Analysis of Heparan Sulfate Oligosaccharides with Ion Pair-Reverse Phase Capillary High Performance Liquid Chromatography-Microelectrospray Ionization Time-of-Flight Mass Spectrometry†
Identifieur interne : 000D27 ( Istex/Checkpoint ); précédent : 000D26; suivant : 000D28Analysis of Heparan Sulfate Oligosaccharides with Ion Pair-Reverse Phase Capillary High Performance Liquid Chromatography-Microelectrospray Ionization Time-of-Flight Mass Spectrometry†
Auteurs : Balagurunathan Kuberan [États-Unis] ; Miroslaw Lech [États-Unis] ; Lijuan Zhang [États-Unis] ; Zhengliang L. Wu [États-Unis] ; David L. Beeler [États-Unis] ; Robert D. Rosenberg [États-Unis]Source :
- Journal of the American Chemical Society [ 0002-7863 ] ; 2002.
Abstract
Heparan sulfate, a cell surface bound glycosaminoglycan polysaccharide, has been implicated in numerous biological functions. Heparan sulfate molecules are highly complex and diverse, yet deceivingly look simple and similar, rendering structure−function correlation tedious. Current chromatographic and mass spectrometric techniques have limitations for analyzing glycosaminoglycan samples that are in low abundance and that are large in size, due to their highly acidic nature arising from a large number of sulfate and of carboxylate groups. A new methodology was developed using capillary ion-paired reverse-phase C18 HPLC directly coupled to ESI-TOF-MS to address the above issues. On the basis of HS disaccharide analysis, dibutylamine was found to be the best suited for HS analysis among many ion-pairing agents investigated. Next, analysis of oligosaccharides derived from heparosan, the precursor for heparan sulfate, was undertaken to demonstrate its greater applicability in a more complex structural analysis. The established chromatographic conditions enabled the characterization of heparosan oligosaccharides of sizes up to tetracontasaccharide with high resolution in a single run and were amenable to negative ion electrospray MS in which sodium adduction and fragmentation were avoided. To date, these are the largest nonsulfated HS precursor oligosaccharides to be characterized by LC/MS. Finally, the current methodology was applied to the characterization of the biologically important ATIII binding pentasaccharide and its precursors, which differ from each other by sulfation pattern and/or degree of sulfation. All of these pentasaccharides were well-resolved and characterized by the LC/MS system with 34SO4 as a mass spectral probe. This newly developed methodology facilitates the purification and rapid characterization of biologically significant HS oligosaccharides, and will thus expedite their synthesis. These findings should undoubtedly pave the way in deciphering multiple functional arrangements, ascribed to many biological activities, which are predictably embedded in a single large chaotic, yet well-organized HS polysaccharide chain. Development of newer techniques for HS oligosaccharide analysis is greatly needed in the postgenome era as attention shifts to the functional implications of proteins and carbohydrates in general and HS in particular.
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DOI: 10.1021/ja0178867
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Pair-Reverse Phase Capillary High Performance Liquid
Chromatography-Microelectrospray Ionization Time-of-Flight
Mass Spectrometry<ref type="bib" target="#ja0178867AF2"><hi rend="superscript">†</hi></ref></title><author><name sortKey="Kuberan, Balagurunathan" sort="Kuberan, Balagurunathan" uniqKey="Kuberan B" first="Balagurunathan" last="Kuberan">Balagurunathan Kuberan</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Massachusetts</region></placeName><wicri:cityArea>Contribution from the Department of Biology, Massachusetts Institute of Technology,Cambridge, Massachusetts 02139, and Department of Molecular Medicine, Beth IsraelDeaconess Medical Center, Harvard Medical School, Boston</wicri:cityArea></affiliation></author><author><name sortKey="Lech, Miroslaw" sort="Lech, Miroslaw" uniqKey="Lech M" first="Miroslaw" last="Lech">Miroslaw Lech</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Massachusetts</region></placeName><wicri:cityArea>Contribution from the Department of Biology, Massachusetts Institute of Technology,Cambridge, Massachusetts 02139, and Department of Molecular Medicine, Beth IsraelDeaconess Medical Center, Harvard Medical School, Boston</wicri:cityArea></affiliation></author><author><name sortKey="Zhang, Lijuan" sort="Zhang, Lijuan" uniqKey="Zhang L" first="Lijuan" last="Zhang">Lijuan Zhang</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Massachusetts</region></placeName><wicri:cityArea>Contribution from the Department of Biology, Massachusetts Institute of Technology,Cambridge, Massachusetts 02139, and Department of Molecular Medicine, Beth IsraelDeaconess Medical Center, Harvard Medical School, Boston</wicri:cityArea></affiliation></author><author><name sortKey="Wu, Zhengliang L" sort="Wu, Zhengliang L" uniqKey="Wu Z" first="Zhengliang L." last="Wu">Zhengliang L. Wu</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Massachusetts</region></placeName><wicri:cityArea>Contribution from the Department of Biology, Massachusetts Institute of Technology,Cambridge, Massachusetts 02139, and Department of Molecular Medicine, Beth IsraelDeaconess Medical Center, Harvard Medical School, Boston</wicri:cityArea></affiliation></author><author><name sortKey="Beeler, David L" sort="Beeler, David L" uniqKey="Beeler D" first="David L." last="Beeler">David L. Beeler</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Massachusetts</region></placeName><wicri:cityArea>Contribution from the Department of Biology, Massachusetts Institute of Technology,Cambridge, Massachusetts 02139, and Department of Molecular Medicine, Beth IsraelDeaconess Medical Center, Harvard Medical School, Boston</wicri:cityArea></affiliation></author><author><name sortKey="Rosenberg, Robert D" sort="Rosenberg, Robert D" uniqKey="Rosenberg R" first="Robert D." last="Rosenberg">Robert D. Rosenberg</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Massachusetts</region></placeName><wicri:cityArea>Contribution from the Department of Biology, Massachusetts Institute of Technology,Cambridge, Massachusetts 02139, and Department of Molecular Medicine, Beth IsraelDeaconess Medical Center, Harvard Medical School, Boston</wicri:cityArea></affiliation><affiliation wicri:level="1"><country wicri:rule="url">États-Unis</country></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Journal of the American Chemical Society</title><title level="j" type="abbrev">J. Am. Chem. Soc.</title><idno type="ISSN">0002-7863</idno><idno type="eISSN">1520-5126</idno><imprint><publisher>American Chemical Society</publisher><date type="e-published">2002</date><date type="published">2002</date><biblScope unit="vol">124</biblScope><biblScope unit="issue">29</biblScope><biblScope unit="page" from="8707">8707</biblScope><biblScope unit="page" to="8718">8718</biblScope></imprint><idno type="ISSN">0002-7863</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0002-7863</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">Heparan sulfate, a cell surface bound glycosaminoglycan polysaccharide, has been implicated in numerous biological functions. Heparan sulfate molecules are highly complex and diverse, yet deceivingly look simple and similar, rendering structure−function correlation tedious. Current chromatographic and mass spectrometric techniques have limitations for analyzing glycosaminoglycan samples that are in low abundance and that are large in size, due to their highly acidic nature arising from a large number of sulfate and of carboxylate groups. A new methodology was developed using capillary ion-paired reverse-phase C18 HPLC directly coupled to ESI-TOF-MS to address the above issues. On the basis of HS disaccharide analysis, dibutylamine was found to be the best suited for HS analysis among many ion-pairing agents investigated. Next, analysis of oligosaccharides derived from heparosan, the precursor for heparan sulfate, was undertaken to demonstrate its greater applicability in a more complex structural analysis. The established chromatographic conditions enabled the characterization of heparosan oligosaccharides of sizes up to tetracontasaccharide with high resolution in a single run and were amenable to negative ion electrospray MS in which sodium adduction and fragmentation were avoided. To date, these are the largest nonsulfated HS precursor oligosaccharides to be characterized by LC/MS. Finally, the current methodology was applied to the characterization of the biologically important ATIII binding pentasaccharide and its precursors, which differ from each other by sulfation pattern and/or degree of sulfation. All of these pentasaccharides were well-resolved and characterized by the LC/MS system with 34SO4 as a mass spectral probe. This newly developed methodology facilitates the purification and rapid characterization of biologically significant HS oligosaccharides, and will thus expedite their synthesis. These findings should undoubtedly pave the way in deciphering multiple functional arrangements, ascribed to many biological activities, which are predictably embedded in a single large chaotic, yet well-organized HS polysaccharide chain. Development of newer techniques for HS oligosaccharide analysis is greatly needed in the postgenome era as attention shifts to the functional implications of proteins and carbohydrates in general and HS in particular.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Massachusetts</li></region></list><tree><country name="États-Unis"><region name="Massachusetts"><name sortKey="Kuberan, Balagurunathan" sort="Kuberan, Balagurunathan" uniqKey="Kuberan B" first="Balagurunathan" last="Kuberan">Balagurunathan Kuberan</name></region><name sortKey="Beeler, David L" sort="Beeler, David L" uniqKey="Beeler D" first="David L." last="Beeler">David L. Beeler</name><name sortKey="Lech, Miroslaw" sort="Lech, Miroslaw" uniqKey="Lech M" first="Miroslaw" last="Lech">Miroslaw Lech</name><name sortKey="Rosenberg, Robert D" sort="Rosenberg, Robert D" uniqKey="Rosenberg R" first="Robert D." last="Rosenberg">Robert D. Rosenberg</name><name sortKey="Rosenberg, Robert D" sort="Rosenberg, Robert D" uniqKey="Rosenberg R" first="Robert D." last="Rosenberg">Robert D. Rosenberg</name><name sortKey="Wu, Zhengliang L" sort="Wu, Zhengliang L" uniqKey="Wu Z" first="Zhengliang L." last="Wu">Zhengliang L. Wu</name><name sortKey="Zhang, Lijuan" sort="Zhang, Lijuan" uniqKey="Zhang L" first="Lijuan" last="Zhang">Lijuan Zhang</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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