| pubmed-article:8552198 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8552198 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8552198 | lifeskim:mentions | umls-concept:C0022984 | lld:lifeskim |
| pubmed-article:8552198 | lifeskim:mentions | umls-concept:C0001511 | lld:lifeskim |
| pubmed-article:8552198 | lifeskim:mentions | umls-concept:C1513095 | lld:lifeskim |
| pubmed-article:8552198 | lifeskim:mentions | umls-concept:C0245382 | lld:lifeskim |
| pubmed-article:8552198 | lifeskim:mentions | umls-concept:C0242210 | lld:lifeskim |
| pubmed-article:8552198 | lifeskim:mentions | umls-concept:C1523874 | lld:lifeskim |
| pubmed-article:8552198 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8552198 | pubmed:dateCreated | 1996-2-21 | lld:pubmed |
| pubmed-article:8552198 | pubmed:abstractText | Galectin-3 is a laminin binding protein which expression is altered in a variety of human carcinomas including colon, breast and endometrium. In these tumors, we consistently observed a down regulation of galectin-3 expression related to increased aggressiveness. Galectin-3 belongs to a family of galactose-binding lectins and binds laminin through its numerous poly-N-acetyllactosamine chains. To date, the exact role of galectin-3 in the complex interactions between cancer cells and laminin has not been clearly defined. Adhesion of melanoma cells to laminin is a critical event during tumor invasion and metastasis. In this study, we explore the possibility that galectin-3 could modulate attachment of two human melanoma cell lines to laminin. A2058 and A375 melanoma cell expressed galectin-3 on their surface as demonstrated by immunofluorescence, and attached to laminin in an in vitro assay. We demonstrate that neither recombinant galectin-3 nor an affinity purified antigalectin-3 antiserum altered adhesion of A2058 or A375 melanoma cells to laminin. Our data strongly suggest that galectin-3 is not a key element in adhesion of the melanoma cells to laminin. These results are not surprising in light of the observation that galectin-3 expression is down regulated in cancer and that increased adhesion to laminin is a constant feature of invasive cancer cells. | lld:pubmed |
| pubmed-article:8552198 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8552198 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8552198 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8552198 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8552198 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8552198 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8552198 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8552198 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8552198 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8552198 | pubmed:issn | 0028-2685 | lld:pubmed |
| pubmed-article:8552198 | pubmed:author | pubmed-author:SobelM EME | lld:pubmed |
| pubmed-article:8552198 | pubmed:author | pubmed-author:LinF MFM | lld:pubmed |
| pubmed-article:8552198 | pubmed:author | pubmed-author:CastronovoVV | lld:pubmed |
| pubmed-article:8552198 | pubmed:author | pubmed-author:van den... | lld:pubmed |
| pubmed-article:8552198 | pubmed:author | pubmed-author:BuicuCC | lld:pubmed |
| pubmed-article:8552198 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8552198 | pubmed:volume | 42 | lld:pubmed |
| pubmed-article:8552198 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8552198 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8552198 | pubmed:pagination | 215-9 | lld:pubmed |
| pubmed-article:8552198 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8552198 | pubmed:meshHeading | pubmed-meshheading:8552198-... | lld:pubmed |
| pubmed-article:8552198 | pubmed:meshHeading | pubmed-meshheading:8552198-... | lld:pubmed |
| pubmed-article:8552198 | pubmed:meshHeading | pubmed-meshheading:8552198-... | lld:pubmed |
| pubmed-article:8552198 | pubmed:meshHeading | pubmed-meshheading:8552198-... | lld:pubmed |
| pubmed-article:8552198 | pubmed:meshHeading | pubmed-meshheading:8552198-... | lld:pubmed |
| pubmed-article:8552198 | pubmed:meshHeading | pubmed-meshheading:8552198-... | lld:pubmed |
| pubmed-article:8552198 | pubmed:meshHeading | pubmed-meshheading:8552198-... | lld:pubmed |
| pubmed-article:8552198 | pubmed:meshHeading | pubmed-meshheading:8552198-... | lld:pubmed |
| pubmed-article:8552198 | pubmed:meshHeading | pubmed-meshheading:8552198-... | lld:pubmed |
| pubmed-article:8552198 | pubmed:meshHeading | pubmed-meshheading:8552198-... | lld:pubmed |
| pubmed-article:8552198 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8552198 | pubmed:articleTitle | Galectin-3, a laminin binding protein, fails to modulate adhesion of human melanoma cells to laminin. | lld:pubmed |
| pubmed-article:8552198 | pubmed:affiliation | Metastasis Research Laboratory, University of Liège, Belgium. | lld:pubmed |
| pubmed-article:8552198 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8552198 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8552198 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8552198 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8552198 | lld:pubmed |
