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Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3.

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Affiliations

  • 1. Department of Biochemistry and Molecular Biology, Biomedical Research Centre, University of British Columbia, Vancouver, BC V6T 1Z3, Canada.
      Authors
    • McQuibban GA 1
    (1 author)

ORCIDs linked to this article

Science, 01 Aug 2000, 289(5482):1202-1206
https://doi.org/10.1126/science.289.5482.1202 PMID: 10947989 

Abstract 

Tissue degradation by the matrix metalloproteinase gelatinase A is pivotal to inflammation and metastases. Recognizing the catalytic importance of substrate-binding exosites outside the catalytic domain, we screened for extracellular substrates using the gelatinase A hemopexin domain as bait in the yeast two-hybrid system. Monocyte chemoattractant protein-3 (MCP-3) was identified as a physiological substrate of gelatinase A. Cleaved MCP-3 binds to CC-chemokine receptors-1, -2, and -3, but no longer induces calcium fluxes or promotes chemotaxis, and instead acts as a general chemokine antagonist that dampens inflammation. This suggests that matrix metalloproteinases are both effectors and regulators of the inflammatory response.

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Read article at publisher's site: https://doi.org/10.1126/science.289.5482.1202

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