N-Glycosylation-defective receptor for erythropoietin can transduce the ligand-induced cell proliferation signal

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Abstract
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.