DENNEY, H., CLENCH, M. and WOODROOFE, M. N. (2009). Cleavage of chemokines CCL2 and CXCL10 by matrix metalloproteinases-2 and -9: implications for chemotaxis. Biochemical and biophysical research communications, 382 (2), 341-347.Full text not available from this repository.
Proteolytic processing of chemokines is a complex process that can result in dramatic effects on their chemotactic activity. Results from gel electrophoresis and mass spectrometry using recombinant CCL2 and CXCL10, incubated with either MMP-2 or -9, indicate that both chemokines are cleaved by the enzymes. N-terminal truncation of four amino acids from CCL2, and four or five residues from CXCL10 occurred, but removal of four residues from the C-terminus of CXCL10 was also observed with both MMPs. The speed of the reaction was chemokine-dependent, with N-terminal processing of CCL2 being complete within 3 h, whereas activity of the MMPs on CXCL10 remained incomplete at 48 h. The effect on the chemotactic potential of N-terminal truncation of CCL2 by MMPs-2 and -9 was investigated using in vitro migration assays. Monocytic cells exhibited a 2-fold reduction in migration to MMP-cleaved CCL2 variants, compared to intact CCL2.
|Research Institute, Centre or Group:||Biomolecular Sciences Research Centre|
|Depositing User:||Sarah Ward|
|Date Deposited:||18 May 2010 14:48|
|Last Modified:||28 Jun 2013 14:58|
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