Mass spectrometry based identification of galectin-3 interacting proteins potentially involved in lung melanoma metastasis

Adhesive interactions between molecules on tumor cells and those on target organs play a key role in organ specific metastasis. Poly-N-acetyl-lactosamine (polyLacNAc) substituted N-oligosaccharides on melanoma cell surface glycoproteins promote lung specific metastasis via galectin-3 by facilitating...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Molecular bioSystems 2017, Vol.13 (11), p.2303-2309
Hauptverfasser: Dange, Manohar C, Bhonsle, Hemangi S, Godbole, Rashmi K, More, Shyam K, Bane, Sanjay M, Kulkarni, Mahesh J, Kalraiya, Rajiv D
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 2309
container_issue 11
container_start_page 2303
container_title Molecular bioSystems
container_volume 13
creator Dange, Manohar C
Bhonsle, Hemangi S
Godbole, Rashmi K
More, Shyam K
Bane, Sanjay M
Kulkarni, Mahesh J
Kalraiya, Rajiv D
description Adhesive interactions between molecules on tumor cells and those on target organs play a key role in organ specific metastasis. Poly-N-acetyl-lactosamine (polyLacNAc) substituted N-oligosaccharides on melanoma cell surface glycoproteins promote lung specific metastasis via galectin-3 by facilitating their arrest and extravasation. This study reports the identification and characterization of galectin-3 interacting proteins using a combination of galectin-3 sepharose affinity and leucoagglutinating phytohemagglutinin (L-PHA) columns. A total of 83 proteins were identified as galectin-3 interacting glycoproteins, of which 35 were constituents of the L-PHA bound fraction, suggesting that these proteins carry polyLacNAc substituted β1,6 branched N-glycans. The identities of some of these proteins, like LAMP-1, LAMP-3, basigin, embigin, and α5 and β1 Integrin, have been confirmed by western blotting, and functional relevance with respect to metastatic properties has been established.
doi_str_mv 10.1039/c7mb00260b
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1936266758</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2010869110</sourcerecordid><originalsourceid>FETCH-LOGICAL-c381t-7576f6de588a1a8910254dfd68ab8201334c0bba68df9e21cfc5b4a88e6df603</originalsourceid><addsrcrecordid>eNpdkU1LAzEQhoMotlYv_gAJeBFhNR-72ezRFr-gxUsP3pZsNikpu5uaZAv115u1tQdhYGbgmXdeeAG4xugBI1o8yrytECIMVSdgjPOUJARl-PQ4s88RuPB-jRDlKUbnYEQ4zzOC6Rh8L4T30G-UDM62KrgdrIRXNTS16oLRRopgbAethivRRMp0CYWmC8qJYVnBjbNBmc7DTezxRDTNLgJb22wHmQ42faRa1YjOtiIOQfhYxl-CMy0ar64OfQKWL8_L2Vsy_3h9nz3NE0k5Dkme5UyzWmWcCyx4gRHJ0lrXjIuKE4QpTSWqKsF4rQtFsNQyq1LBuWK1ZohOwN1eNhr96pUPZWu8VE30o2zvS1xQRhjLMx7R23_o2vaui-bK-AhxVmA8CN7vKems907pcuNMK9yuxKgcAiln-WL6G8g0wjcHyb5qVX1E_xKgP-zMiFI</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2010869110</pqid></control><display><type>article</type><title>Mass spectrometry based identification of galectin-3 interacting proteins potentially involved in lung melanoma metastasis</title><source>MEDLINE</source><source>Royal Society Of Chemistry Journals</source><source>Alma/SFX Local Collection</source><creator>Dange, Manohar C ; Bhonsle, Hemangi S ; Godbole, Rashmi K ; More, Shyam K ; Bane, Sanjay M ; Kulkarni, Mahesh J ; Kalraiya, Rajiv D</creator><creatorcontrib>Dange, Manohar C ; Bhonsle, Hemangi S ; Godbole, Rashmi K ; More, Shyam K ; Bane, Sanjay M ; Kulkarni, Mahesh J ; Kalraiya, Rajiv D</creatorcontrib><description>Adhesive interactions between molecules on tumor cells and those on target organs play a key role in organ specific metastasis. Poly-N-acetyl-lactosamine (polyLacNAc) substituted N-oligosaccharides on melanoma cell surface glycoproteins promote lung specific metastasis via galectin-3 by facilitating their arrest and extravasation. This study reports the identification and characterization of galectin-3 interacting proteins using a combination of galectin-3 sepharose affinity and leucoagglutinating phytohemagglutinin (L-PHA) columns. A total of 83 proteins were identified as galectin-3 interacting glycoproteins, of which 35 were constituents of the L-PHA bound fraction, suggesting that these proteins carry polyLacNAc substituted β1,6 branched N-glycans. The identities of some of these proteins, like LAMP-1, LAMP-3, basigin, embigin, and α5 and β1 Integrin, have been confirmed by western blotting, and functional relevance with respect to metastatic properties has been established.</description><identifier>ISSN: 1742-206X</identifier><identifier>EISSN: 1742-2051</identifier><identifier>DOI: 10.1039/c7mb00260b</identifier><identifier>PMID: 28875213</identifier><language>eng</language><publisher>England: Royal Society of Chemistry</publisher><subject>Animals ; Carrier Proteins - metabolism ; CD147 antigen ; Cell adhesion ; Cell surface ; Chromatography, Affinity ; Chromatography, Liquid ; Extravasation ; Galectin 3 - metabolism ; Galectin-3 ; Glycoproteins ; LAMP-1 protein ; Lung Neoplasms - metabolism ; Lung Neoplasms - secondary ; Lungs ; Mass spectrometry ; Mass Spectrometry - methods ; Mass spectroscopy ; Melanoma ; Melanoma - pathology ; Melanoma, Experimental ; Metastases ; Metastasis ; Mice ; N-glycans ; Oligosaccharides ; Organs ; Polysaccharides ; Protein Binding ; Protein Interaction Mapping - methods ; Proteins ; Reproducibility of Results ; Substitutes ; Tumor cells ; Western blotting ; Workflow</subject><ispartof>Molecular bioSystems, 2017, Vol.13 (11), p.2303-2309</ispartof><rights>Copyright Royal Society of Chemistry 2017</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c381t-7576f6de588a1a8910254dfd68ab8201334c0bba68df9e21cfc5b4a88e6df603</citedby><cites>FETCH-LOGICAL-c381t-7576f6de588a1a8910254dfd68ab8201334c0bba68df9e21cfc5b4a88e6df603</cites><orcidid>0000-0003-3932-9092</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,4025,27925,27926,27927</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28875213$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dange, Manohar C</creatorcontrib><creatorcontrib>Bhonsle, Hemangi S</creatorcontrib><creatorcontrib>Godbole, Rashmi K</creatorcontrib><creatorcontrib>More, Shyam K</creatorcontrib><creatorcontrib>Bane, Sanjay M</creatorcontrib><creatorcontrib>Kulkarni, Mahesh J</creatorcontrib><creatorcontrib>Kalraiya, Rajiv D</creatorcontrib><title>Mass spectrometry based identification of galectin-3 interacting proteins potentially involved in lung melanoma metastasis</title><title>Molecular bioSystems</title><addtitle>Mol Biosyst</addtitle><description>Adhesive interactions between molecules on tumor cells and those on target organs play a key role in organ specific metastasis. Poly-N-acetyl-lactosamine (polyLacNAc) substituted N-oligosaccharides on melanoma cell surface glycoproteins promote lung specific metastasis via galectin-3 by facilitating their arrest and extravasation. This study reports the identification and characterization of galectin-3 interacting proteins using a combination of galectin-3 sepharose affinity and leucoagglutinating phytohemagglutinin (L-PHA) columns. A total of 83 proteins were identified as galectin-3 interacting glycoproteins, of which 35 were constituents of the L-PHA bound fraction, suggesting that these proteins carry polyLacNAc substituted β1,6 branched N-glycans. The identities of some of these proteins, like LAMP-1, LAMP-3, basigin, embigin, and α5 and β1 Integrin, have been confirmed by western blotting, and functional relevance with respect to metastatic properties has been established.</description><subject>Animals</subject><subject>Carrier Proteins - metabolism</subject><subject>CD147 antigen</subject><subject>Cell adhesion</subject><subject>Cell surface</subject><subject>Chromatography, Affinity</subject><subject>Chromatography, Liquid</subject><subject>Extravasation</subject><subject>Galectin 3 - metabolism</subject><subject>Galectin-3</subject><subject>Glycoproteins</subject><subject>LAMP-1 protein</subject><subject>Lung Neoplasms - metabolism</subject><subject>Lung Neoplasms - secondary</subject><subject>Lungs</subject><subject>Mass spectrometry</subject><subject>Mass Spectrometry - methods</subject><subject>Mass spectroscopy</subject><subject>Melanoma</subject><subject>Melanoma - pathology</subject><subject>Melanoma, Experimental</subject><subject>Metastases</subject><subject>Metastasis</subject><subject>Mice</subject><subject>N-glycans</subject><subject>Oligosaccharides</subject><subject>Organs</subject><subject>Polysaccharides</subject><subject>Protein Binding</subject><subject>Protein Interaction Mapping - methods</subject><subject>Proteins</subject><subject>Reproducibility of Results</subject><subject>Substitutes</subject><subject>Tumor cells</subject><subject>Western blotting</subject><subject>Workflow</subject><issn>1742-206X</issn><issn>1742-2051</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkU1LAzEQhoMotlYv_gAJeBFhNR-72ezRFr-gxUsP3pZsNikpu5uaZAv115u1tQdhYGbgmXdeeAG4xugBI1o8yrytECIMVSdgjPOUJARl-PQ4s88RuPB-jRDlKUbnYEQ4zzOC6Rh8L4T30G-UDM62KrgdrIRXNTS16oLRRopgbAethivRRMp0CYWmC8qJYVnBjbNBmc7DTezxRDTNLgJb22wHmQ42faRa1YjOtiIOQfhYxl-CMy0ar64OfQKWL8_L2Vsy_3h9nz3NE0k5Dkme5UyzWmWcCyx4gRHJ0lrXjIuKE4QpTSWqKsF4rQtFsNQyq1LBuWK1ZohOwN1eNhr96pUPZWu8VE30o2zvS1xQRhjLMx7R23_o2vaui-bK-AhxVmA8CN7vKems907pcuNMK9yuxKgcAiln-WL6G8g0wjcHyb5qVX1E_xKgP-zMiFI</recordid><startdate>2017</startdate><enddate>2017</enddate><creator>Dange, Manohar C</creator><creator>Bhonsle, Hemangi S</creator><creator>Godbole, Rashmi K</creator><creator>More, Shyam K</creator><creator>Bane, Sanjay M</creator><creator>Kulkarni, Mahesh J</creator><creator>Kalraiya, Rajiv D</creator><general>Royal Society of Chemistry</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>7QO</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0003-3932-9092</orcidid></search><sort><creationdate>2017</creationdate><title>Mass spectrometry based identification of galectin-3 interacting proteins potentially involved in lung melanoma metastasis</title><author>Dange, Manohar C ; Bhonsle, Hemangi S ; Godbole, Rashmi K ; More, Shyam K ; Bane, Sanjay M ; Kulkarni, Mahesh J ; Kalraiya, Rajiv D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c381t-7576f6de588a1a8910254dfd68ab8201334c0bba68df9e21cfc5b4a88e6df603</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Animals</topic><topic>Carrier Proteins - metabolism</topic><topic>CD147 antigen</topic><topic>Cell adhesion</topic><topic>Cell surface</topic><topic>Chromatography, Affinity</topic><topic>Chromatography, Liquid</topic><topic>Extravasation</topic><topic>Galectin 3 - metabolism</topic><topic>Galectin-3</topic><topic>Glycoproteins</topic><topic>LAMP-1 protein</topic><topic>Lung Neoplasms - metabolism</topic><topic>Lung Neoplasms - secondary</topic><topic>Lungs</topic><topic>Mass spectrometry</topic><topic>Mass Spectrometry - methods</topic><topic>Mass spectroscopy</topic><topic>Melanoma</topic><topic>Melanoma - pathology</topic><topic>Melanoma, Experimental</topic><topic>Metastases</topic><topic>Metastasis</topic><topic>Mice</topic><topic>N-glycans</topic><topic>Oligosaccharides</topic><topic>Organs</topic><topic>Polysaccharides</topic><topic>Protein Binding</topic><topic>Protein Interaction Mapping - methods</topic><topic>Proteins</topic><topic>Reproducibility of Results</topic><topic>Substitutes</topic><topic>Tumor cells</topic><topic>Western blotting</topic><topic>Workflow</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dange, Manohar C</creatorcontrib><creatorcontrib>Bhonsle, Hemangi S</creatorcontrib><creatorcontrib>Godbole, Rashmi K</creatorcontrib><creatorcontrib>More, Shyam K</creatorcontrib><creatorcontrib>Bane, Sanjay M</creatorcontrib><creatorcontrib>Kulkarni, Mahesh J</creatorcontrib><creatorcontrib>Kalraiya, Rajiv D</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular bioSystems</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dange, Manohar C</au><au>Bhonsle, Hemangi S</au><au>Godbole, Rashmi K</au><au>More, Shyam K</au><au>Bane, Sanjay M</au><au>Kulkarni, Mahesh J</au><au>Kalraiya, Rajiv D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mass spectrometry based identification of galectin-3 interacting proteins potentially involved in lung melanoma metastasis</atitle><jtitle>Molecular bioSystems</jtitle><addtitle>Mol Biosyst</addtitle><date>2017</date><risdate>2017</risdate><volume>13</volume><issue>11</issue><spage>2303</spage><epage>2309</epage><pages>2303-2309</pages><issn>1742-206X</issn><eissn>1742-2051</eissn><abstract>Adhesive interactions between molecules on tumor cells and those on target organs play a key role in organ specific metastasis. Poly-N-acetyl-lactosamine (polyLacNAc) substituted N-oligosaccharides on melanoma cell surface glycoproteins promote lung specific metastasis via galectin-3 by facilitating their arrest and extravasation. This study reports the identification and characterization of galectin-3 interacting proteins using a combination of galectin-3 sepharose affinity and leucoagglutinating phytohemagglutinin (L-PHA) columns. A total of 83 proteins were identified as galectin-3 interacting glycoproteins, of which 35 were constituents of the L-PHA bound fraction, suggesting that these proteins carry polyLacNAc substituted β1,6 branched N-glycans. The identities of some of these proteins, like LAMP-1, LAMP-3, basigin, embigin, and α5 and β1 Integrin, have been confirmed by western blotting, and functional relevance with respect to metastatic properties has been established.</abstract><cop>England</cop><pub>Royal Society of Chemistry</pub><pmid>28875213</pmid><doi>10.1039/c7mb00260b</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0003-3932-9092</orcidid></addata></record>
fulltext fulltext
identifier ISSN: 1742-206X
ispartof Molecular bioSystems, 2017, Vol.13 (11), p.2303-2309
issn 1742-206X
1742-2051
language eng
recordid cdi_proquest_miscellaneous_1936266758
source MEDLINE; Royal Society Of Chemistry Journals; Alma/SFX Local Collection
subjects Animals
Carrier Proteins - metabolism
CD147 antigen
Cell adhesion
Cell surface
Chromatography, Affinity
Chromatography, Liquid
Extravasation
Galectin 3 - metabolism
Galectin-3
Glycoproteins
LAMP-1 protein
Lung Neoplasms - metabolism
Lung Neoplasms - secondary
Lungs
Mass spectrometry
Mass Spectrometry - methods
Mass spectroscopy
Melanoma
Melanoma - pathology
Melanoma, Experimental
Metastases
Metastasis
Mice
N-glycans
Oligosaccharides
Organs
Polysaccharides
Protein Binding
Protein Interaction Mapping - methods
Proteins
Reproducibility of Results
Substitutes
Tumor cells
Western blotting
Workflow
title Mass spectrometry based identification of galectin-3 interacting proteins potentially involved in lung melanoma metastasis
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-17T17%3A50%3A09IST&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=Mass%20spectrometry%20based%20identification%20of%20galectin-3%20interacting%20proteins%20potentially%20involved%20in%20lung%20melanoma%20metastasis&rft.jtitle=Molecular%20bioSystems&rft.au=Dange,%20Manohar%20C&rft.date=2017&rft.volume=13&rft.issue=11&rft.spage=2303&rft.epage=2309&rft.pages=2303-2309&rft.issn=1742-206X&rft.eissn=1742-2051&rft_id=info:doi/10.1039/c7mb00260b&rft_dat=%3Cproquest_cross%3E2010869110%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=2010869110&rft_id=info:pmid/28875213&rfr_iscdi=true