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Isolation and characterization of a monoclonal antibody that recognizes the
human c-kit receptor
VC Broudy, N Lin, KM Zsebo, NC Birkett, KA Smith, ID Bernstein and T Papayannopoulou
Department of Medicine, University of Washington, Seattle 98195.
Stem cell factor (SCF) stimulates the growth of burst-forming unit-
erythroid (BFU-E) and colony-forming unit granulocyte-macrophage (CFU- GM)
by binding to a specific cell surface receptor. The receptor for SCF is
encoded by the protooncogene c-kit. After immunizing mice with the human
erythroleukemia cell line OCIM1, we obtained a monoclonal antibody (MoAb)
that recognizes the human c-kit receptor. This MoAb, designated SR-1,
blocks binding of 125I-human SCF to the c-kit receptor, and neutralizes the
biologic effects of SCF in hematopoietic colony assays. With few
exceptions, c-kit expression was identified on all hematopoietic and
lymphoid cell lines tested by indirect immunofluorescent analysis using
SR-1 and by binding studies with 125I- SCF. SR-1 recognizes a small
fraction of normal bone marrow mononuclear cells, and these cells have the
morphologic appearance of blasts. Colony assays show that BFU-E and CFU-GM
display the c-kit receptor. SR- 1 does not cross-react with murine c-kit
protein, indicating that the binding epitopes of the human and murine c-kit
receptors are antigenically distinct. This MoAb may be useful to
characterize the spectrum of cells that display the c-kit receptor and to
further define the role of SCF in hematopoiesis.
Volume 79,
Issue 2,
pp. 338-346,
01/15/1992
Copyright © 1992 by The American Society of Hematology
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