The BioGRID Database Seperator
Search
Organism:

Science Aug (2000); 289(5482):1202-6
Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3.
McQuibban GA, Gong JH, Tam EM, McCulloch CA, Clark-Lewis I, Overall CM
Department of Biochemistry and Molecular Biology, Biomedical Research Centre, University of British Columbia, Vancouver, BC V6T 1Z3, Canada.
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.
[PUBMED: 10947989] Download Biogrid Interactions in a variety of formats including PSI FormatPUBMED
terms and conditions - privacy policy - Osprey Network Visualization System
BioGRID: A General Repository for Interaction Datasets.
Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
Nucleic Acids Res. Jan 1;34:D535-9.