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

Science (New York, N.Y.) | Aug 18, 2000

http://www.ncbi.nlm.nih.gov/pubmed/10947989

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.

Pubmed ID: 10947989 RIS Download

Mesh terms: Animals | Calcium | Catalytic Domain | Cell Line | Chemokine CCL7 | Chemokines | Chemotaxis, Leukocyte | Collagen | Cytokines | Enzyme Activation | Gene Library | Hemopexin | Humans | Inflammation | Mass Spectrometry | Matrix Metalloproteinase 2 | Mice | Monocyte Chemoattractant Proteins | Protein Binding | Protein Structure, Tertiary | Receptors, Chemokine | Recombinant Proteins | Tissue Inhibitor of Metalloproteinase-2 | Two-Hybrid System Techniques

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