Vitronectin (Vn) glycosylation patterned by lectin affinity assays—A potent glycoproteomic tool to discriminate plasma Vn from cancer ascites Vn
Changes in glycosylation have been associated with human cancer, but their complexity poses an analytical challenge. Ovarian cancer is a major cause of death in women because of an often late diagnosis. At least one‐third of patients presents ascites fluid at diagnosis, and almost all have ascites a...
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| Veröffentlicht in: | Journal of molecular recognition 2018-05, Vol.31 (5), p.e2690-n/a |
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| creator | Benachour, H. Leroy‐Dudal, J. Agniel, R. Wilson, J. Briand, M. Carreiras, F. Gallet, O. |
| description | Changes in glycosylation have been associated with human cancer, but their complexity poses an analytical challenge. Ovarian cancer is a major cause of death in women because of an often late diagnosis. At least one‐third of patients presents ascites fluid at diagnosis, and almost all have ascites at recurrence. Vitronectin (Vn) is a multifunctional glycoprotein that is suggested to be implicated in ovarian cancer metastasis and is found within ascites. The present study evaluated the potential of using lectin affinity for characterizing the glycosylation pattern of Vn. Human Vn was purified from 1 sample of ovarian cancer ascites or a pool of plasma samples. Consistent findings were observed with both dot blot and lectin array assays. Based on a panel of 40 lectins, the lectin array revealed discriminant patterns of lectin binding to Vn glycans. Interestingly, almost all the highlighted interactions were found to be higher with Vn from ascites relative to the plasma counterpart. Also, the lectin array was able to discriminate profiles of lectin interactions (ConA, SNA‐I, PHA‐E, PHA‐L) between Vn samples that were not evident using dot blot, indicating its high sensitivity. The model of ConA binding during thermal unfolding of Vn confirmed the higher accessibility of mannosylated glycans in Vn from ascites as monitored by turbidimetry. Thus, this study demonstrated the usefulness of lectins and the lectin array as a glycoproteomic tool for high throughput and sensitive analysis of glycosylation patterns. Our data provide novel insights concerning Vn glycosylation patterns in clinical specimens, paving the way for further investigations regarding their functional impact and clinical interest.
Vitronectin (Vn) glycoprotein is suggested to be implicated in ovarian cancer metastasis. In this paper, a novel lectin array approach allowed a more comprehensive and high sensitive semi‐quantitative analysis, revealing discriminant patterns of lectin interactions with human Vn glycans according to the Vn sample. The highlighted lectin interactions were found to be higher with Vn glycans from ovarian cancer ascites relative to healthy plasma, suggesting a functional role of Vn glycosylation in cancerogenesis. |
| doi_str_mv | 10.1002/jmr.2690 |
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Vitronectin (Vn) glycoprotein is suggested to be implicated in ovarian cancer metastasis. In this paper, a novel lectin array approach allowed a more comprehensive and high sensitive semi‐quantitative analysis, revealing discriminant patterns of lectin interactions with human Vn glycans according to the Vn sample. The highlighted lectin interactions were found to be higher with Vn glycans from ovarian cancer ascites relative to healthy plasma, suggesting a functional role of Vn glycosylation in cancerogenesis.</description><identifier>ISSN: 0952-3499</identifier><identifier>EISSN: 1099-1352</identifier><identifier>DOI: 10.1002/jmr.2690</identifier><identifier>PMID: 29205553</identifier><language>eng</language><publisher>England: Wiley Subscription Services, Inc</publisher><subject>Affinity ; Ascites ; Binding ; Biochemistry ; Biochemistry, Molecular Biology ; Cancer ; Diagnosis ; extracellular matrix ; Glycoproteins ; glycoproteomics ; Glycosylation ; human plasma ; lectin affinity ; lectin array ; Lectins ; Life Sciences ; Metastases ; Ovarian cancer ; ovarian cancer ascites ; Polysaccharides ; Turbidimetry ; Vitronectin</subject><ispartof>Journal of molecular recognition, 2018-05, Vol.31 (5), p.e2690-n/a</ispartof><rights>Copyright © 2017 John Wiley & Sons, Ltd.</rights><rights>Copyright © 2018 John Wiley & Sons, Ltd.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2980-a1fbc713fd78c3c915d4d121b6c65a49285641aa9efba50ff88d1b5a5f8154023</citedby><cites>FETCH-LOGICAL-c2980-a1fbc713fd78c3c915d4d121b6c65a49285641aa9efba50ff88d1b5a5f8154023</cites><orcidid>0000-0002-2956-7532 ; 0000-0003-4254-4703</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjmr.2690$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjmr.2690$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,315,781,785,886,1418,27929,27930,45579,45580</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29205553$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://cyu.hal.science/hal-01927243$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Benachour, H.</creatorcontrib><creatorcontrib>Leroy‐Dudal, J.</creatorcontrib><creatorcontrib>Agniel, R.</creatorcontrib><creatorcontrib>Wilson, J.</creatorcontrib><creatorcontrib>Briand, M.</creatorcontrib><creatorcontrib>Carreiras, F.</creatorcontrib><creatorcontrib>Gallet, O.</creatorcontrib><title>Vitronectin (Vn) glycosylation patterned by lectin affinity assays—A potent glycoproteomic tool to discriminate plasma Vn from cancer ascites Vn</title><title>Journal of molecular recognition</title><addtitle>J Mol Recognit</addtitle><description>Changes in glycosylation have been associated with human cancer, but their complexity poses an analytical challenge. Ovarian cancer is a major cause of death in women because of an often late diagnosis. At least one‐third of patients presents ascites fluid at diagnosis, and almost all have ascites at recurrence. Vitronectin (Vn) is a multifunctional glycoprotein that is suggested to be implicated in ovarian cancer metastasis and is found within ascites. The present study evaluated the potential of using lectin affinity for characterizing the glycosylation pattern of Vn. Human Vn was purified from 1 sample of ovarian cancer ascites or a pool of plasma samples. Consistent findings were observed with both dot blot and lectin array assays. Based on a panel of 40 lectins, the lectin array revealed discriminant patterns of lectin binding to Vn glycans. Interestingly, almost all the highlighted interactions were found to be higher with Vn from ascites relative to the plasma counterpart. Also, the lectin array was able to discriminate profiles of lectin interactions (ConA, SNA‐I, PHA‐E, PHA‐L) between Vn samples that were not evident using dot blot, indicating its high sensitivity. The model of ConA binding during thermal unfolding of Vn confirmed the higher accessibility of mannosylated glycans in Vn from ascites as monitored by turbidimetry. Thus, this study demonstrated the usefulness of lectins and the lectin array as a glycoproteomic tool for high throughput and sensitive analysis of glycosylation patterns. Our data provide novel insights concerning Vn glycosylation patterns in clinical specimens, paving the way for further investigations regarding their functional impact and clinical interest.
Vitronectin (Vn) glycoprotein is suggested to be implicated in ovarian cancer metastasis. In this paper, a novel lectin array approach allowed a more comprehensive and high sensitive semi‐quantitative analysis, revealing discriminant patterns of lectin interactions with human Vn glycans according to the Vn sample. The highlighted lectin interactions were found to be higher with Vn glycans from ovarian cancer ascites relative to healthy plasma, suggesting a functional role of Vn glycosylation in cancerogenesis.</description><subject>Affinity</subject><subject>Ascites</subject><subject>Binding</subject><subject>Biochemistry</subject><subject>Biochemistry, Molecular Biology</subject><subject>Cancer</subject><subject>Diagnosis</subject><subject>extracellular matrix</subject><subject>Glycoproteins</subject><subject>glycoproteomics</subject><subject>Glycosylation</subject><subject>human plasma</subject><subject>lectin affinity</subject><subject>lectin array</subject><subject>Lectins</subject><subject>Life Sciences</subject><subject>Metastases</subject><subject>Ovarian cancer</subject><subject>ovarian cancer ascites</subject><subject>Polysaccharides</subject><subject>Turbidimetry</subject><subject>Vitronectin</subject><issn>0952-3499</issn><issn>1099-1352</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNp1kdFuFCEUhonR2LWa-ASGxJv2Yioww-xwuWnUataYGN1bcoYBZcPACKxm7voMjU_ok8g6tTEm3kA4fHw5hx-hp5RcUELYi_0YL1gryD20okSIitac3UcrIjir6kaIE_QopT0h5Y6Th-iECUY45_UK3exsjsFrla3HZzt_jj-7WYU0O8g2eDxBzjp6PeB-xm7BwBjrbZ4xpARz-nn9Y4OnkLXPy-MplkMYrcI5BFcWPNikoh2th6zx5CCNgHcemxhGrMArHYtL2axTKT9GDwy4pJ_c7qfo06uXHy-vqu37128uN9tKMdGRCqjp1ZrWZlh3qlaC8qEZKKN9q1oOjWAdbxsKILTpgRNjum6gPQduOsobwupTdL54v4CTU2kP4iwDWHm12cpjjVDB1qypv9HCni1sme3rQacsxzKSdg68DockqVjXhLHy1QV9_g-6D4foyySSEcYFaUn7l1DFkFLU5q4DSuQxU1kylcdMC_rsVnjoRz3cgX9CLEC1AN-t0_N_RfLtuw-_hb8ACCas7A</recordid><startdate>201805</startdate><enddate>201805</enddate><creator>Benachour, H.</creator><creator>Leroy‐Dudal, J.</creator><creator>Agniel, R.</creator><creator>Wilson, J.</creator><creator>Briand, M.</creator><creator>Carreiras, F.</creator><creator>Gallet, O.</creator><general>Wiley Subscription Services, Inc</general><general>Wiley</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QO</scope><scope>7QP</scope><scope>7QQ</scope><scope>7SE</scope><scope>7SR</scope><scope>7TA</scope><scope>7TK</scope><scope>7TM</scope><scope>8BQ</scope><scope>8FD</scope><scope>F28</scope><scope>FR3</scope><scope>H8G</scope><scope>JG9</scope><scope>P64</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-2956-7532</orcidid><orcidid>https://orcid.org/0000-0003-4254-4703</orcidid></search><sort><creationdate>201805</creationdate><title>Vitronectin (Vn) glycosylation patterned by lectin affinity assays—A potent glycoproteomic tool to discriminate plasma Vn from cancer ascites Vn</title><author>Benachour, H. ; Leroy‐Dudal, J. ; Agniel, R. ; Wilson, J. ; Briand, M. ; Carreiras, F. ; Gallet, O.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2980-a1fbc713fd78c3c915d4d121b6c65a49285641aa9efba50ff88d1b5a5f8154023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Affinity</topic><topic>Ascites</topic><topic>Binding</topic><topic>Biochemistry</topic><topic>Biochemistry, Molecular Biology</topic><topic>Cancer</topic><topic>Diagnosis</topic><topic>extracellular matrix</topic><topic>Glycoproteins</topic><topic>glycoproteomics</topic><topic>Glycosylation</topic><topic>human plasma</topic><topic>lectin affinity</topic><topic>lectin array</topic><topic>Lectins</topic><topic>Life Sciences</topic><topic>Metastases</topic><topic>Ovarian cancer</topic><topic>ovarian cancer ascites</topic><topic>Polysaccharides</topic><topic>Turbidimetry</topic><topic>Vitronectin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Benachour, H.</creatorcontrib><creatorcontrib>Leroy‐Dudal, J.</creatorcontrib><creatorcontrib>Agniel, R.</creatorcontrib><creatorcontrib>Wilson, J.</creatorcontrib><creatorcontrib>Briand, M.</creatorcontrib><creatorcontrib>Carreiras, F.</creatorcontrib><creatorcontrib>Gallet, O.</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Materials Business File</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Copper Technical Reference Library</collection><collection>Materials Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Journal of molecular recognition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Benachour, H.</au><au>Leroy‐Dudal, J.</au><au>Agniel, R.</au><au>Wilson, J.</au><au>Briand, M.</au><au>Carreiras, F.</au><au>Gallet, O.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Vitronectin (Vn) glycosylation patterned by lectin affinity assays—A potent glycoproteomic tool to discriminate plasma Vn from cancer ascites Vn</atitle><jtitle>Journal of molecular recognition</jtitle><addtitle>J Mol Recognit</addtitle><date>2018-05</date><risdate>2018</risdate><volume>31</volume><issue>5</issue><spage>e2690</spage><epage>n/a</epage><pages>e2690-n/a</pages><issn>0952-3499</issn><eissn>1099-1352</eissn><abstract>Changes in glycosylation have been associated with human cancer, but their complexity poses an analytical challenge. Ovarian cancer is a major cause of death in women because of an often late diagnosis. At least one‐third of patients presents ascites fluid at diagnosis, and almost all have ascites at recurrence. Vitronectin (Vn) is a multifunctional glycoprotein that is suggested to be implicated in ovarian cancer metastasis and is found within ascites. The present study evaluated the potential of using lectin affinity for characterizing the glycosylation pattern of Vn. Human Vn was purified from 1 sample of ovarian cancer ascites or a pool of plasma samples. Consistent findings were observed with both dot blot and lectin array assays. Based on a panel of 40 lectins, the lectin array revealed discriminant patterns of lectin binding to Vn glycans. Interestingly, almost all the highlighted interactions were found to be higher with Vn from ascites relative to the plasma counterpart. Also, the lectin array was able to discriminate profiles of lectin interactions (ConA, SNA‐I, PHA‐E, PHA‐L) between Vn samples that were not evident using dot blot, indicating its high sensitivity. The model of ConA binding during thermal unfolding of Vn confirmed the higher accessibility of mannosylated glycans in Vn from ascites as monitored by turbidimetry. Thus, this study demonstrated the usefulness of lectins and the lectin array as a glycoproteomic tool for high throughput and sensitive analysis of glycosylation patterns. Our data provide novel insights concerning Vn glycosylation patterns in clinical specimens, paving the way for further investigations regarding their functional impact and clinical interest.
Vitronectin (Vn) glycoprotein is suggested to be implicated in ovarian cancer metastasis. In this paper, a novel lectin array approach allowed a more comprehensive and high sensitive semi‐quantitative analysis, revealing discriminant patterns of lectin interactions with human Vn glycans according to the Vn sample. The highlighted lectin interactions were found to be higher with Vn glycans from ovarian cancer ascites relative to healthy plasma, suggesting a functional role of Vn glycosylation in cancerogenesis.</abstract><cop>England</cop><pub>Wiley Subscription Services, Inc</pub><pmid>29205553</pmid><doi>10.1002/jmr.2690</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0002-2956-7532</orcidid><orcidid>https://orcid.org/0000-0003-4254-4703</orcidid></addata></record> |
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| subjects | Affinity Ascites Binding Biochemistry Biochemistry, Molecular Biology Cancer Diagnosis extracellular matrix Glycoproteins glycoproteomics Glycosylation human plasma lectin affinity lectin array Lectins Life Sciences Metastases Ovarian cancer ovarian cancer ascites Polysaccharides Turbidimetry Vitronectin |
| title | Vitronectin (Vn) glycosylation patterned by lectin affinity assays—A potent glycoproteomic tool to discriminate plasma Vn from cancer ascites Vn |
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