| pubmed-article:7733948 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7733948 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:7733948 | lifeskim:mentions | umls-concept:C0022984 | lld:lifeskim |
| pubmed-article:7733948 | lifeskim:mentions | umls-concept:C1513095 | lld:lifeskim |
| pubmed-article:7733948 | lifeskim:mentions | umls-concept:C0007577 | lld:lifeskim |
| pubmed-article:7733948 | lifeskim:mentions | umls-concept:C0252527 | lld:lifeskim |
| pubmed-article:7733948 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:7733948 | pubmed:dateCreated | 1995-5-30 | lld:pubmed |
| pubmed-article:7733948 | pubmed:abstractText | Galectins constitute a gene family of beta-galactoside-specific lectins that show high homology in their carbohydrate-binding site. They have been postulated to be involved in many biological events, but their specific functions are not yet well defined. Galectin-1 is a laminin binding protein that recognizes poly-N-acetyllactosamine chains on this major basement membrane glycoprotein. In this study, we analyzed the possibility that galectin-1 could modulate interactions between human melanoma cells and laminin. We demonstrated that A375 and A2058 cell lines express galectin-1 both intracellularly and on the cell surface. In an in vitro assay, recombinant galectin-1 increased melanoma cell attachment to laminin in a dose-dependent manner. This effect was abolished by lactose. Anti-galectin-1 inhibited adhesion of melanoma cells to laminin in a dose-dependent fashion. However, neither galectin-1 nor anti-galectin-1 antibody affected melanoma cell spreading on laminin in vitro. These data indicate that galectin-1 might participate in melanoma cell adhesion to laminin and therefore could be a modulator of invasion and metastasis. | lld:pubmed |
| pubmed-article:7733948 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733948 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7733948 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733948 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7733948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7733948 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7733948 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:7733948 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:7733948 | pubmed:author | pubmed-author:SobelM EME | lld:pubmed |
| pubmed-article:7733948 | pubmed:author | pubmed-author:CooperD NDN | lld:pubmed |
| pubmed-article:7733948 | pubmed:author | pubmed-author:CastronovoVV | lld:pubmed |
| pubmed-article:7733948 | pubmed:author | pubmed-author:van den... | lld:pubmed |
| pubmed-article:7733948 | pubmed:author | pubmed-author:MarschalPP | lld:pubmed |
| pubmed-article:7733948 | pubmed:author | pubmed-author:BaldetMM | lld:pubmed |
| pubmed-article:7733948 | pubmed:author | pubmed-author:BuicuCC | lld:pubmed |
| pubmed-article:7733948 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7733948 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:7733948 | pubmed:volume | 209 | lld:pubmed |
| pubmed-article:7733948 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7733948 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7733948 | pubmed:pagination | 760-7 | lld:pubmed |
| pubmed-article:7733948 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:7733948 | pubmed:meshHeading | pubmed-meshheading:7733948-... | lld:pubmed |
| pubmed-article:7733948 | pubmed:meshHeading | pubmed-meshheading:7733948-... | lld:pubmed |
| pubmed-article:7733948 | pubmed:meshHeading | pubmed-meshheading:7733948-... | lld:pubmed |
| pubmed-article:7733948 | pubmed:meshHeading | pubmed-meshheading:7733948-... | lld:pubmed |
| pubmed-article:7733948 | pubmed:meshHeading | pubmed-meshheading:7733948-... | lld:pubmed |
| pubmed-article:7733948 | pubmed:meshHeading | pubmed-meshheading:7733948-... | lld:pubmed |
| pubmed-article:7733948 | pubmed:meshHeading | pubmed-meshheading:7733948-... | lld:pubmed |
| pubmed-article:7733948 | pubmed:meshHeading | pubmed-meshheading:7733948-... | lld:pubmed |
| pubmed-article:7733948 | pubmed:meshHeading | pubmed-meshheading:7733948-... | lld:pubmed |
| pubmed-article:7733948 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7733948 | pubmed:articleTitle | Galectin-1 modulates human melanoma cell adhesion to laminin. | lld:pubmed |
| pubmed-article:7733948 | pubmed:affiliation | Metastasis Research Laboratory, University of Liège, Belgium. | lld:pubmed |
| pubmed-article:7733948 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7733948 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:7733948 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7733948 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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