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Hypo-glycosylated human follicle-stimulating hormone (hFSH(21/18)) is much more active in vitro than fully-glycosylated hFSH (hFSH(24)).
- Source :
-
Molecular and cellular endocrinology [Mol Cell Endocrinol] 2014 Feb 15; Vol. 382 (2), pp. 989-97. Date of Electronic Publication: 2013 Dec 01. - Publication Year :
- 2014
-
Abstract
- Hypo-glycosylated hFSH(21/18) (possesses FSHβ(21) and FSHβ(18)bands) was isolated from hLH preparations by immunoaffinity chromatography followed by gel filtration. Fully-glycosylated hFSH(24) was prepared by combining the fully-glycosylated FSHβ(24) variant with hCGα and isolating the heterodimer. The hFSH(21/18) glycoform preparation was significantly smaller than the hFSH(24) preparation and possessed 60% oligomannose glycans, which is unusual for hFSH. Hypo-glycosylated hFSH(21/18) was 9- to 26-fold more active than fully-glycosylated hFSH(24) in FSH radioligand assays. Significantly greater binding of (125)I-hFSH(21/18) tracer than hFSH(24) tracer was observed in all competitive binding assays. In addition, higher binding of hFSH(21/18) was noted in association and saturation binding assays, in which twice as much hFSH(21/18) was bound as hFSH(24). This suggests that more ligand binding sites are available to hFSH(21/18) in FSHR than to hFSH(24). Hypo-glycosylated hFSH(21/18) also bound rat FSHRs more rapidly, exhibiting almost no lag in binding, whereas hFSH(24) specific binding proceeded very slowly for almost the first hour of incubation.<br /> (Copyright © 2013 The Authors. Published by Elsevier Ireland Ltd.. All rights reserved.)
- Subjects :
- Animals
Binding Sites
Binding, Competitive
Chromatography, Affinity
Chromatography, Gel
Follicle Stimulating Hormone, Human isolation & purification
Follicle Stimulating Hormone, Human metabolism
Glycoprotein Hormones, alpha Subunit metabolism
Glycosylation
Humans
Iodine Radioisotopes
Luteinizing Hormone metabolism
Mannose metabolism
Protein Binding
Protein Multimerization
Radioligand Assay
Rats
Receptors, FSH metabolism
Sequence Analysis, Protein
Follicle Stimulating Hormone, Human chemistry
Glycoprotein Hormones, alpha Subunit chemistry
Luteinizing Hormone chemistry
Mannose chemistry
Receptors, FSH chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1872-8057
- Volume :
- 382
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Molecular and cellular endocrinology
- Publication Type :
- Academic Journal
- Accession number :
- 24291635
- Full Text :
- https://doi.org/10.1016/j.mce.2013.11.008