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Steel factor and c-kit regulate cell-matrix adhesion
T Kinashi and TA Springer
Center For Blood Research, Boston, MA 02115.
Steel (SI) and white spotting (W) loci encode steel factor (c-kit ligand)
and the c-kit tyrosine kinase receptor, respectively. Mutations at these
loci affect migration and differentiation of primordial germ cells, neural
crest-derived melanoblasts, and hematopoietic cells. In these processes,
cell adhesion molecules are hypothesized to be crucial. We have examined
the role of steel factor and c-kit in cell- extracellular matrix adhesion
using bone marrow-derived mast cells as a model system. Steel factor
stimulates mast cells to bind to fibronectin and, to a lesser extent, to
vitronectin, whereas interleukin-3 and interleukin-4, which are also mast
cell growth factors, do not. Activation of adhesiveness is transient,
occurs at concentrations of steel factor 100-fold lower than required for
growth stimulation, and requires the integrin VLA-5. Mast cells from c-kit
mutant mice adhere to fibronectin on stimulation with phorbol 12-myristate
13-acetate (PMA), but not on stimulation with steel factor, indicating that
stimulation of integrin adhesiveness requires activation of the c-kit
protein tyrosine kinase. By contrast, c-kit mutant and wild-type mast cells
adhere equally well to COS cells expressing membrane-anchored steel factor,
showing that the kinase activity of c-kit is not required for adhesion
directly mediated by c-kit. Our findings suggest that regulation of
adhesion is an important biologic function of steel factor.
Volume 83,
Issue 4,
pp. 1033-1038,
02/15/1994
Copyright © 1994 by The American Society of Hematology
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