Title
Carboxyterminal cleavage of the chemokines MIG and IP-10 by gelatinase B and neutrophil collagenase
Author
Faculty/Department
Faculty of Sciences. Biology
Publication type
article
Publication
New York, N.Y. ,
Subject
Chemistry
Biology
Human medicine
Source (journal)
Biochemical and biophysical research communications. - New York, N.Y.
Volume/pages
310(2003) :3 , p. 889-896
ISSN
0006-291X
ISI
000185991400035
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Abstract
Proteolytic processing is an important regulatory mechanism for chemokines. Matrix metalloproteinases (MMPs), such as gelatinase A/MMP-2 and gelatinase B/MMP-9, are known to process the aminoterminal end of various chemokines, including interleukin-8 (IL-8/CXCL-8) and monocyte chemotactic protein-3 (MCP-3/CXCL-7). In the present study, two proteases, gelatinase B and neutrophil collagenase/MMP-8, are shown for the first time to process the carboxyterminal end of two chemokines, monokine induced by interferon (IFN)-γ (MIG/CXCL-9) and IFN-inducible protein-10 (IP-10/CXCL-10). Neutrophil collagenase degrades MIG into small fragments and cleaves IP-10 behind positions 71 and 73. Gelatinase B degrades IP-10 and cleaves MIG at three different sites in its extended carboxyterminal region. This results in the formation of MIG(194), MIG(193), and MIG(190). In general, gelatinase B was more efficient than neutrophil collagenase in processing these chemokines. Alignment of the CXC chemokines with the respective cleavage sites by both MMPs identified the ELR motif as a possible determinant for amino terminal cleavage by these MMPs.
E-info
https://repository.uantwerpen.be/docman/iruaauth/5a1ffb/d09a9a9c409.pdf
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