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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1995-4-10
|
| pubmed:abstractText |
Ladsin is a large cell-adhesive protein with potent cell-scattering activity, which was recently identified in the culture of a malignant human gastric carcinoma cell line [Miyazaki, K. et al. (1993) Proc. Natl. Acad. Sci. USA 90, 11767-11771]. It is a heterotrimeric protein, containing a 140-kDa subunit similar or identical to the laminin B2t chain. Ladsin is similar to the keratinocyte-derived matrix proteins, "epiligrin" and "kalinin." In the present study, the cell-adhesion and cell-migration activities of ladsin were examined in comparison with those of three cell adhesion proteins, laminin, fibronectin, and vitronectin. Ladsin showed high cell-adhesion activity toward rat liver cell line BRL at concentrations 4-20-times lower than in the case of the other three proteins. In a monolayer culture, ladsin stimulated the migration of BRL cells about 2-times more strongly than the others, as compared at the minimal concentrations required for the maximal cell-adhesion activity. In Boyden chambers, ladsin stimulated both the chemotactic and chemokinetic migration of BRL cells. When the effect of anti-integrin antibodies on the adhesion of human fibrosarcoma cell line HT1080 was examined, the adhesion to ladsin was effectively inhibited by both the anti-integrin alpha 3 and beta 1 antibodies, but not the anti-integrin alpha 6 antibody, indicating that the primary receptor of ladsin is integrin alpha 3 beta 1. These results demonstrate that ladsin is a unique extracellular matrix component which may play a major role in cell migration.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Chemotactic Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Matrix Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hepatocyte Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Laminin,
http://linkedlifedata.com/resource/pubmed/chemical/Vitronectin
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0021-924X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
116
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
862-9
|
| pubmed:dateRevised |
2007-12-19
|
| pubmed:meshHeading |
pubmed-meshheading:7533763-Adult,
pubmed-meshheading:7533763-Animals,
pubmed-meshheading:7533763-Cell Adhesion,
pubmed-meshheading:7533763-Cell Adhesion Molecules,
pubmed-meshheading:7533763-Cell Movement,
pubmed-meshheading:7533763-Cells, Cultured,
pubmed-meshheading:7533763-Chemotactic Factors,
pubmed-meshheading:7533763-Extracellular Matrix Proteins,
pubmed-meshheading:7533763-Female,
pubmed-meshheading:7533763-Fibronectins,
pubmed-meshheading:7533763-Glycoproteins,
pubmed-meshheading:7533763-Hepatocyte Growth Factor,
pubmed-meshheading:7533763-Humans,
pubmed-meshheading:7533763-Laminin,
pubmed-meshheading:7533763-Liver,
pubmed-meshheading:7533763-Rats,
pubmed-meshheading:7533763-Rats, Inbred BUF,
pubmed-meshheading:7533763-Stimulation, Chemical,
pubmed-meshheading:7533763-Tumor Cells, Cultured,
pubmed-meshheading:7533763-Vitronectin
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Marked stimulation of cell adhesion and motility by ladsin, a laminin-like scatter factor.
|
| pubmed:affiliation |
Division of Cell Biology, Kihara Institute for Biological Research, Yokohama City University.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|