| Endocrine Journal | |
| Processing of O-linked Glycosylation in the Chimera Consisting of α-Subunit and Carboxyl-terminal Peptide of the Human Chorionic Gonadotropin β-Subunit is Affected by Dimer Formation with Follicle-stimulating Hormone β-Subunit | |
| Madoka FURUHASHI2  Nobuhiko SUGANUMA1  | |
| [1] Infertility Center, Toyohashi Municipal Hospital;Department of Obstetrics and Gynecology, Japanese Red Cross Nagoya First Hospital | |
| 关键词: hCGβ-subunit; α-subunit; Carboxyl-terminal peptide; O-Linked glycosylation; | |
| DOI : 10.1507/endocrj.51.53 | |
| 学科分类:内分泌与代谢学 | |
| 来源: Japan Endocrine Society | |
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【 摘 要 】
References(38)hCG, LH, FSH, and TSH are a family of heterodimeric glycoprotein hormones that contain a common α-subunit, but differ in their hormone-specific β-subunits. hCGβ is unique among β-subunits due to a carboxyl-terminal peptide (CTP) bearing four O-linked oligosaccharides. We previously reported that there were differences in O-glycosylation between two chimeras consisting of α-subunit and CTP, i.e. a variant with CTP at the N-terminal region (Cα) and another analog with CTP at the C-terminus (αC) of the α-subunit. To address whether O-glycosylation is influenced by the heterodimer formation, Cα and αC were expressed alone or with FSHβ-subunit in Chinese hamster ovary cells. The O-linked glycosylation was assessed by continuous labeling with [35S]methionine/cysteine, immunoprecipitation with anti-α or anti-FSH serum, serial digestion with endoglycosidase-F and neuraminidase, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The decrease in molecular weight of dimeric chimeras digested with endoglycosidase-F was greater in Cα than that in αC after treatment with neuraminidase, revealing that both chimeras have different numbers of sialic acids on O-linked carbohydrates. By treating with endoglycosidase-F, the dimeric αC migrated faster than its free form, whereas the mobility difference between assembled and unassembled forms of Cα was very little. These data indicate that processing of O-glycosylation is affected by the backbone polypeptide chain(s).
【 授权许可】
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| Files | Size | Format | View |
|---|---|---|---|
| RO201911300448035ZK.pdf | 198KB |
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