Control of cell motility and tumour invasion by extracellular matrix interactions View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1992-08

AUTHORS

E Ruoslahti

ABSTRACT

Integrins are heterodimeric transmembrane proteins with large ectodomains and a short cytoplasmic tail inside the cell. They mediate cell adhesion to extracellular matrix proteins and to the surfaces of other cells. In many cases the sequence recognised by the integrins in the extracellular matrix proteins is the tripeptide Arg-Gly-Asp (RGD). Short synthetic peptides containing this sequence can inhibit invasion in vitro and tumour dissemination in vivo. Thus, the alpha 5 beta 1 fibronectin binding integrin appears to be the key integrin in the invasion of at least melanoma, osteosarcoma and glioblastoma cells. Modulation of the level and activities of this integrin can suppress invasion, whereas the alpha v beta 3 vitronectin binding integrin appears to be associated with increased invasiveness. There is increasing evidence that some of these effects are mediated through signals elicited by the binding of integrins to their target proteins. This possibility has generated a great deal of interest in the cytoplasmic molecules that might mediate the integrin-associated signalling. More... »

PAGES

239-242

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/bjc.1992.250

DOI

http://dx.doi.org/10.1038/bjc.1992.250

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1041198140

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1503896


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