Linked Life Data

14871893

Source:http://linkedlifedata.com/resource/pubmed/id/14871893

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2004-4-19
pubmed:abstractText
Cell migration plays roles in invasion of transformed cells and scattering of embryonic mesenchymal cells into surrounding tissues. We have found that Ig-like Necl-5/Tage4 is up-regulated in NIH3T3 cells transformed by an oncogenic Ras (V12Ras-NIH3T3 cells) and heterophilically trans-interacts with a Ca(2+)-independent Ig-like cell adhesion molecule nectin-3, eventually enhancing their intercellular motility. We show here that Necl-5 furthermore enhances cell migration in a nectin-3-independent manner. Studies using L fibroblasts expressing various mutants of Necl-5, NIH3T3 cells, and V12Ras-NIH3T3 cells have revealed that Necl-5 enhances serum- and platelet-derived growth factor-induced cell migration. The extracellular region of Necl-5 is necessary for directional cell migration, but not for random cell motility. The cytoplasmic region of Necl-5 is necessary for both directional and random cell movement. Necl-5 colocalizes with integrin alpha(V)beta(3) at leading edges of migrating cells. Analyses using an inhibitor or an activator of integrin alpha(V)beta(3) or a dominant negative mutant of Necl-5 have shown the functional association of Necl-5 with integrin alpha(V)beta(3) in cell motility. Cdc42 and Rac small G proteins are activated by the action of Necl-5 and required for the serum-induced, Necl-5-enhanced cell motility. These results indicate that Necl-5 regulates serum- and platelet-derived growth factor-induced cell migration in an integrin-dependent, nectin-3-independent manner, when cells do not contact other cells. We furthermore show here that enhanced motility and metastasis of V12Ras-NIH3T3 cells are at least partly the result of up-regulated Necl-5.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18015-25
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:14871893-Animals, pubmed-meshheading:14871893-Antigens, Neoplasm, pubmed-meshheading:14871893-Calcium, pubmed-meshheading:14871893-Cell Adhesion, pubmed-meshheading:14871893-Cell Adhesion Molecules, pubmed-meshheading:14871893-Cell Division, pubmed-meshheading:14871893-Cell Line, Transformed, pubmed-meshheading:14871893-Cell Movement, pubmed-meshheading:14871893-Cell Transformation, Neoplastic, pubmed-meshheading:14871893-Cytoplasm, pubmed-meshheading:14871893-Enzyme Inhibitors, pubmed-meshheading:14871893-Fibroblasts, pubmed-meshheading:14871893-Fluorescence Resonance Energy Transfer, pubmed-meshheading:14871893-Integrin alphaVbeta3, pubmed-meshheading:14871893-Integrins, pubmed-meshheading:14871893-Mice, pubmed-meshheading:14871893-Mice, Nude, pubmed-meshheading:14871893-Microscopy, Fluorescence, pubmed-meshheading:14871893-NIH 3T3 Cells, pubmed-meshheading:14871893-Neoplasm Metastasis, pubmed-meshheading:14871893-Neoplasm Proteins, pubmed-meshheading:14871893-Platelet-Derived Growth Factor, pubmed-meshheading:14871893-Protein Binding, pubmed-meshheading:14871893-Transfection, pubmed-meshheading:14871893-Up-Regulation
pubmed:year
2004
pubmed:articleTitle
Nectin-like molecule-5/Tage4 enhances cell migration in an integrin-dependent, Nectin-3-independent manner.
pubmed:affiliation
Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita 565-0871, Osaka, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't