| pubmed-article:1842179 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1842179 | lifeskim:mentions | umls-concept:C0699790 | lld:lifeskim |
| pubmed-article:1842179 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1842179 | lifeskim:mentions | umls-concept:C0245382 | lld:lifeskim |
| pubmed-article:1842179 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:1842179 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:1842179 | pubmed:dateCreated | 1992-12-3 | lld:pubmed |
| pubmed-article:1842179 | pubmed:abstractText | The interaction of tumor cells with laminin is thought to be critical in invasion and metastasis. We found that an endogenous lectin, carbohydrate-binding protein 35 (CBP-35), is the major laminin-binding protein on human colon carcinoma cells and that its surface expression suggests involvement in metastasis. We identified CBP-35 by laminin-affinity chromatography and immunoblotting. Surface expression of CBP-35 on eight human colon carcinoma cell lines was compared by flow cytometry. Poorly differentiated cell lines and DLD-2, a signet-ring carcinoma cell line, expressed more surface CBP-35 than well-differentiated cell lines. Poorly differentiated cell lines and DLD-2 are characterized as aggressive cell lines because they adhere to and invade through reconstituted basement membrane significantly better than well-differentiated cell lines. These data suggest that CBP-35 is involved in tumor cell-basement membrane interactions and that an increase in CBP-35 surface expression may facilitate metastatic potential of colon carcinoma cells. | lld:pubmed |
| pubmed-article:1842179 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1842179 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1842179 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1842179 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:1842179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1842179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1842179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1842179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1842179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1842179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1842179 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1842179 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:1842179 | pubmed:issn | 0004-0010 | lld:pubmed |
| pubmed-article:1842179 | pubmed:author | pubmed-author:LeeE CEC | lld:pubmed |
| pubmed-article:1842179 | pubmed:author | pubmed-author:SteeleG DGDJr | lld:pubmed |
| pubmed-article:1842179 | pubmed:author | pubmed-author:SonD SDS | lld:pubmed |
| pubmed-article:1842179 | pubmed:author | pubmed-author:MercurioA MAM | lld:pubmed |
| pubmed-article:1842179 | pubmed:author | pubmed-author:KorzeliusC... | lld:pubmed |
| pubmed-article:1842179 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1842179 | pubmed:volume | 126 | lld:pubmed |
| pubmed-article:1842179 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1842179 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1842179 | pubmed:pagination | 1498-502 | lld:pubmed |
| pubmed-article:1842179 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1842179 | pubmed:meshHeading | pubmed-meshheading:1842179-... | lld:pubmed |
| pubmed-article:1842179 | pubmed:meshHeading | pubmed-meshheading:1842179-... | lld:pubmed |
| pubmed-article:1842179 | pubmed:meshHeading | pubmed-meshheading:1842179-... | lld:pubmed |
| pubmed-article:1842179 | pubmed:meshHeading | pubmed-meshheading:1842179-... | lld:pubmed |
| pubmed-article:1842179 | pubmed:meshHeading | pubmed-meshheading:1842179-... | lld:pubmed |
| pubmed-article:1842179 | pubmed:meshHeading | pubmed-meshheading:1842179-... | lld:pubmed |
| pubmed-article:1842179 | pubmed:meshHeading | pubmed-meshheading:1842179-... | lld:pubmed |
| pubmed-article:1842179 | pubmed:meshHeading | pubmed-meshheading:1842179-... | lld:pubmed |
| pubmed-article:1842179 | pubmed:meshHeading | pubmed-meshheading:1842179-... | lld:pubmed |
| pubmed-article:1842179 | pubmed:meshHeading | pubmed-meshheading:1842179-... | lld:pubmed |
| pubmed-article:1842179 | pubmed:meshHeading | pubmed-meshheading:1842179-... | lld:pubmed |
| pubmed-article:1842179 | pubmed:meshHeading | pubmed-meshheading:1842179-... | lld:pubmed |
| pubmed-article:1842179 | pubmed:meshHeading | pubmed-meshheading:1842179-... | lld:pubmed |
| pubmed-article:1842179 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1842179 | pubmed:articleTitle | Carbohydrate-binding protein 35 is the major cell-surface laminin-binding protein in colon carcinoma. | lld:pubmed |
| pubmed-article:1842179 | pubmed:affiliation | Laboratory of Cancer Biology, Deaconess Hospital, Harvard Medical School, Boston, Mass 02115. | lld:pubmed |
| pubmed-article:1842179 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1842179 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1842179 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1842179 | lld:pubmed |
