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Elastase and metalloproteinase activities regulate soluble complement receptor 1 release.

S Sadallah1, C Hess, S Miot

  • 1Department of Research University Hospital Basel, Basel, Switzerland. sadallah@ubaclu.unibas.ch

European Journal of Immunology
|November 11, 1999
PubMed
Summary
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Soluble complement receptor 1 (sCR1) is released from immune cells by enzymes like human neutrophil elastase (HNE). This shedding of functional sCR1 is regulated by metalloproteases and alpha1-antiprotease.

Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Complement receptor 1 (CR1) is a key immune molecule found on polymorphonuclear cells (PMNs).
  • CR1 can be released as a soluble fragment (sCR1), but the mechanisms and enzymes involved are not fully understood.

Purpose of the Study:

  • To investigate the enzymes responsible for cleaving CR1 from PMNs and other cells.
  • To identify inhibitors that can block the shedding of soluble CR1 (sCR1).

Main Methods:

  • In vitro stimulation of purified human PMNs.
  • Cleavage assays using purified human neutrophil elastase (HNE) on PMNs, erythrocytes, and urinary vesicles.
  • Assessment of sCR1 shedding inhibition using various protease inhibitors (PMSF, alpha1-antiprotease, elafin, 1,10-phenanthroline) and an antibody against MMP8.

Related Experiment Videos

  • Specificity testing by evaluating the effect of inhibitors on L-selectin shedding.

    • Main Results:

    • Human neutrophil elastase (HNE) cleaves CR1 from erythrocytes and urinary vesicles, and significantly enhances CR1 cleavage from activated PMNs.
    • The largest HNE-cleaved fragment from PMNs matches the size of spontaneously shed CR1, and these fragments retain functionality.
    • sCR1 shedding is inhibited by serine protease inhibitors (PMSF, alpha1-antiprotease, elafin) and metalloprotease inhibitors (1,10-phenanthroline, anti-MMP8 antibody).
    • Combined inhibition with 1,10-phenanthroline and elafin maximally blocked sCR1 shedding, with no effect on L-selectin shedding, indicating specificity.

    Conclusions:

    • Elastase or elastase-like activity is likely responsible for in vivo shedding of functional sCR1.
    • The shedding process is tightly regulated by the local release of PMN-derived metalloproteases and alpha1-antiprotease.