| pubmed-article:11888899 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C0022984 | lld:lifeskim |
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| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C1510470 | lld:lifeskim |
| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C0442805 | lld:lifeskim |
| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C0486805 | lld:lifeskim |
| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C0030685 | lld:lifeskim |
| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C1521828 | lld:lifeskim |
| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C0680255 | lld:lifeskim |
| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C0391871 | lld:lifeskim |
| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C1283071 | lld:lifeskim |
| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C1963578 | lld:lifeskim |
| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:11888899 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:11888899 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:11888899 | pubmed:dateCreated | 2002-3-12 | lld:pubmed |
| pubmed-article:11888899 | pubmed:abstractText | The 67-kDa laminin receptor (67LR) is a high-affinity laminin-binding protein that is overexpressed on the tumor cell surface in a variety of cancers. We report here that the 67LR molecule also functions in the proteolytic cleavage of laminin-1, a relevant event in basement membrane degradation and tumor dissemination. In the presence of a synthetic peptide (peptide G) corresponding to the 67LR laminin binding site, the rate of laminin-1 degradation by the cysteine proteinase cathepsin B was significantly increased, and a new proteolytic fragment particularly active in in vitro cell migration assays was generated. The YIGSR peptide, corresponding to the 67LR binding site on laminin-1, blocked the peptide G-dependent proteolytic degradation. Our results shed light on the mechanism by which an adhesion receptor such as the 67LR plays a major role in tumor aggressiveness and metastasis. | lld:pubmed |
| pubmed-article:11888899 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11888899 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11888899 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11888899 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11888899 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11888899 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11888899 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11888899 | pubmed:issn | 0008-5472 | lld:pubmed |
| pubmed-article:11888899 | pubmed:author | pubmed-author:PollegioniLor... | lld:pubmed |
| pubmed-article:11888899 | pubmed:author | pubmed-author:MénardSylvieS | lld:pubmed |
| pubmed-article:11888899 | pubmed:author | pubmed-author:TagliabueElda... | lld:pubmed |
| pubmed-article:11888899 | pubmed:author | pubmed-author:ArdiniElenaE | lld:pubmed |
| pubmed-article:11888899 | pubmed:author | pubmed-author:SporchiaBarba... | lld:pubmed |
| pubmed-article:11888899 | pubmed:author | pubmed-author:ModugnoMichel... | lld:pubmed |
| pubmed-article:11888899 | pubmed:author | pubmed-author:GhirelliCrist... | lld:pubmed |
| pubmed-article:11888899 | pubmed:author | pubmed-author:CastiglioniFa... | lld:pubmed |
| pubmed-article:11888899 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11888899 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11888899 | pubmed:volume | 62 | lld:pubmed |
| pubmed-article:11888899 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11888899 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11888899 | pubmed:pagination | 1321-5 | lld:pubmed |
| pubmed-article:11888899 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:11888899 | pubmed:meshHeading | pubmed-meshheading:11888899... | lld:pubmed |
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| pubmed-article:11888899 | pubmed:meshHeading | pubmed-meshheading:11888899... | lld:pubmed |
| pubmed-article:11888899 | pubmed:meshHeading | pubmed-meshheading:11888899... | lld:pubmed |
| pubmed-article:11888899 | pubmed:meshHeading | pubmed-meshheading:11888899... | lld:pubmed |
| pubmed-article:11888899 | pubmed:meshHeading | pubmed-meshheading:11888899... | lld:pubmed |
| pubmed-article:11888899 | pubmed:meshHeading | pubmed-meshheading:11888899... | lld:pubmed |
| pubmed-article:11888899 | pubmed:meshHeading | pubmed-meshheading:11888899... | lld:pubmed |
| pubmed-article:11888899 | pubmed:meshHeading | pubmed-meshheading:11888899... | lld:pubmed |
| pubmed-article:11888899 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11888899 | pubmed:articleTitle | Identification of a novel function for 67-kDa laminin receptor: increase in laminin degradation rate and release of motility fragments. | lld:pubmed |
| pubmed-article:11888899 | pubmed:affiliation | Molecular Targeting Unit, Department of Experimental Oncology, Istituto Nazionale Tumori, 20133 Milan, Italy. | lld:pubmed |
| pubmed-article:11888899 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11888899 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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