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Human erythropoietin receptor: cloning, expression, and biologic
characterization
SS Jones, AD D'Andrea, LL Haines and GG Wong
Genetics Institute, Cambridge, MA 02140.
We have isolated the human homologue of the murine erythropoietin receptor
(mEPO-R) from an erythroleukemia line, OCIM1, and from fetal liver. Both
the cDNA and protein sequence of the human receptor were 82% homologous to
the mEPO-R. Heterologous expression of the human cDNA in COS cells yielded
a protein of about 66 Kd. The protein could be specifically
immunoprecipitated with either an antibody raised against the amino
terminus of mEPO-R or by a monoclonal antibody that bound EPO bound to its
receptor. Cross-linking of radioiodinated EPO to COS cells expressing the
human EPO-R gave apparent molecular weights of 66 and 100 Kd for the
receptor. The murine interleukin-3-dependent pre-B- lymphocyte cell line,
Ba/F3, was made EPO-dependent by transfection of the human cDNA into the
cells and selecting for growth in EPO- containing media.
Volume 76,
Issue 1,
pp. 31-35,
07/01/1990
Copyright © 1990 by The American Society of Hematology
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