Related Experiment Video

Updated: Oct 11, 2026

Quantitative In vitro Assay to Measure Neutrophil Adhesion to Activated Primary Human Microvascular Endothelial Cells under Static Conditions
11:22

Quantitative In vitro Assay to Measure Neutrophil Adhesion to Activated Primary Human Microvascular Endothelial Cells under Static Conditions

Published on: August 23, 2013

The soluble endothelial protein C receptor binds to activated neutrophils: involvement of proteinase-3 and CD11b/CD18

S Kurosawa1, C T Esmon, D J Stearns-Kurosawa

  • 1Cardiovascular Biology Research, Oklahoma Medical Research Foundation, Oklahoma City, OK 73104, USA.

Journal of Immunology (Baltimore, Md. : 1950)
|October 18, 2000
PubMed

Insights

Soluble endothelial protein C receptor (EPCR) binds to activated neutrophils via proteinase-3 (PR3) and Mac-1. This finding suggests a link between the protein C pathway and neutrophil functions.

Area of Science:

  • Hematology
  • Immunology
  • Biochemistry

Background:

  • The protein C pathway regulates blood coagulation and inflammation.
  • Endothelial protein C receptor (EPCR) accelerates the formation of activated protein C, an anticoagulant and anti-inflammatory agent.

Purpose of the Study:

  • To investigate the interaction between soluble EPCR and activated neutrophils.
  • To identify the specific molecules involved in this interaction.

Main Methods:

  • Affinity chromatography
  • Binding studies with purified components
  • Antibody blockade studies

Main Results:

  • Soluble EPCR binds to PMA-activated neutrophils.
  • Soluble EPCR binds to proteinase-3 (PR3), a neutrophil granule proteinase.
  • EPCR binding to neutrophils is partially dependent on Mac-1 (a beta(2) integrin).

Conclusions:

  • Soluble EPCR interacts with activated neutrophils through PR3 and Mac-1.
  • This interaction suggests a novel link between the protein C pathway and neutrophil functions, impacting processes like inflammation and immunity.

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