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A low-affinity human granulocyte-macrophage colony-stimulating
factor/murine erythropoietin hybrid receptor functions in murine cell lines
PT Jubinsky, DG Nathan, DJ Wilson and CA Sieff
Division of Pediatric Hematology and Oncology, Children's Hospital, Boston,
MA.
To identify domains in hematopoietic growth factor receptors that are
important for signal transduction, a hybrid receptor (GMER) was constructed
by splicing the DNA of the entire extracellular and transmembrane domains
of the human granulocyte-macrophage colony- stimulating factor (GM-CSF)
receptor alpha 2 subunit (GMR) to the cytoplasmic domain of the murine
erythropoietin receptor (mEpoR). The hybrid receptor was introduced into
the interleukin-3 factor-dependent murine hematopoietic cell line Ba/F3.
Cells that expressed high receptor numbers were selected by cell sorting
using phycoerythrin- labeled human GM-CSF. Immunoprecipitation of GMER from
Ba/F3 cells showed a band with an Mr of 105,000 daltons. Human GM-CSF
binding to Ba/F3 cells that expressed GMER showed a kd of 3.0 nmol/L and
475 binding sites/cell, while the same cells that expressed GMR had 300
sites/cell and a kd of 3.5 nmol/L. The proliferative response to GM-CSF of
Ba/F3 cells that expressed GMER showed 1/2 maximal cell growth (as measured
by 3H-thymidine incorporation) at a GM-CSF concentration of 2.5 x 10(-8)
mol/L. When cultured in human GM-CSF, Ba/F3-GMER cells expressed cell
surface glycophorin. Similar results were obtained with Ba/F3 cells
transfected with the mEpoR and cultured in erythropoietin. Expression of
GMR plus the human GM-CSF receptor beta chain in the same cell line also
resulted in human GM-CSF stimulated proliferation; however, cell surface
glycophorin was not detected. These data show that a low-affinity
GM-CSF/Epo hybrid receptor can promote GM-CSF- dependent proliferation and
can induce the expression of glycophorin, an erythroid-specific protein.
Volume 81,
Issue 3,
pp. 587-591,
02/01/1993
Copyright © 1993 by The American Society of Hematology
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