen-platelet interaction: type XI collagen-induced platelet aggregation.

T M Chiang1, M Cremer, A H Kang

  • 1V.A. Medical Center, Memphis, TN.

Thrombosis Research
|August 1, 1990
PubMed
Summary

Fibrillar type XI collagen, but not soluble forms, triggers human platelet aggregation and adenosine triphosphate release, an effect blocked by aspirin.

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Area of Science:

  • Biochemistry
  • Hematology
  • Cell Biology

Background:

  • Collagen is a known inducer of platelet aggregation.
  • The specific role of Type XI collagen in platelet activation is not fully understood.

Purpose of the Study:

  • To investigate the effect of Type XI collagen on human platelet aggregation and adenosine triphosphate release.
  • To compare the activity of fibrillar versus monomeric Type XI collagen.
  • To determine if aspirin affects Type XI collagen-mediated platelet responses.

Main Methods:

  • Incubation of human platelets with fibrillar and monomeric Type XI collagen.
  • Measurement of platelet aggregation and adenosine triphosphate release.
  • Assessment of radiolabeled phosphate incorporation into platelet proteins.

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  • Inhibition studies using aspirin.

    • Main Results:

    • Fibrillar Type XI collagen induced human platelet aggregation and adenosine triphosphate release in a dose-dependent manner.
    • Soluble monomeric Type XI collagen did not elicit these responses.
    • Aspirin inhibited the aggregation and release mediated by fibrillar Type XI collagen.
    • Type XI collagen increased radiolabeled phosphate incorporation into 42 KDa and 22 KDa protein bands.
    • Type IX collagen did not induce these effects.

    Conclusions:

    • Fibrillar Type XI collagen acts as a potent inducer of human platelet aggregation and adenosine triphosphate release.
    • The mechanism involves specific interactions sensitive to aspirin, similar to other collagen types.
    • These findings highlight the biological significance of fibrillar Type XI collagen in hemostasis.