Recognition of galactan components of pectin by galectin‐3
It has been reported that modified forms of pectin possess anticancer activity. To account for this bioactivity, it has been proposed that fragments of pectin molecules can act by binding to and inhibiting the various roles of the mammalian protein galectin 3 (Gal3) in cancer progression and metasta...
Gespeichert in:
| Veröffentlicht in: | The FASEB journal 2009-02, Vol.23 (2), p.415-424 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 424 |
|---|---|
| container_issue | 2 |
| container_start_page | 415 |
| container_title | The FASEB journal |
| container_volume | 23 |
| creator | Gunning, A. Patrick Bongaerts, Roy J. M. Morris, Victor J. |
| description | It has been reported that modified forms of pectin possess anticancer activity. To account for this bioactivity, it has been proposed that fragments of pectin molecules can act by binding to and inhibiting the various roles of the mammalian protein galectin 3 (Gal3) in cancer progression and metastasis. Despite this clear molecular hypothesis and evidence for the bioactivity of modified pectin, the structural origins of the “bioactive fragments” of pectin molecules are currently ill defined. By using a combination of fluorescence microscopy, flow cytometry, and force spectroscopy, it has been possible to demonstrate, for the first time, specific binding of a pectin galactan to the recombinant form of human Gal3. Present studies suggest that bioactivity resides in the neutral sugar side chains of pectin polysaccharides and that these components could be isolated and modified to optimize bioactivity.—Gunning, A. P., Bongaerts, R. J. M., Morris, V. J. Recognition of galactan components of pectin by galectin‐3. FASEB J. 23, 415–424 (2009) |
| doi_str_mv | 10.1096/fj.08-106617 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_66864833</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>66864833</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4347-2cc2f6c4f508f8823c88a6e39a936b3680615611f480ebf5fcce690f345b48953</originalsourceid><addsrcrecordid>eNp9kEtLw0AQgBdRbH3cPEtOnkydzSbTCXjRYn1QEHycl826W1KSbMymSG_-BH-jv8TUBLx5mmH4-GA-xk44TDikeGFXE6CQAyKf7rAxTwSESAi7bAyURiGioBE78H4FABw47rMRJxJRkuKYXT4Z7ZZV3uauCpwNlqpQulVVoF1Zu8pUrd-ea6PbvAqyzRb43b8_v8QR27Oq8OZ4mIfsdX7zMrsLF4-397OrRahjEU_DSOvIoo5tAmSJIqGJFBqRqlRgJpAAeYKc25jAZDaxWhtMwYo4yWJKE3HIznpv3bj3tfGtLHOvTVGoyri1l9j9G5MQHXjeg7px3jfGyrrJS9VsJAe5rSXtSgLJvlaHnw7edVaatz94yNMB1AMfeWE2_8rk_Pk6mj8ADe4fE-V1WQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>66864833</pqid></control><display><type>article</type><title>Recognition of galactan components of pectin by galectin‐3</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Alma/SFX Local Collection</source><creator>Gunning, A. Patrick ; Bongaerts, Roy J. M. ; Morris, Victor J.</creator><creatorcontrib>Gunning, A. Patrick ; Bongaerts, Roy J. M. ; Morris, Victor J.</creatorcontrib><description>It has been reported that modified forms of pectin possess anticancer activity. To account for this bioactivity, it has been proposed that fragments of pectin molecules can act by binding to and inhibiting the various roles of the mammalian protein galectin 3 (Gal3) in cancer progression and metastasis. Despite this clear molecular hypothesis and evidence for the bioactivity of modified pectin, the structural origins of the “bioactive fragments” of pectin molecules are currently ill defined. By using a combination of fluorescence microscopy, flow cytometry, and force spectroscopy, it has been possible to demonstrate, for the first time, specific binding of a pectin galactan to the recombinant form of human Gal3. Present studies suggest that bioactivity resides in the neutral sugar side chains of pectin polysaccharides and that these components could be isolated and modified to optimize bioactivity.—Gunning, A. P., Bongaerts, R. J. M., Morris, V. J. Recognition of galactan components of pectin by galectin‐3. FASEB J. 23, 415–424 (2009)</description><identifier>ISSN: 0892-6638</identifier><identifier>EISSN: 1530-6860</identifier><identifier>DOI: 10.1096/fj.08-106617</identifier><identifier>PMID: 18832596</identifier><language>eng</language><publisher>United States: Federation of American Societies for Experimental Biology</publisher><subject>AFM ; antimetastasis activity ; Carbohydrate Sequence ; flow cytometry ; Galactans - chemistry ; Galactans - metabolism ; Galactans - ultrastructure ; Galectin 3 - chemistry ; Galectin 3 - metabolism ; Magnetic Resonance Spectroscopy ; Microscopy, Atomic Force ; Microscopy, Electron, Scanning ; Molecular Sequence Data ; Pectins - chemistry ; Pectins - metabolism ; polygalacturonic acid ; RGI ; Solanum tuberosum - chemistry ; Solanum tuberosum - metabolism</subject><ispartof>The FASEB journal, 2009-02, Vol.23 (2), p.415-424</ispartof><rights>FASEB</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4347-2cc2f6c4f508f8823c88a6e39a936b3680615611f480ebf5fcce690f345b48953</citedby><cites>FETCH-LOGICAL-c4347-2cc2f6c4f508f8823c88a6e39a936b3680615611f480ebf5fcce690f345b48953</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1096%2Ffj.08-106617$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1096%2Ffj.08-106617$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,777,781,1412,27905,27906,45555,45556</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18832596$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gunning, A. Patrick</creatorcontrib><creatorcontrib>Bongaerts, Roy J. M.</creatorcontrib><creatorcontrib>Morris, Victor J.</creatorcontrib><title>Recognition of galactan components of pectin by galectin‐3</title><title>The FASEB journal</title><addtitle>FASEB J</addtitle><description>It has been reported that modified forms of pectin possess anticancer activity. To account for this bioactivity, it has been proposed that fragments of pectin molecules can act by binding to and inhibiting the various roles of the mammalian protein galectin 3 (Gal3) in cancer progression and metastasis. Despite this clear molecular hypothesis and evidence for the bioactivity of modified pectin, the structural origins of the “bioactive fragments” of pectin molecules are currently ill defined. By using a combination of fluorescence microscopy, flow cytometry, and force spectroscopy, it has been possible to demonstrate, for the first time, specific binding of a pectin galactan to the recombinant form of human Gal3. Present studies suggest that bioactivity resides in the neutral sugar side chains of pectin polysaccharides and that these components could be isolated and modified to optimize bioactivity.—Gunning, A. P., Bongaerts, R. J. M., Morris, V. J. Recognition of galactan components of pectin by galectin‐3. FASEB J. 23, 415–424 (2009)</description><subject>AFM</subject><subject>antimetastasis activity</subject><subject>Carbohydrate Sequence</subject><subject>flow cytometry</subject><subject>Galactans - chemistry</subject><subject>Galactans - metabolism</subject><subject>Galactans - ultrastructure</subject><subject>Galectin 3 - chemistry</subject><subject>Galectin 3 - metabolism</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Microscopy, Atomic Force</subject><subject>Microscopy, Electron, Scanning</subject><subject>Molecular Sequence Data</subject><subject>Pectins - chemistry</subject><subject>Pectins - metabolism</subject><subject>polygalacturonic acid</subject><subject>RGI</subject><subject>Solanum tuberosum - chemistry</subject><subject>Solanum tuberosum - metabolism</subject><issn>0892-6638</issn><issn>1530-6860</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLw0AQgBdRbH3cPEtOnkydzSbTCXjRYn1QEHycl826W1KSbMymSG_-BH-jv8TUBLx5mmH4-GA-xk44TDikeGFXE6CQAyKf7rAxTwSESAi7bAyURiGioBE78H4FABw47rMRJxJRkuKYXT4Z7ZZV3uauCpwNlqpQulVVoF1Zu8pUrd-ea6PbvAqyzRb43b8_v8QR27Oq8OZ4mIfsdX7zMrsLF4-397OrRahjEU_DSOvIoo5tAmSJIqGJFBqRqlRgJpAAeYKc25jAZDaxWhtMwYo4yWJKE3HIznpv3bj3tfGtLHOvTVGoyri1l9j9G5MQHXjeg7px3jfGyrrJS9VsJAe5rSXtSgLJvlaHnw7edVaatz94yNMB1AMfeWE2_8rk_Pk6mj8ADe4fE-V1WQ</recordid><startdate>200902</startdate><enddate>200902</enddate><creator>Gunning, A. Patrick</creator><creator>Bongaerts, Roy J. M.</creator><creator>Morris, Victor J.</creator><general>Federation of American Societies for Experimental Biology</general><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>7X8</scope></search><sort><creationdate>200902</creationdate><title>Recognition of galactan components of pectin by galectin‐3</title><author>Gunning, A. Patrick ; Bongaerts, Roy J. M. ; Morris, Victor J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4347-2cc2f6c4f508f8823c88a6e39a936b3680615611f480ebf5fcce690f345b48953</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>AFM</topic><topic>antimetastasis activity</topic><topic>Carbohydrate Sequence</topic><topic>flow cytometry</topic><topic>Galactans - chemistry</topic><topic>Galactans - metabolism</topic><topic>Galactans - ultrastructure</topic><topic>Galectin 3 - chemistry</topic><topic>Galectin 3 - metabolism</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Microscopy, Atomic Force</topic><topic>Microscopy, Electron, Scanning</topic><topic>Molecular Sequence Data</topic><topic>Pectins - chemistry</topic><topic>Pectins - metabolism</topic><topic>polygalacturonic acid</topic><topic>RGI</topic><topic>Solanum tuberosum - chemistry</topic><topic>Solanum tuberosum - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gunning, A. Patrick</creatorcontrib><creatorcontrib>Bongaerts, Roy J. M.</creatorcontrib><creatorcontrib>Morris, Victor J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The FASEB journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gunning, A. Patrick</au><au>Bongaerts, Roy J. M.</au><au>Morris, Victor J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Recognition of galactan components of pectin by galectin‐3</atitle><jtitle>The FASEB journal</jtitle><addtitle>FASEB J</addtitle><date>2009-02</date><risdate>2009</risdate><volume>23</volume><issue>2</issue><spage>415</spage><epage>424</epage><pages>415-424</pages><issn>0892-6638</issn><eissn>1530-6860</eissn><abstract>It has been reported that modified forms of pectin possess anticancer activity. To account for this bioactivity, it has been proposed that fragments of pectin molecules can act by binding to and inhibiting the various roles of the mammalian protein galectin 3 (Gal3) in cancer progression and metastasis. Despite this clear molecular hypothesis and evidence for the bioactivity of modified pectin, the structural origins of the “bioactive fragments” of pectin molecules are currently ill defined. By using a combination of fluorescence microscopy, flow cytometry, and force spectroscopy, it has been possible to demonstrate, for the first time, specific binding of a pectin galactan to the recombinant form of human Gal3. Present studies suggest that bioactivity resides in the neutral sugar side chains of pectin polysaccharides and that these components could be isolated and modified to optimize bioactivity.—Gunning, A. P., Bongaerts, R. J. M., Morris, V. J. Recognition of galactan components of pectin by galectin‐3. FASEB J. 23, 415–424 (2009)</abstract><cop>United States</cop><pub>Federation of American Societies for Experimental Biology</pub><pmid>18832596</pmid><doi>10.1096/fj.08-106617</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0892-6638 |
| ispartof | The FASEB journal, 2009-02, Vol.23 (2), p.415-424 |
| issn | 0892-6638 1530-6860 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_66864833 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | AFM antimetastasis activity Carbohydrate Sequence flow cytometry Galactans - chemistry Galactans - metabolism Galactans - ultrastructure Galectin 3 - chemistry Galectin 3 - metabolism Magnetic Resonance Spectroscopy Microscopy, Atomic Force Microscopy, Electron, Scanning Molecular Sequence Data Pectins - chemistry Pectins - metabolism polygalacturonic acid RGI Solanum tuberosum - chemistry Solanum tuberosum - metabolism |
| title | Recognition of galactan components of pectin by galectin‐3 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-21T06%3A48%3A45IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Recognition%20of%20galactan%20components%20of%20pectin%20by%20galectin%E2%80%903&rft.jtitle=The%20FASEB%20journal&rft.au=Gunning,%20A.%20Patrick&rft.date=2009-02&rft.volume=23&rft.issue=2&rft.spage=415&rft.epage=424&rft.pages=415-424&rft.issn=0892-6638&rft.eissn=1530-6860&rft_id=info:doi/10.1096/fj.08-106617&rft_dat=%3Cproquest_cross%3E66864833%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=66864833&rft_id=info:pmid/18832596&rfr_iscdi=true |