Differentiation of 3-O-Sulfated Heparin Disaccharide Isomers: Identification of Structural Aspects of the Heparin CCL2 Binding Motif
The presence of 3-O-sulfated glucosamine residues in heparin or heparan sulfate plays a role in binding to antithrombin III and HSV infection. In this study, tandem mass spectrometry was used to differentiate between two heparin disaccharide isomers containing variable sulfate at C6 in a common disa...
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| Veröffentlicht in: | Journal of the American Society for Mass Spectrometry 2009-04, Vol.20 (4), p.652-657 |
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| creator | Meissen, John K. Sweeney, Matthew D. Girardi, Matthew Lawrence, Roger Esko, Jeffrey D. Leary, Julie A. |
| description | The presence of 3-O-sulfated glucosamine residues in heparin or heparan sulfate plays a role in binding to antithrombin III and HSV infection. In this study, tandem mass spectrometry was used to differentiate between two heparin disaccharide isomers containing variable sulfate at C6 in a common disaccharide and C3 in a more rare one. The dissociation patterns shown by MS
2 and MS
3 were clearly distinguishable between the isomers, allowing their differentiation and quantitation. Using this technique, we show that an octasaccharide with 11 sulfate groups with high affinity for inflammatory chemokine CCL2 does not contain 3-O-sulfated disaccharides.
CID was used to distinguish between heparin disaccharide isomers containing or lacking 3-O-sulfation and applied to evaluate the involvement of 3-O-sulfation in the heparin/CCL2 interaction. |
| doi_str_mv | 10.1016/j.jasms.2008.12.002 |
| format | Article |
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2 and MS
3 were clearly distinguishable between the isomers, allowing their differentiation and quantitation. Using this technique, we show that an octasaccharide with 11 sulfate groups with high affinity for inflammatory chemokine CCL2 does not contain 3-O-sulfated disaccharides.
CID was used to distinguish between heparin disaccharide isomers containing or lacking 3-O-sulfation and applied to evaluate the involvement of 3-O-sulfation in the heparin/CCL2 interaction.</description><identifier>ISSN: 1044-0305</identifier><identifier>EISSN: 1879-1123</identifier><identifier>DOI: 10.1016/j.jasms.2008.12.002</identifier><identifier>PMID: 19185514</identifier><language>eng</language><publisher>New York: Elsevier Inc</publisher><subject>Analytical Chemistry ; Animals ; Anticoagulants ; Binding ; Binding Sites ; Bioinformatics ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; Chemokine CCL2 - chemistry ; CHO Cells ; Cricetinae ; Cricetulus ; Differentiation ; Disaccharides - chemistry ; Glycosaminoglycans - chemistry ; Heparan sulfate ; Heparin - analogs & derivatives ; Heparin - chemistry ; Humans ; Isomerism ; Isomers ; Mass spectrometry ; Oligosaccharides - chemistry ; Organic Chemistry ; Protein Binding ; Proteomics ; Sulfates - chemistry ; Tandem Mass Spectrometry - methods</subject><ispartof>Journal of the American Society for Mass Spectrometry, 2009-04, Vol.20 (4), p.652-657</ispartof><rights>2009</rights><rights>American Society for Mass Spectrometry 2009</rights><rights>Journal of The American Society for Mass Spectrometry is a copyright of Springer, 2009.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c530t-842005ba6a9096a4c5e0d26e54a48fe1cf60fa5e9e22fd888cb6d01e68a124133</citedby><cites>FETCH-LOGICAL-c530t-842005ba6a9096a4c5e0d26e54a48fe1cf60fa5e9e22fd888cb6d01e68a124133</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1016/j.jasms.2008.12.002$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1016/j.jasms.2008.12.002$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,780,784,885,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19185514$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Meissen, John K.</creatorcontrib><creatorcontrib>Sweeney, Matthew D.</creatorcontrib><creatorcontrib>Girardi, Matthew</creatorcontrib><creatorcontrib>Lawrence, Roger</creatorcontrib><creatorcontrib>Esko, Jeffrey D.</creatorcontrib><creatorcontrib>Leary, Julie A.</creatorcontrib><title>Differentiation of 3-O-Sulfated Heparin Disaccharide Isomers: Identification of Structural Aspects of the Heparin CCL2 Binding Motif</title><title>Journal of the American Society for Mass Spectrometry</title><addtitle>J Am Soc Mass Spectrom</addtitle><addtitle>J Am Soc Mass Spectrom</addtitle><description>The presence of 3-O-sulfated glucosamine residues in heparin or heparan sulfate plays a role in binding to antithrombin III and HSV infection. In this study, tandem mass spectrometry was used to differentiate between two heparin disaccharide isomers containing variable sulfate at C6 in a common disaccharide and C3 in a more rare one. The dissociation patterns shown by MS
2 and MS
3 were clearly distinguishable between the isomers, allowing their differentiation and quantitation. Using this technique, we show that an octasaccharide with 11 sulfate groups with high affinity for inflammatory chemokine CCL2 does not contain 3-O-sulfated disaccharides.
CID was used to distinguish between heparin disaccharide isomers containing or lacking 3-O-sulfation and applied to evaluate the involvement of 3-O-sulfation in the heparin/CCL2 interaction.</description><subject>Analytical Chemistry</subject><subject>Animals</subject><subject>Anticoagulants</subject><subject>Binding</subject><subject>Binding Sites</subject><subject>Bioinformatics</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chemokine CCL2 - chemistry</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>Differentiation</subject><subject>Disaccharides - chemistry</subject><subject>Glycosaminoglycans - chemistry</subject><subject>Heparan sulfate</subject><subject>Heparin - analogs & derivatives</subject><subject>Heparin - chemistry</subject><subject>Humans</subject><subject>Isomerism</subject><subject>Isomers</subject><subject>Mass spectrometry</subject><subject>Oligosaccharides - chemistry</subject><subject>Organic Chemistry</subject><subject>Protein Binding</subject><subject>Proteomics</subject><subject>Sulfates - chemistry</subject><subject>Tandem Mass Spectrometry - methods</subject><issn>1044-0305</issn><issn>1879-1123</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9kU9r3DAQxU1paf60n6BQDIXe7EiyZMuFFpJNmyxsySHtWWil0a6MLW0kO5B7Pni12WWb9pCTBs37vZnhZdkHjEqMcH3WlZ2MQywJQrzEpESIvMqOMW_aAmNSvU41orRAFWJH2UmMHUK4QW3zNjvCLeaMYXqcPV5aYyCAG60crXe5N3lV3BS3U2_kCDq_ho0M1uWXNkql1qnWkM-jHyDEL_lcb0lj1QG-HcOkxinIPj-PG1Bj3P6Oazg4zWYLkl9Yp61b5T99wt9lb4zsI7zfv6fZ7x_ff82ui8XN1Xx2vigUq9BYcJpOZUtZyxa1taSKAdKkBkYl5QawMjUykkELhBjNOVfLWiMMNZeYUFxVp9m3ne9mWg6gVdo97Sk2wQ4yPAgvrfi34-xarPy9IA3j_Mng894g-LsJ4igGGxX0vXTgpyjqBtGm4jwJP_0n7PwUXDpO4JZhRpqW0KSqdioVfIwBzGEVjMQ2Y9GJp4zFNmOBiUgZJ-rj8yv-MvtQk4DuBDG13ArCs-Ev-n7dYZAiuLcJi8qCU6BtSDkK7e2L_B8Ey8u0</recordid><startdate>20090401</startdate><enddate>20090401</enddate><creator>Meissen, John K.</creator><creator>Sweeney, Matthew D.</creator><creator>Girardi, Matthew</creator><creator>Lawrence, Roger</creator><creator>Esko, Jeffrey D.</creator><creator>Leary, Julie A.</creator><general>Elsevier Inc</general><general>Springer-Verlag</general><general>Springer Nature B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FG</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090401</creationdate><title>Differentiation of 3-O-Sulfated Heparin Disaccharide Isomers: Identification of Structural Aspects of the Heparin CCL2 Binding Motif</title><author>Meissen, John K. ; Sweeney, Matthew D. ; Girardi, Matthew ; Lawrence, Roger ; Esko, Jeffrey D. ; Leary, Julie A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c530t-842005ba6a9096a4c5e0d26e54a48fe1cf60fa5e9e22fd888cb6d01e68a124133</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Analytical Chemistry</topic><topic>Animals</topic><topic>Anticoagulants</topic><topic>Binding</topic><topic>Binding Sites</topic><topic>Bioinformatics</topic><topic>Biotechnology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chemokine CCL2 - chemistry</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Cricetulus</topic><topic>Differentiation</topic><topic>Disaccharides - chemistry</topic><topic>Glycosaminoglycans - chemistry</topic><topic>Heparan sulfate</topic><topic>Heparin - analogs & derivatives</topic><topic>Heparin - chemistry</topic><topic>Humans</topic><topic>Isomerism</topic><topic>Isomers</topic><topic>Mass spectrometry</topic><topic>Oligosaccharides - chemistry</topic><topic>Organic Chemistry</topic><topic>Protein Binding</topic><topic>Proteomics</topic><topic>Sulfates - chemistry</topic><topic>Tandem Mass Spectrometry - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Meissen, John K.</creatorcontrib><creatorcontrib>Sweeney, Matthew D.</creatorcontrib><creatorcontrib>Girardi, Matthew</creatorcontrib><creatorcontrib>Lawrence, Roger</creatorcontrib><creatorcontrib>Esko, Jeffrey D.</creatorcontrib><creatorcontrib>Leary, Julie A.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of the American Society for Mass Spectrometry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Meissen, John K.</au><au>Sweeney, Matthew D.</au><au>Girardi, Matthew</au><au>Lawrence, Roger</au><au>Esko, Jeffrey D.</au><au>Leary, Julie A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differentiation of 3-O-Sulfated Heparin Disaccharide Isomers: Identification of Structural Aspects of the Heparin CCL2 Binding Motif</atitle><jtitle>Journal of the American Society for Mass Spectrometry</jtitle><stitle>J Am Soc Mass Spectrom</stitle><addtitle>J Am Soc Mass Spectrom</addtitle><date>2009-04-01</date><risdate>2009</risdate><volume>20</volume><issue>4</issue><spage>652</spage><epage>657</epage><pages>652-657</pages><issn>1044-0305</issn><eissn>1879-1123</eissn><abstract>The presence of 3-O-sulfated glucosamine residues in heparin or heparan sulfate plays a role in binding to antithrombin III and HSV infection. In this study, tandem mass spectrometry was used to differentiate between two heparin disaccharide isomers containing variable sulfate at C6 in a common disaccharide and C3 in a more rare one. The dissociation patterns shown by MS
2 and MS
3 were clearly distinguishable between the isomers, allowing their differentiation and quantitation. Using this technique, we show that an octasaccharide with 11 sulfate groups with high affinity for inflammatory chemokine CCL2 does not contain 3-O-sulfated disaccharides.
CID was used to distinguish between heparin disaccharide isomers containing or lacking 3-O-sulfation and applied to evaluate the involvement of 3-O-sulfation in the heparin/CCL2 interaction.</abstract><cop>New York</cop><pub>Elsevier Inc</pub><pmid>19185514</pmid><doi>10.1016/j.jasms.2008.12.002</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Analytical Chemistry Animals Anticoagulants Binding Binding Sites Bioinformatics Biotechnology Chemistry Chemistry and Materials Science Chemokine CCL2 - chemistry CHO Cells Cricetinae Cricetulus Differentiation Disaccharides - chemistry Glycosaminoglycans - chemistry Heparan sulfate Heparin - analogs & derivatives Heparin - chemistry Humans Isomerism Isomers Mass spectrometry Oligosaccharides - chemistry Organic Chemistry Protein Binding Proteomics Sulfates - chemistry Tandem Mass Spectrometry - methods |
| title | Differentiation of 3-O-Sulfated Heparin Disaccharide Isomers: Identification of Structural Aspects of the Heparin CCL2 Binding Motif |
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