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RNA-seq Analysis of Transcriptomes in Thrombin-treated and Control Human Pulmonary Microvascular Endothelial Cells
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Published on: February 13, 2013

Long range communication between exosites 1 and 2 modulates thrombin function.

Nicolas S Petrera1, Alan R Stafford, Beverly A Leslie

  • 1Department of Medicine, McMaster University, and Henderson Research Center, Hamilton, Ontario L8V 1C3, Canada.

The Journal of Biological Chemistry
|July 11, 2009
PubMed
Summary

This study demonstrates bidirectional communication between thrombin

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Published on: February 14, 2017

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Thrombin's exosites 1 and 2 regulate its activity by binding substrates and cofactors.
  • Allosteric modulation of thrombin's active site is influenced by exosite interactions.
  • The direct allosteric linkage between thrombin's exosites 1 and 2 remains unclear.

Purpose of the Study:

  • To investigate the direct allosteric linkage between thrombin exosites 1 and 2.
  • To explore the functional consequences of inter-exosite communication on thrombin activity.
  • To provide evidence for long-range allosteric regulation in thrombin.

Main Methods:

  • Titration of fluorescently labeled thrombin variant with exosite 2 ligands (HD22, gamma'-peptide, heparin).
  • Evaluation of exosite 2 ligand capacity to inhibit thrombin binding to fibrin clots.
  • Surface plasmon resonance to monitor thrombin interactions with fibrinogen and fibrin.

Main Results:

  • Exosite 2 ligands induced concentration-dependent, saturable fluorescence changes, indicating inter-exosite linkage.
  • Exosite 2 ligands dose-dependently inhibited thrombin binding to fibrin clots.
  • Exosite 1 ligands inhibited exosite 2-mediated thrombin interactions, confirming bidirectional communication.

Conclusions:

  • Direct allosteric linkage exists between thrombin exosites 1 and 2.
  • Bidirectional communication between exosites modulates thrombin's interaction with substrates.
  • These findings reveal increased complexity in thrombin regulation mechanisms.