Regulation of cell-matrix adhesion by receptor tyrosine kinases.
Cell-cell and cell-matrix adhesive interactions mediated by integrins play crucial roles in leukocyte migration to inflamed tissues, and also in cell migration during embryogenesis. Much remains to be learned about the molecular mechanisms of regulation of adhesion mediated by integrins. Recently we found that steel factor and c-kit induce adhesion to fibronectin by VLA-5 in mast cells. Activation of adhesiveness is transient, and occurs at concentrations of steel factor 100-fold lower than required for growth stimulation. This suggests that regulation of adhesion is an important biological function of steel factor and c-kit. Other receptor tyrosine kinases such as the PDGF receptor can substitute for c-kit. Signaling through receptor tyrosine kinases may offer a general mechanism for the regulation of integrin avidity.
Kinashi
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Department of Immunology, University of Tokyo, Japan.
Springer
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TA
D000818:Animals; D002448:Cell Adhesion / Q000502:physiology*; D002465:Cell Movement / Q000502:physiology*; D002874:Chromosome Mapping; D005109:Extracellular Matrix / Q000502:physiology*; D005353:Fibronectins / Q000502:physiology; D008407:Mast Cells / Q000166:cytology; D051379:Mice; D008817:Mice, Mutant Strains; D010641:Phenotype; D019009:Proto-Oncogene Proteins c-kit / Q000502:physiology; D020794:Receptor Protein-Tyrosine Kinases / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology; D019089:Stem Cell Factor / Q000502:physiology
D005353:Fibronectins; D019089:Stem Cell Factor; D019009:Proto-Oncogene Proteins c-kit; D020794:Receptor Protein-Tyrosine Kinases