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• W2030336125 abstract "We have previously demonstrated that granulocyte-macrophage colony-stimulating factor (GM-CSF) receptors are composed of at least two molecules of 80 and 135 kDa, which were denoted α- and β-chains, respectively [Chiba, S., Shibuya, K., Piao, Y.-F., Tojo, A., Sasaki, N., Matsuki, S., Miyagawa, K., Miyazono, K. & Takaku, F. (1990) Cell Regul. 1, 327–335]. In this paper, we describe an investigation of the biochemical disparity noted between the α- and β-chains of GM-CSF receptors using proteolytic and deglycosidic enzymes, and further demonstrate the potential importance of carbohydrate structures of the GM-CSF receptors using different lectins and glycoprotein synthesis inhibitors. Cross-linked α- and β-chains with 125I-GM-CSF were digested by Staphylococcus aureus V8 protease and gave a different pattern. Furthermore, the size of the α-chain was reduced by 25 kDa by the removal of the N-linked oligosaccharides with peptidase: N-glycosidase F treatment, whereas that of the β-chain remained unmodified by the enzyme. These results suggest that the α-chain of GM-CSF receptors agrees with the recently cloned low-affinity GM-CSF receptor [Gearing, D. P., King, J. A., Gough, N. M. & Nicola, N. A. (1989) EMBO J. 8, 3667–3676] having approximately 30% N-linked oligosaccharides and is biochemically different from the αβ-chain. By analyses using lectins, some of the oligosaccharides in the α-chain seem to be the complex-type and/or hybrid-type, because wheat germ agglutinin and leukoagglutinating phytohemagglutinin inhibited both GM-CSF-induced proliferation and GM-CSF binding to its receptors. Further analyses using glycoprotein synthesis inhibitors showed that N-linked processing of the α-chain, especially glucose removal by glucosidase I and II (whose activities are inhibited by deoxynojirimycin), appeared to be required for the expression onto the cell surface although the β-chain expression was little affected by their inhibitors. Thus the β-chain, probably located near the α-chain on the cell surface, was associated with a high-affinity class of GM-CSF receptors." @default.
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• W2030336125 date "1991-06-01" @default.
• W2030336125 modified "2023-10-02" @default.
• W2030336125 title "Structural and functional analyses of glycosylation on the distinct molecules of human GM-CSF receptors" @default.
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• W2030336125 doi "https://doi.org/10.1111/j.1432-1033.1991.tb16064.x" @default.
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