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...
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Veröffentlicht in: | Molecular bioSystems 2017, Vol.13 (11), p.2303-2309 |
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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 |
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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. 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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. 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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. 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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 |
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