Interactions between galectin-3 and mac-2-binding protein mediate cell-cell adhesion
Galectin-3 is a beta-galactoside-specific lectin implicated in diverse processes involved in cellular interactions. Recently, the Mac-2-binding protein, a heavily N-glycosylated secreted protein with a subunit Mr of 97,000, was identified as its ligand. The present study characterizes the interactio...
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| Veröffentlicht in: | Cancer research (Chicago, Ill.) Ill.), 1996-10, Vol.56 (19), p.4530-4534 |
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| container_title | Cancer research (Chicago, Ill.) |
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| creator | INOHARA, H AKAHANI, S KOTHS, K RAZ, A |
| description | Galectin-3 is a beta-galactoside-specific lectin implicated in diverse processes involved in cellular interactions. Recently, the Mac-2-binding protein, a heavily N-glycosylated secreted protein with a subunit Mr of 97,000, was identified as its ligand. The present study characterizes the interaction between galectin-3 and Mac-2-binding protein in whole cells and measures their relative expression levels. Incubation of A375 cells with affinity-purified Mac-2-binding protein resulted in its binding to galectin-3 on the cell surface in a specific carbohydrate-dependent manner. Mac-2-binding protein also induced homotypic cell aggregation, which was inhibited by lactose or Fab' fragments of an anti-galectin-3 antibody. Northern blotting analysis revealed differences in the transcriptional regulation of galectin-3 and Mac-2-binding protein. These results provide the first direct evidence for a Mac-2-binding protein function and suggest that it may play a role in tumor cell embolization during metastasis through interaction with galectin-3. |
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These results provide the first direct evidence for a Mac-2-binding protein function and suggest that it may play a role in tumor cell embolization during metastasis through interaction with galectin-3.</description><identifier>ISSN: 0008-5472</identifier><identifier>EISSN: 1538-7445</identifier><identifier>PMID: 8813152</identifier><identifier>CODEN: CNREA8</identifier><language>eng</language><publisher>Philadelphia, PA: American Association for Cancer Research</publisher><subject>Antigens, Differentiation - genetics ; Antigens, Differentiation - metabolism ; Antigens, Neoplasm ; Biological and medical sciences ; Biomarkers, Tumor ; Blotting, Northern ; Breast Neoplasms - pathology ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell Adhesion - physiology ; Cell Aggregation ; Dissemination ; DNA, Complementary - genetics ; Female ; Galectin 3 ; Gene Expression Regulation, Neoplastic ; Glycoproteins - genetics ; Glycoproteins - metabolism ; Humans ; Medical sciences ; Melanoma - pathology ; Neoplastic Cells, Circulating ; Protein Binding ; Tumor cell ; Tumors</subject><ispartof>Cancer research (Chicago, Ill.), 1996-10, Vol.56 (19), p.4530-4534</ispartof><rights>1996 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3227634$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8813152$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>INOHARA, H</creatorcontrib><creatorcontrib>AKAHANI, S</creatorcontrib><creatorcontrib>KOTHS, K</creatorcontrib><creatorcontrib>RAZ, A</creatorcontrib><title>Interactions between galectin-3 and mac-2-binding protein mediate cell-cell adhesion</title><title>Cancer research (Chicago, Ill.)</title><addtitle>Cancer Res</addtitle><description>Galectin-3 is a beta-galactoside-specific lectin implicated in diverse processes involved in cellular interactions. Recently, the Mac-2-binding protein, a heavily N-glycosylated secreted protein with a subunit Mr of 97,000, was identified as its ligand. The present study characterizes the interaction between galectin-3 and Mac-2-binding protein in whole cells and measures their relative expression levels. Incubation of A375 cells with affinity-purified Mac-2-binding protein resulted in its binding to galectin-3 on the cell surface in a specific carbohydrate-dependent manner. Mac-2-binding protein also induced homotypic cell aggregation, which was inhibited by lactose or Fab' fragments of an anti-galectin-3 antibody. Northern blotting analysis revealed differences in the transcriptional regulation of galectin-3 and Mac-2-binding protein. These results provide the first direct evidence for a Mac-2-binding protein function and suggest that it may play a role in tumor cell embolization during metastasis through interaction with galectin-3.</description><subject>Antigens, Differentiation - genetics</subject><subject>Antigens, Differentiation - metabolism</subject><subject>Antigens, Neoplasm</subject><subject>Biological and medical sciences</subject><subject>Biomarkers, Tumor</subject><subject>Blotting, Northern</subject><subject>Breast Neoplasms - pathology</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Adhesion - physiology</subject><subject>Cell Aggregation</subject><subject>Dissemination</subject><subject>DNA, Complementary - genetics</subject><subject>Female</subject><subject>Galectin 3</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>Glycoproteins - genetics</subject><subject>Glycoproteins - metabolism</subject><subject>Humans</subject><subject>Medical sciences</subject><subject>Melanoma - pathology</subject><subject>Neoplastic Cells, Circulating</subject><subject>Protein Binding</subject><subject>Tumor cell</subject><subject>Tumors</subject><issn>0008-5472</issn><issn>1538-7445</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kEtrwzAQhEVpSdO0P6GgQ-lNYL0s-VhCH4FAL-nZrKx1omIrqSVT-u_rUNPLLjszDB97QZZcS8uMUvqSLIuisEwrI67JTUqf06l5oRdkYS2XXIsl2W1ixgGaHI4xUYf5GzHSPXQ4SZFJCtHTHhommAvRh7inp-GYMUTaow-QkTbYdew8KPgDpqnolly10CW8m_eKfLw879ZvbPv-ulk_bdlBlFVmXGBVqVK3pkXw2noH3kmjOUjuTQuiBKucM4ClqdrSNaZU3EgnhDbeVk6uyONf74T0NWLKdR_SmQQiHsdUGyuVFlZMwfs5OLoJuz4NoYfhp57fMPkPsw-pga4dIDYh_cekEKaUSv4ChARmyQ</recordid><startdate>19961001</startdate><enddate>19961001</enddate><creator>INOHARA, H</creator><creator>AKAHANI, S</creator><creator>KOTHS, K</creator><creator>RAZ, A</creator><general>American Association for Cancer Research</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19961001</creationdate><title>Interactions between galectin-3 and mac-2-binding protein mediate cell-cell adhesion</title><author>INOHARA, H ; AKAHANI, S ; KOTHS, K ; RAZ, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h269t-12e99465f7fead58dbadb3751a31d7fa26a84bb7ae679f6bc764173b2257d89b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Antigens, Differentiation - genetics</topic><topic>Antigens, Differentiation - metabolism</topic><topic>Antigens, Neoplasm</topic><topic>Biological and medical sciences</topic><topic>Biomarkers, Tumor</topic><topic>Blotting, Northern</topic><topic>Breast Neoplasms - pathology</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Adhesion - physiology</topic><topic>Cell Aggregation</topic><topic>Dissemination</topic><topic>DNA, Complementary - genetics</topic><topic>Female</topic><topic>Galectin 3</topic><topic>Gene Expression Regulation, Neoplastic</topic><topic>Glycoproteins - genetics</topic><topic>Glycoproteins - metabolism</topic><topic>Humans</topic><topic>Medical sciences</topic><topic>Melanoma - pathology</topic><topic>Neoplastic Cells, Circulating</topic><topic>Protein Binding</topic><topic>Tumor cell</topic><topic>Tumors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>INOHARA, H</creatorcontrib><creatorcontrib>AKAHANI, S</creatorcontrib><creatorcontrib>KOTHS, K</creatorcontrib><creatorcontrib>RAZ, A</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Cancer research (Chicago, Ill.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>INOHARA, H</au><au>AKAHANI, S</au><au>KOTHS, K</au><au>RAZ, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interactions between galectin-3 and mac-2-binding protein mediate cell-cell adhesion</atitle><jtitle>Cancer research (Chicago, Ill.)</jtitle><addtitle>Cancer Res</addtitle><date>1996-10-01</date><risdate>1996</risdate><volume>56</volume><issue>19</issue><spage>4530</spage><epage>4534</epage><pages>4530-4534</pages><issn>0008-5472</issn><eissn>1538-7445</eissn><coden>CNREA8</coden><abstract>Galectin-3 is a beta-galactoside-specific lectin implicated in diverse processes involved in cellular interactions. Recently, the Mac-2-binding protein, a heavily N-glycosylated secreted protein with a subunit Mr of 97,000, was identified as its ligand. The present study characterizes the interaction between galectin-3 and Mac-2-binding protein in whole cells and measures their relative expression levels. Incubation of A375 cells with affinity-purified Mac-2-binding protein resulted in its binding to galectin-3 on the cell surface in a specific carbohydrate-dependent manner. Mac-2-binding protein also induced homotypic cell aggregation, which was inhibited by lactose or Fab' fragments of an anti-galectin-3 antibody. Northern blotting analysis revealed differences in the transcriptional regulation of galectin-3 and Mac-2-binding protein. These results provide the first direct evidence for a Mac-2-binding protein function and suggest that it may play a role in tumor cell embolization during metastasis through interaction with galectin-3.</abstract><cop>Philadelphia, PA</cop><pub>American Association for Cancer Research</pub><pmid>8813152</pmid><tpages>5</tpages></addata></record> |
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| ispartof | Cancer research (Chicago, Ill.), 1996-10, Vol.56 (19), p.4530-4534 |
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| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; American Association for Cancer Research |
| subjects | Antigens, Differentiation - genetics Antigens, Differentiation - metabolism Antigens, Neoplasm Biological and medical sciences Biomarkers, Tumor Blotting, Northern Breast Neoplasms - pathology Carrier Proteins - genetics Carrier Proteins - metabolism Cell Adhesion - physiology Cell Aggregation Dissemination DNA, Complementary - genetics Female Galectin 3 Gene Expression Regulation, Neoplastic Glycoproteins - genetics Glycoproteins - metabolism Humans Medical sciences Melanoma - pathology Neoplastic Cells, Circulating Protein Binding Tumor cell Tumors |
| title | Interactions between galectin-3 and mac-2-binding protein mediate cell-cell adhesion |
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