N-glycosylation-defective receptor for erythropoietin can transduce the ligand-induced cell proliferation signal.
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.
Nagao
M
M
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Japan.
Morishita
E
E
Hanai
Y
Y
Kobayashi
K
K
Sasaki
R
R
D000818:Animals; D015153:Blotting, Western; D002455:Cell Division; D002460:Cell Line; D002999:Clone Cells / Q000378:metabolism; D004921:Erythropoietin / Q000378:metabolism* / Q000494:pharmacology; D015870:Gene Expression; D006031:Glycosylation; D051379:Mice; D008970:Molecular Weight; D017354:Point Mutation; D011485:Protein Binding; D017467:Receptors, Erythropoietin / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction
D017467:Receptors, Erythropoietin; D004921:Erythropoietin