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dc.contributor.authorBousfield, George R.
dc.contributor.authorButnev, Vladimir Y.
dc.contributor.authorButnev, Viktor Y.
dc.contributor.authorHiromasa, Yasuaki
dc.contributor.authorHarvey, David J.
dc.contributor.authorMay, Jeffrey V.
dc.date.accessioned2014-04-15T16:48:11Z
dc.date.available2014-04-15T16:48:11Z
dc.date.issued2014-02-15
dc.identifier.citationBousfield, George R.; Butnev, Vladimir Y.; Butnev, Viktor Y.; Hiromasa, Yasuaki; Harvey, David J.; May, Jeffrey V. 2014. Hypo-glycosylated human follicle-stimulating hormone (hFSH(21/18)) is much more active in vitro than fully-glycosylated hFSH (hFSH(24)). Molecular and Cellular Endocrinology, vol. 382:no. 2, 15 February 2014: ppg. 989–997en_US
dc.identifier.issn0303-7207
dc.identifier.otherWOS:000331915500021
dc.identifier.urihttp://dx.doi.org/10.1016/j.mce.2013.11.008
dc.identifier.urihttp://hdl.handle.net/10057/10561
dc.descriptionThis is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike License, which permits noncommercial use, distribution, and reproduction in any medium, provided the original author and source are credited.en_US
dc.description.abstractHypo-glycosylated hFSH21/18 (possesses FSHβ21 and FSHβ18bands) was isolated from hLH preparations by immunoaffinity chromatography followed by gel filtration. Fully-glycosylated hFSH24 was prepared by combining the fully-glycosylated FSHβ24 variant with hCGα and isolating the heterodimer. The hFSH21/18 glycoform preparation was significantly smaller than the hFSH24 preparation and possessed 60% oligomannose glycans, which is unusual for hFSH. Hypo-glycosylated hFSH21/18 was 9- to 26-fold more active than fully-glycosylated hFSH24 in FSH radioligand assays. Significantly greater binding of 125I-hFSH21/18 tracer than hFSH24 tracer was observed in all competitive binding assays. In addition, higher binding of hFSH21/18 was noted in association and saturation binding assays, in which twice as much hFSH21/18 was bound as hFSH24. This suggests that more ligand binding sites are available to hFSH21/18 in FSHR than to hFSH24. Hypo-glycosylated hFSH21/18 also bound rat FSHRs more rapidly, exhibiting almost no lag in binding, whereas hFSH24 specific binding proceeded very slowly for almost the first hour of incubation.en_US
dc.description.sponsorshipNIH Grants P01 AG-029531, G20 RR-031092, P20 RR-016475, and matching funds from Wichita State University.en_US
dc.language.isoen_USen_US
dc.publisherElsevier Ireland Ltden_US
dc.relation.ispartofseriesMolecular and Cellular Endocrinology;v.382:no.2
dc.subjectFSH isoformsen_US
dc.subjectOligosaccharideen_US
dc.subjectFSHRen_US
dc.titleHypo-glycosylated human follicle-stimulating hormone (hFSH(21/18)) is much more active in vitro than fully-glycosylated hFSH (hFSH(24))en_US
dc.typeArticleen_US
dc.rights.holderCopyright © 2013, The Authors.


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