Title
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Carboxyterminal cleavage of the chemokines MIG and IP-10 by gelatinase B and neutrophil collagenase
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Author
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Abstract
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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. |
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Language
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English
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Source (journal)
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Biochemical and biophysical research communications. - New York, N.Y.
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Publication
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New York, N.Y.
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2003
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ISSN
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0006-291X
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DOI
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10.1016/J.BBRC.2003.09.098
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Volume/pages
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310
:3
(2003)
, p. 889-896
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ISI
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000185991400035
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Full text (Publisher's DOI)
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Full text (publisher's version - intranet only)
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