| pubmed-article:8835318 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8835318 | lifeskim:mentions | umls-concept:C0010453 | lld:lifeskim |
| pubmed-article:8835318 | lifeskim:mentions | umls-concept:C0007578 | lld:lifeskim |
| pubmed-article:8835318 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:8835318 | lifeskim:mentions | umls-concept:C1624612 | lld:lifeskim |
| pubmed-article:8835318 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8835318 | pubmed:dateCreated | 1996-12-5 | lld:pubmed |
| pubmed-article:8835318 | pubmed:abstractText | Ladsin is a laminin-like cell-adhesive scatter factor with potent cell motility-stimulating ability and was purified from serum-free conditioned medium of a malignant human gastric adenocarcinoma cell line STKM-1. To test its possible role in tumor angiogenesis, we investigated its effect on primary culture of endothelial cells (human umbilical vein endothelial cells) and endothelial cell line ECV304 in this study. Cell adhesion and motility effects of ladsin were observed in both types of endothelial cells. In cell-attachment assay, ladsin interacted with integrin alpha 3 beta 1 that was expressed on the endothelial cell surface. In Boyden chambers, ladsin stimulated both directed and random migration of ECV304 cells. Ladsin induced repair of artificial wounds generated in ECV304 cell monolayers by stimulating cell migration. Ladsin did not affect the growth rate of ECV304 cells at a low cell density but significantly increased the saturation cell density. These results suggest that ladsin may be involved in the adhesion and migration of endothelial cells under some physiological and pathological conditions. | lld:pubmed |
| pubmed-article:8835318 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8835318 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8835318 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8835318 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8835318 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8835318 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8835318 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8835318 | pubmed:issn | 1071-2690 | lld:pubmed |
| pubmed-article:8835318 | pubmed:author | pubmed-author:MizushimaHH | lld:pubmed |
| pubmed-article:8835318 | pubmed:author | pubmed-author:MiyazakiKK | lld:pubmed |
| pubmed-article:8835318 | pubmed:author | pubmed-author:UmedaMM | lld:pubmed |
| pubmed-article:8835318 | pubmed:author | pubmed-author:KikkawaYY | lld:pubmed |
| pubmed-article:8835318 | pubmed:author | pubmed-author:YamanakaNN | lld:pubmed |
| pubmed-article:8835318 | pubmed:author | pubmed-author:AkaogiKK | lld:pubmed |
| pubmed-article:8835318 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8835318 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:8835318 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8835318 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8835318 | pubmed:pagination | 46-52 | lld:pubmed |
| pubmed-article:8835318 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8835318 | pubmed:meshHeading | pubmed-meshheading:8835318-... | lld:pubmed |
| pubmed-article:8835318 | pubmed:meshHeading | pubmed-meshheading:8835318-... | lld:pubmed |
| pubmed-article:8835318 | pubmed:meshHeading | pubmed-meshheading:8835318-... | lld:pubmed |
| pubmed-article:8835318 | pubmed:meshHeading | pubmed-meshheading:8835318-... | lld:pubmed |
| pubmed-article:8835318 | pubmed:meshHeading | pubmed-meshheading:8835318-... | lld:pubmed |
| pubmed-article:8835318 | pubmed:meshHeading | pubmed-meshheading:8835318-... | lld:pubmed |
| pubmed-article:8835318 | pubmed:meshHeading | pubmed-meshheading:8835318-... | lld:pubmed |
| pubmed-article:8835318 | pubmed:meshHeading | pubmed-meshheading:8835318-... | lld:pubmed |
| pubmed-article:8835318 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8835318 | pubmed:articleTitle | Stimulation of endothelial cell migration in culture by ladsin, a laminin-5-like cell adhesion protein. | lld:pubmed |
| pubmed-article:8835318 | pubmed:affiliation | Division of Cell Biology, Yokohama City University, Japan. | lld:pubmed |
| pubmed-article:8835318 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8835318 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8835318 | lld:pubmed |
