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N ‐Glycosylation‐defective receptor for erythropoietin can transduce the ligand‐induced cell proliferation signal
Author(s) -
Nagao Masaya,
Morishita Emi,
Hanai Yasumitsu,
Kobayashi Kazuhira,
Sasaki Ryuzo
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01046-h
Subject(s) - erythropoietin , microbiology and biotechnology , glycosylation , erythropoietin receptor , chemistry , receptor , signal transduction , ligand (biochemistry) , cell growth , biochemistry , biology , genetics
Erythropoietin receptor (EPOR) contains a single N‐linked sugar in an extracellular domain. It has been suggested that an erythroleukemia cell line with high sensitivity to EPO expresses a high molecular mass form of EPOR, which appears to be a highly N ‐glycosylated form responsible for EPO‐mediated signal transduction [Sawyer and Hankins (1993) Proc. Natl. Acad. Sci. USA 90, 6849–6853]. To examine the role of the N‐linked sugar chain, we prepared EPO‐dependent cell lines expressing the wild‐type EPOR and N ‐glycosylation‐defective EPOR. There was little difference in the expression of EPOR on the cell surface, EPO binding kinetics, and EPO‐induced cell proliferation between the clones expressing the mutant EPOR and those expressing the wild‐type EPOR.