MMP-9 Sheds the β2 Integrin Subunit (CD18) from MacrophagesS

Activated macrophages are essential effectors of immunity and a rich source of matrix metalloproteinase-9 (MMP-9; gelatinase B). To search for cellular substrates of the enzyme, we subjected wild-type macrophages and macrophages expressing an autoactivating form of pro-MMP-9 (M9A macrophages) to pro...

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Published inMolecular & cellular proteomics Vol. 8; no. 5; pp. 1044 - 1060
Main Authors Vaisar, Tomáš, Kassim, Sean Y., Gomez, Ivan G., Green, Pattie S., Hargarten, Sara, Gough, Peter J., Parks, William C., Wilson, Carole L., Raines, Elaine W., Heinecke, Jay W.
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LanguageEnglish
Published Elsevier Inc 01.05.2009
American Society for Biochemistry and Molecular Biology
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Abstract Activated macrophages are essential effectors of immunity and a rich source of matrix metalloproteinase-9 (MMP-9; gelatinase B). To search for cellular substrates of the enzyme, we subjected wild-type macrophages and macrophages expressing an autoactivating form of pro-MMP-9 (M9A macrophages) to proteomics analysis. Two-dimensional liquid chromatography together with tandem mass spectrometry identified 467 proteins in medium conditioned by M9A and/or wild-type macrophages. Subtractive proteomics identified 18 candidate MMP-9 substrates. Biochemical studies confirmed that two transmembrane proteins, β2 integrin subunit (CD18) and amyloid protein precursor (APP), were enriched in the medium of M9A macrophages. To identify potential cleavage sites, we synthesized an overlapping library of peptides that spanned 60 residues of the ectodomain and transmembrane domain of β2 integrin. Active MMP-9 cleaved a single peptide, ECVKGPNVAAIVGGT, at residues corresponding to Ala705 and Ile706 of the β2 integrin. Peptides corresponding to this cleavage site were detected by tandem mass spectrometric analysis only in medium from M9A macrophages, strongly supporting the proposal that β2 integrin is shed by autoactivating MMP-9. Our observations indicate that subtractive proteomics in concert with peptide substrate mapping is a powerful approach for identifying proteolytic substrates and suggest that MMP-9 plays previously unsuspected roles in the regulation and shedding of β2 integrin.
AbstractList Activated macrophages are essential effectors of immunity and a rich source of matrix metalloproteinase-9 (MMP-9; gelatinase B). To search for cellular substrates of the enzyme, we subjected wild-type macrophages and macrophages expressing an autoactivating form of pro-MMP-9 (M9A macrophages) to proteomics analysis. Two-dimensional liquid chromatography together with tandem mass spectrometry identified 467 proteins in medium conditioned by M9A and/or wild-type macrophages. Subtractive proteomics identified 18 candidate MMP-9 substrates. Biochemical studies confirmed that two transmembrane proteins, β 2 integrin subunit (CD18) and amyloid protein precursor (APP), were enriched in the medium of M9A macrophages. To identify potential cleavage sites, we synthesized an overlapping library of peptides that spanned 60 residues of the ectodomain and transmembrane domain of β 2 integrin. Active MMP-9 cleaved a single peptide, ECVKGPNVAAIVGGT, at residues corresponding to Ala 705 and Ile 706 of the β 2 integrin. Peptides corresponding to this cleavage site were detected by tandem mass spectrometric analysis only in medium from M9A macrophages, strongly supporting the proposal that β 2 integrin is shed by autoactivating MMP-9. Our observations indicate that subtractive proteomics in concert with peptide substrate mapping is a powerful approach for identifying proteolytic substrates and suggest that MMP-9 plays previously unsuspected roles in the regulation and shedding of β 2 integrin.
Activated macrophages are essential effectors of immunity and a rich source of matrix metalloproteinase-9 (MMP-9; gelatinase B). To search for cellular substrates of the enzyme, we subjected wild-type macrophages and macrophages expressing an autoactivating form of pro-MMP-9 (M9A macrophages) to proteomics analysis. Two-dimensional liquid chromatography together with tandem mass spectrometry identified 467 proteins in medium conditioned by M9A and/or wild-type macrophages. Subtractive proteomics identified 18 candidate MMP-9 substrates. Biochemical studies confirmed that two transmembrane proteins, β2 integrin subunit (CD18) and amyloid protein precursor (APP), were enriched in the medium of M9A macrophages. To identify potential cleavage sites, we synthesized an overlapping library of peptides that spanned 60 residues of the ectodomain and transmembrane domain of β2 integrin. Active MMP-9 cleaved a single peptide, ECVKGPNVAAIVGGT, at residues corresponding to Ala705 and Ile706 of the β2 integrin. Peptides corresponding to this cleavage site were detected by tandem mass spectrometric analysis only in medium from M9A macrophages, strongly supporting the proposal that β2 integrin is shed by autoactivating MMP-9. Our observations indicate that subtractive proteomics in concert with peptide substrate mapping is a powerful approach for identifying proteolytic substrates and suggest that MMP-9 plays previously unsuspected roles in the regulation and shedding of β2 integrin.
Author Raines, Elaine W.
Kassim, Sean Y.
Gough, Peter J.
Heinecke, Jay W.
Gomez, Ivan G.
Green, Pattie S.
Vaisar, Tomáš
Hargarten, Sara
Wilson, Carole L.
Parks, William C.
AuthorAffiliation From the Departments of ‡ Medicine and ¶ Pathology, School of Medicine, University of Washington, Seattle, Washington 98195
AuthorAffiliation_xml – name: From the Departments of ‡ Medicine and ¶ Pathology, School of Medicine, University of Washington, Seattle, Washington 98195
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  givenname: Ivan G.
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Notes Present address: GlaxoSmithKline, Collegeville, PA 19426.
To whom correspondence should be addressed: Division of Metabolism, Endocrinology, and Nutrition, Box 358055, University of Washington Medicine SLU, 815 Mercer, Seattle, WA 98109. E-mail: heinecke@u.washington.edu
Supported by a pilot award from the University of Washington Diabetes Endocrinology Research Center.
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Snippet Activated macrophages are essential effectors of immunity and a rich source of matrix metalloproteinase-9 (MMP-9; gelatinase B). To search for cellular...
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StartPage 1044
Title MMP-9 Sheds the β2 Integrin Subunit (CD18) from MacrophagesS
URI https://dx.doi.org/10.1074/mcp.M800449-MCP200
https://pubmed.ncbi.nlm.nih.gov/PMC2689762
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