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Necessity of extracellular domain of W (c-kit) receptors for attachment of
murine cultured mast cells to fibroblasts
S Adachi, Y Ebi, S Nishikawa, S Hayashi, M Yamazaki, T Kasugai, T Yamamura, S Nomura and Y Kitamura
Department of Pathology, Osaka University Medical School, Suita, Japan.
The receptor encoded by the W (c-kit) locus (W receptor) is expressed on
the surface of cultured mast cells (CMC) derived from normal (+/+) mice,
whereas its ligand encoded by the Sl locus (Sl ligand) is expressed on the
surface of fibroblast cell lines derived from murine embryos. Involvement
of W receptors and Sl ligands in attachment of CMC to fibroblasts was
investigated. CMC were cocultured with fibroblasts; nonattaching CMC were
removed and the remaining CMC were counted. CMC derived from mice of the
W/W genotype did not express the extracellular domain of W receptors, and
attachment of W/W CMC to +/+ fibroblasts was significantly impaired.
Fibroblasts derived from embryos of the Sl/Sl genotype did not express Sl
ligands, and the attachment of +/+ CMC to Sl/Sl fibroblasts was also
impaired. The Wv and W42 alleles are point mutations at the intracellular
tyrosine kinase domain. Attachment of either Wv/Wv, W/Wv, or W/W42 CMC to
+/+ fibroblasts was comparable with that of +/+ CMC. Moreover, the addition
of monoclonal antibody against the extracellular domain of W receptors
inhibited the attachment of +/+ CMC to +/+ fibroblasts. Thus, the
extracellular domain of W receptors appeared to be necessary for attachment
of CMC to fibroblasts.
Volume 79,
Issue 3,
pp. 650-656,
02/01/1992
Copyright © 1992 by The American Society of Hematology
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