O-Glycan Analysis of Natural Human Neutrophil Gelatinase B Using a Combination of Normal Phase- HPLC and Online Tandem Mass Spectrometry: Implications for the Domain Organization of the Enzyme†
Identifieur interne : 001911 ( Main/Exploration ); précédent : 001910; suivant : 001912O-Glycan Analysis of Natural Human Neutrophil Gelatinase B Using a Combination of Normal Phase- HPLC and Online Tandem Mass Spectrometry: Implications for the Domain Organization of the Enzyme†
Auteurs : Taj S. Mattu [Belgique, États-Unis] ; Louise Royle [Belgique] ; Jim Langridge [Belgique] ; Mark R. Wormald [Belgique] ; Philippe E. Van Den Steen [Belgique] ; Jo Van Damme [Belgique] ; Ghislain Opdenakker [Belgique] ; David J. Harvey [Belgique] ; Raymond A. Dwek [Belgique, Royaume-Uni] ; Pauline M. Rudd [Belgique, Royaume-Uni]Source :
- Biochemistry [ 0006-2960 ] ; 2000.
Abstract
Gelatinase B is a matrix metalloproteinase (MMP-9) expressed under strict control by many cell types including neutrophils, monocytes, macrophages, and tumor cells. MMP-9 is a key mediator in the physiological maintenance of the extracellular matrix both in tissue remodeling and development, while uncontrolled enzyme activity contributes to pathologies such as cancer and inflammation. Neutrophils release MMP-9 from granules in response to IL-8 stimulation. Human MMP-9 has three potential N-linked glycosylation sites and contains a Ser/Pro/Thr rich domain, known as the type V collagen-like domain, which is expected to be heavily O-glycosylated. Indeed, approximately 85% of the total sugars on human neutrophil MMP-9 are O-linked. This paper presents the detailed analysis of picomole amounts of these O-glycans using a novel HPLC-based strategy for O-glycan analysis that provides linkage and arm specific information in addition to monosaccharide sequence. The initial structural assignments were confirmed using HPLC with online MS/MS fragmentation analysis. Twelve sugars were identified that contained from two to nine monosaccharide residues. Most of these contained type 2 core structures with Galβ1-4GlcNAc (N-acetyl lactosamine) extensions, with or without sialic acid or fucose. The O-glycans were modeled using the oligosaccharide structural database. On the basis of the structure of gelatinase A (MMP-2), a model of MMP-9 suggests that the type V collagen-like domain in gelatinase B is located on a loop remote from the active site. Fourteen potential O-glycosylation sites are multiply presented on this loop of 52 amino acids. Many of the O-glycans identified contain terminal galactose residues that may provide recognition epitopes. Importantly, heavy glycosylation of this loop region, absent in gelatinase A, has considerable implications for the domain organization of MMP-9.
Url:
DOI: 10.1021/bi001367j
Affiliations:
- Belgique, Royaume-Uni, États-Unis
- Angleterre, Oxfordshire, Pennsylvanie, Province du Brabant flamand
- Louvain, Oxford
- Université d'Oxford
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Mattu</name><affiliation wicri:level="4"><country xml:lang="fr">Belgique</country><wicri:regionArea>Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road,Oxford, OX1 3QU, United Kingdom, Micromass UK Ltd., Floats Road, Wythenshawe,Manchester, M23 9LZ, United Kingdom, and Laboratory of Molecular Immunology,Rega Institute, University of Leuven, Minderbroederstraat 10, 3000 Leuven</wicri:regionArea><placeName><region type="province" nuts="2">Province du Brabant flamand</region><settlement type="city">Louvain</settlement></placeName><orgName type="university">Université d'Oxford</orgName></affiliation><affiliation></affiliation><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea> Current address: Jefferson Center for Biomedical Research,Thomas Jefferson University, 700 East Butler Avenue, Doylestown</wicri:cityArea></affiliation></author><author><name sortKey="Royle, Louise" sort="Royle, Louise" uniqKey="Royle L" first="Louise" last="Royle">Louise Royle</name><affiliation wicri:level="4"><country xml:lang="fr">Belgique</country><wicri:regionArea>Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road,Oxford, OX1 3QU, United Kingdom, Micromass UK Ltd., Floats Road, Wythenshawe,Manchester, M23 9LZ, United Kingdom, and Laboratory of Molecular Immunology,Rega Institute, University of Leuven, Minderbroederstraat 10, 3000 Leuven</wicri:regionArea><placeName><region type="province" nuts="2">Province du Brabant flamand</region><settlement type="city">Louvain</settlement></placeName><orgName type="university">Université d'Oxford</orgName></affiliation><affiliation></affiliation></author><author><name sortKey="Langridge, Jim" sort="Langridge, Jim" uniqKey="Langridge J" first="Jim" last="Langridge">Jim Langridge</name><affiliation wicri:level="4"><country xml:lang="fr">Belgique</country><wicri:regionArea>Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road,Oxford, OX1 3QU, United Kingdom, Micromass UK Ltd., Floats Road, Wythenshawe,Manchester, M23 9LZ, United Kingdom, and Laboratory of Molecular Immunology,Rega Institute, University of Leuven, Minderbroederstraat 10, 3000 Leuven</wicri:regionArea><placeName><region type="province" nuts="2">Province du Brabant flamand</region><settlement type="city">Louvain</settlement></placeName><orgName type="university">Université d'Oxford</orgName></affiliation><affiliation></affiliation></author><author><name sortKey="Wormald, Mark R" sort="Wormald, Mark R" uniqKey="Wormald M" first="Mark R." last="Wormald">Mark R. Wormald</name><affiliation wicri:level="4"><country xml:lang="fr">Belgique</country><wicri:regionArea>Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road,Oxford, OX1 3QU, United Kingdom, Micromass UK Ltd., Floats Road, Wythenshawe,Manchester, M23 9LZ, United Kingdom, and Laboratory of Molecular Immunology,Rega Institute, University of Leuven, Minderbroederstraat 10, 3000 Leuven</wicri:regionArea><placeName><region type="province" nuts="2">Province du Brabant flamand</region><settlement type="city">Louvain</settlement></placeName><orgName type="university">Université d'Oxford</orgName></affiliation><affiliation></affiliation></author><author><name sortKey="Van Den Steen, Philippe E" sort="Van Den Steen, Philippe E" uniqKey="Van Den Steen P" first="Philippe E." last="Van Den Steen">Philippe E. Van Den Steen</name><affiliation wicri:level="4"><country xml:lang="fr">Belgique</country><wicri:regionArea>Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road,Oxford, OX1 3QU, United Kingdom, Micromass UK Ltd., Floats Road, Wythenshawe,Manchester, M23 9LZ, United Kingdom, and Laboratory of Molecular Immunology,Rega Institute, University of Leuven, Minderbroederstraat 10, 3000 Leuven</wicri:regionArea><placeName><region type="province" nuts="2">Province du Brabant flamand</region><settlement type="city">Louvain</settlement></placeName><orgName type="university">Université d'Oxford</orgName></affiliation><affiliation></affiliation></author><author><name sortKey="Van Damme, Jo" sort="Van Damme, Jo" uniqKey="Van Damme J" first="Jo" last="Van Damme">Jo Van Damme</name><affiliation wicri:level="4"><country xml:lang="fr">Belgique</country><wicri:regionArea>Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road,Oxford, OX1 3QU, United Kingdom, Micromass UK Ltd., Floats Road, Wythenshawe,Manchester, M23 9LZ, United Kingdom, and Laboratory of Molecular Immunology,Rega Institute, University of Leuven, Minderbroederstraat 10, 3000 Leuven</wicri:regionArea><placeName><region type="province" nuts="2">Province du Brabant flamand</region><settlement type="city">Louvain</settlement></placeName><orgName type="university">Université d'Oxford</orgName></affiliation><affiliation></affiliation></author><author><name sortKey="Opdenakker, Ghislain" sort="Opdenakker, Ghislain" uniqKey="Opdenakker G" first="Ghislain" last="Opdenakker">Ghislain Opdenakker</name><affiliation wicri:level="4"><country xml:lang="fr">Belgique</country><wicri:regionArea>Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road,Oxford, OX1 3QU, United Kingdom, Micromass UK Ltd., Floats Road, Wythenshawe,Manchester, M23 9LZ, United Kingdom, and Laboratory of Molecular Immunology,Rega Institute, University of Leuven, Minderbroederstraat 10, 3000 Leuven</wicri:regionArea><placeName><region type="province" nuts="2">Province du Brabant flamand</region><settlement type="city">Louvain</settlement></placeName><orgName type="university">Université d'Oxford</orgName></affiliation><affiliation></affiliation></author><author><name sortKey="Harvey, David J" sort="Harvey, David J" uniqKey="Harvey D" first="David J." last="Harvey">David J. Harvey</name><affiliation wicri:level="4"><country xml:lang="fr">Belgique</country><wicri:regionArea>Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road,Oxford, OX1 3QU, United Kingdom, Micromass UK Ltd., Floats Road, Wythenshawe,Manchester, M23 9LZ, United Kingdom, and Laboratory of Molecular Immunology,Rega Institute, University of Leuven, Minderbroederstraat 10, 3000 Leuven</wicri:regionArea><placeName><region type="province" nuts="2">Province du Brabant flamand</region><settlement type="city">Louvain</settlement></placeName><orgName type="university">Université d'Oxford</orgName></affiliation><affiliation></affiliation></author><author><name sortKey="Dwek, Raymond A" sort="Dwek, Raymond A" uniqKey="Dwek R" first="Raymond A." last="Dwek">Raymond A. Dwek</name><affiliation wicri:level="4"><country xml:lang="fr">Belgique</country><wicri:regionArea>Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road,Oxford, OX1 3QU, United Kingdom, Micromass UK Ltd., Floats Road, Wythenshawe,Manchester, M23 9LZ, United Kingdom, and Laboratory of Molecular Immunology,Rega Institute, University of Leuven, Minderbroederstraat 10, 3000 Leuven</wicri:regionArea><placeName><region type="province" nuts="2">Province du Brabant flamand</region><settlement type="city">Louvain</settlement></placeName><orgName type="university">Université d'Oxford</orgName></affiliation><affiliation></affiliation><affiliation wicri:level="4"><country wicri:rule="url">Royaume-Uni</country><wicri:regionArea> To whom correspondence should be addressed at The GlycobiologyInstitute, Department of Biochemistry, University of Oxford, SouthParks Road, Oxford OX1 3QU</wicri:regionArea><orgName type="university">Université d'Oxford</orgName><placeName><settlement type="city">Oxford</settlement><region type="nation">Angleterre</region><region type="région" nuts="1">Oxfordshire</region></placeName></affiliation></author><author><name sortKey="Rudd, Pauline M" sort="Rudd, Pauline M" uniqKey="Rudd P" first="Pauline M." last="Rudd">Pauline M. Rudd</name><affiliation wicri:level="4"><country xml:lang="fr">Belgique</country><wicri:regionArea>Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road,Oxford, OX1 3QU, United Kingdom, Micromass UK Ltd., Floats Road, Wythenshawe,Manchester, M23 9LZ, United Kingdom, and Laboratory of Molecular Immunology,Rega Institute, University of Leuven, Minderbroederstraat 10, 3000 Leuven</wicri:regionArea><placeName><region type="province" nuts="2">Province du Brabant flamand</region><settlement type="city">Louvain</settlement></placeName><orgName type="university">Université d'Oxford</orgName></affiliation><affiliation></affiliation><affiliation wicri:level="4"><country wicri:rule="url">Royaume-Uni</country><wicri:regionArea> To whom correspondence should be addressed at The GlycobiologyInstitute, Department of Biochemistry, University of Oxford, SouthParks Road, Oxford OX1 3QU</wicri:regionArea><orgName type="university">Université d'Oxford</orgName><placeName><settlement type="city">Oxford</settlement><region type="nation">Angleterre</region><region type="région" nuts="1">Oxfordshire</region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Biochemistry</title><title level="j" type="abbrev">Biochemistry</title><idno type="ISSN">0006-2960</idno><idno type="eISSN">1520-4995</idno><imprint><publisher>American Chemical Society</publisher><date type="e-published" when="2000-12-02">2000</date><date when="2000-12-26">2000</date><biblScope unit="vol">39</biblScope><biblScope unit="issue">51</biblScope><biblScope unit="page" from="15695">15695</biblScope><biblScope unit="page" to="15704">15704</biblScope></imprint><idno type="ISSN">0006-2960</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-2960</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">Gelatinase B is a matrix metalloproteinase (MMP-9) expressed under strict control by many cell types including neutrophils, monocytes, macrophages, and tumor cells. MMP-9 is a key mediator in the physiological maintenance of the extracellular matrix both in tissue remodeling and development, while uncontrolled enzyme activity contributes to pathologies such as cancer and inflammation. Neutrophils release MMP-9 from granules in response to IL-8 stimulation. Human MMP-9 has three potential N-linked glycosylation sites and contains a Ser/Pro/Thr rich domain, known as the type V collagen-like domain, which is expected to be heavily O-glycosylated. Indeed, approximately 85% of the total sugars on human neutrophil MMP-9 are O-linked. This paper presents the detailed analysis of picomole amounts of these O-glycans using a novel HPLC-based strategy for O-glycan analysis that provides linkage and arm specific information in addition to monosaccharide sequence. The initial structural assignments were confirmed using HPLC with online MS/MS fragmentation analysis. Twelve sugars were identified that contained from two to nine monosaccharide residues. Most of these contained type 2 core structures with Galβ1-4GlcNAc (N-acetyl lactosamine) extensions, with or without sialic acid or fucose. The O-glycans were modeled using the oligosaccharide structural database. On the basis of the structure of gelatinase A (MMP-2), a model of MMP-9 suggests that the type V collagen-like domain in gelatinase B is located on a loop remote from the active site. Fourteen potential O-glycosylation sites are multiply presented on this loop of 52 amino acids. Many of the O-glycans identified contain terminal galactose residues that may provide recognition epitopes. Importantly, heavy glycosylation of this loop region, absent in gelatinase A, has considerable implications for the domain organization of MMP-9.</div></front></TEI><affiliations><list><country><li>Belgique</li><li>Royaume-Uni</li><li>États-Unis</li></country><region><li>Angleterre</li><li>Oxfordshire</li><li>Pennsylvanie</li><li>Province du Brabant flamand</li></region><settlement><li>Louvain</li><li>Oxford</li></settlement><orgName><li>Université d'Oxford</li></orgName></list><tree><country name="Belgique"><region name="Province du Brabant flamand"><name sortKey="Mattu, Taj S" sort="Mattu, Taj S" uniqKey="Mattu T" first="Taj S." last="Mattu">Taj S. Mattu</name></region><name sortKey="Dwek, Raymond A" sort="Dwek, Raymond A" uniqKey="Dwek R" first="Raymond A." last="Dwek">Raymond A. Dwek</name><name sortKey="Harvey, David J" sort="Harvey, David J" uniqKey="Harvey D" first="David J." last="Harvey">David J. Harvey</name><name sortKey="Langridge, Jim" sort="Langridge, Jim" uniqKey="Langridge J" first="Jim" last="Langridge">Jim Langridge</name><name sortKey="Opdenakker, Ghislain" sort="Opdenakker, Ghislain" uniqKey="Opdenakker G" first="Ghislain" last="Opdenakker">Ghislain Opdenakker</name><name sortKey="Royle, Louise" sort="Royle, Louise" uniqKey="Royle L" first="Louise" last="Royle">Louise Royle</name><name sortKey="Rudd, Pauline M" sort="Rudd, Pauline M" uniqKey="Rudd P" first="Pauline M." last="Rudd">Pauline M. Rudd</name><name sortKey="Van Damme, Jo" sort="Van Damme, Jo" uniqKey="Van Damme J" first="Jo" last="Van Damme">Jo Van Damme</name><name sortKey="Van Den Steen, Philippe E" sort="Van Den Steen, Philippe E" uniqKey="Van Den Steen P" first="Philippe E." last="Van Den Steen">Philippe E. Van Den Steen</name><name sortKey="Wormald, Mark R" sort="Wormald, Mark R" uniqKey="Wormald M" first="Mark R." last="Wormald">Mark R. Wormald</name></country><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Mattu, Taj S" sort="Mattu, Taj S" uniqKey="Mattu T" first="Taj S." last="Mattu">Taj S. Mattu</name></region></country><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Dwek, Raymond A" sort="Dwek, Raymond A" uniqKey="Dwek R" first="Raymond A." last="Dwek">Raymond A. Dwek</name></region><name sortKey="Rudd, Pauline M" sort="Rudd, Pauline M" uniqKey="Rudd P" first="Pauline M." last="Rudd">Pauline M. Rudd</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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