Human erythropoietin receptor: cloning, expression, and biologic characterization.
Human erythropoietin receptor: cloning, expression, and biologic characterization.
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DOI:
10.1182/blood.v76.1.31.bloodjournal76131
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发表时间:
1990-07
期刊:
影响因子:
20.3
通讯作者:
S. Jones;Alan D. D’Andrea;Lora L. Haines;Gordon G. Wong
中科院分区:
文献类型:
--
作者:
S. Jones;Alan D. D’Andrea;Lora L. Haines;Gordon G. Wong
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.