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Related Experiment Videos

The specific binding of thrombin to human polymorphonuclear leucocytes.

O Sonne1

  • 1Institute of Physiology, University of Aarhus, Denmark.

Scandinavian Journal of Clinical and Laboratory Investigation
|December 1, 1988
PubMed
Summary

Thrombin acts as a chemoattractant for polymorphonuclear leukocytes. This study characterizes thrombin binding kinetics, revealing specific receptors that may explain thrombin-induced cell migration.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Immunology

Background:

  • Thrombin is recognized as a chemotaxin, attracting polymorphonuclear leukocytes (PMNs).
  • Understanding the molecular interactions between thrombin and PMNs is crucial for elucidating inflammatory processes.

Purpose of the Study:

  • To characterize the binding kinetics of 125I-labelled thrombin to purified polymorphonuclear leukocytes.
  • To determine the receptor characteristics and affinity for thrombin on PMNs.

Main Methods:

  • Utilized 125I-labelled thrombin for binding assays with purified PMNs at 4°C and 37°C.
  • Investigated tracer dissociation upon addition of unlabeled thrombin or hirudin.
  • Quantified receptor numbers and dissociation constants (Kd).

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Main Results:

  • 125I-labelled thrombin exhibited rapid binding to PMNs with a half-time of approximately 3 minutes at 4°C.
  • Approximately 77% of bound tracer dissociated with excess unlabeled thrombin or hirudin.
  • PMNs possess two distinct receptor populations: ~50 receptors with a Kd of 18 pmol/L and ~6000 receptors with a Kd of 31 nmol/L.
  • Binding affinity at 37°C was 7-10 fold lower than at 4°C.

Conclusions:

  • The characterized thrombin binding kinetics and receptor affinities suggest a molecular basis for thrombin-induced PMN chemotaxis.
  • High-affinity and low-affinity receptors contribute to thrombin's role in PMN recruitment and function.