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Science 289 (5482): 1202-1206

Copyright © 2000 by the American Association for the Advancement of Science

Inflammation Dampened by Gelatinase A Cleavage of Monocyte Chemoattractant Protein-3

G. Angus McQuibban,1 Jiang-Hong Gong,2 Eric M. Tam,1 Christopher A. G. McCulloch,4 Ian Clark-Lewis,2 Christopher M. Overall13*

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.

1 Department of Biochemistry and Molecular Biology,
2 Biomedical Research Centre,
3 Department of Oral Biological and Medical Sciences, University of British Columbia, Vancouver, BC V6T 1Z3, Canada.
4 Medical Research Council Group in Periodontal Physiology, University of Toronto, Toronto, ON M5S 3E8, Canada.
*   To whom correspondence should be addressed. E-mail: overall{at}interchange.ubc.ca

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R. Visse and H. Nagase (2003)
Circ. Res. 92, 827-839
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Cathepsin D Specifically Cleaves the Chemokines Macrophage Inflammatory Protein-1{alpha}, Macrophage Inflammatory Protein-1{beta}, and SLC That Are Expressed in Human Breast Cancer.
M. Wolf, I. Clark-Lewis, C. Buri, H. Langen, M. Lis, and L. Mazzucchelli (2003)
Am. J. Pathol. 162, 1183-1190
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Matrix metalloproteinase-2 mediates cytokine-induced myocardial contractile dysfunction.
C. Qun Gao, G. Sawicki, W. L Suarez-Pinzon, T. Csont, M. Wozniak, P. Ferdinandy, and R. Schulz (2003)
Cardiovasc Res 57, 426-433
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Utilization of a Novel Recombinant Myoglobin Fusion Protein Expression System to Characterize the Tissue Inhibitor of Metalloproteinase (TIMP)-4 and TIMP-2 C-terminal Domain and Tails by Mutagenesis. THE IMPORTANCE OF ACIDIC RESIDUES IN BINDING THE MMP-2 HEMOPEXIN C DOMAIN.
H. S.-T. Kai, G. S. Butler, C. J. Morrison, A. E. King, G. R. Pelman, and C. M. Overall (2002)
J. Biol. Chem. 277, 48696-48707
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Collagen Binding Properties of the Membrane Type-1 Matrix Metalloproteinase (MT1-MMP) Hemopexin C Domain. THE ECTODOMAIN OF THE 44-kDa AUTOCATALYTIC PRODUCT OF MT1-MMP INHIBITS CELL INVASION BY DISRUPTING NATIVE TYPE I COLLAGEN CLEAVAGE.
E. M. Tam, Y. I. Wu, G. S. Butler, M. S. Stack, and C. M. Overall (2002)
J. Biol. Chem. 277, 39005-39014
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Matrix Metalloproteinases Cleave Connective Tissue Growth Factor and Reactivate Angiogenic Activity of Vascular Endothelial Growth Factor 165.
G. Hashimoto, I. Inoki, Y. Fujii, T. Aoki, E. Ikeda, and Y. Okada (2002)
J. Biol. Chem. 277, 36288-36295
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Intracellular Action of Matrix Metalloproteinase-2 Accounts for Acute Myocardial Ischemia and Reperfusion Injury.
W. Wang, C. J. Schulze, W. L. Suarez-Pinzon, J. R.B. Dyck, G. Sawicki, and R. Schulz (2002)
Circulation 106, 1543-1549
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