All-or-none N-glycosylation in primate follicle-stimulating hormone β-subunits

Bousfield, George R.; Butnev, Vladimir Y.; Walton, Wendy J.; Nguyen, Van Toan; Huneidi, Jennifer; Singh, Vinod; Kolli, V. S. Kumar; Harvey, David J.; Rance, Naomi E.

doi:10.1016/j.mce.2006.02.017

Cited by 65 publications

(83 citation statements)

References 30 publications

(52 reference statements)

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“…Recent studies have shown that pituitary hFSH consists of two classes of molecules: those that possess a non-glycosylated b-subunit and those that possess di-glycosylated b-subunits (Walton et al 2001, Bousfield et al 2007). These differences impact on the b-subunit and FSH molecular weight.…”

Section: Discussionmentioning

confidence: 99%

Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells

Loreti¹,

Ambao²,

Andreone³

et al. 2013

Reproduction

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Granulosa cell (GC) inhibin A and B production is regulated by FSH and gonadal factors. This gonadotrophin is released as a mixture of glycoforms, which induce different biological responses in vivo and in vitro. Our aim was to determine the effect of recombinant human FSH (rhFSH) glycosylation variants on inhibin A and B production by rat GCs. Preparative isoelectro focusing was used to isolate more acidic/sialylated (pH !4.00) and less acidic/sialylated (pH O5.00) rhFSH charge analogues. Concanavalin A was used to isolate unbound and firmly bound rhFSH glycoforms on the basis of their oligosaccharide complexity. GCs, obtained from oestrogen-primed immature rats, were cultured with either native rhFSH or its glycosylation variants. Inhibin A and B were determined using specific ELISAs. Results were expressed as meanGS.E.M. Under basal conditions, inhibin A was the predominant dimer produced (inhibin A: 673G55; inhibin B: 80G4 pg/ml). More acidic/sialylated charge analogues stimulated inhibin B production when compared to inhibin A at all doses studied; by contrast, less acidic/sialylated charge analogues stimulated inhibin A production and elicited no effect on inhibin B. Glycoforms bearing complex oligosaccharides showed a potent stimulatory effect on inhibin B when compared to inhibin A production (i.e. dose 1 ng/ml: 4.9G0.5 vs 0.9G0.1-fold stimulation, P!0.001). Glycoforms bearing hybrid-type oligosaccharides favoured inhibin A production (i.e. dose 4 ng/ml 2.9G0.1 vs 1.6G0.1-fold stimulation, P!0.05). These results show that the sialylation degree as well as the complexity of oligosaccharides present in the rhFSH molecule may be considered additional factors that differentially regulate dimeric inhibin production by rat GCs.

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Section: Discussionmentioning

confidence: 99%

Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells

Loreti¹,

Ambao²,

Andreone³

et al. 2013

Reproduction

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“…Broad MALDI peaks (m/z 23.4 kDa) with masses higher than that calculated from the amino acid sequence, recorded in linear mode, have indicated glycosylation in the fusion protein shFas from HeLa cells (Li et al, 2007h). Smaller glycoproteins with multiple glycosylation sites also give broad unresolved peaks as shown by a recent study of human pituitary follicle-stimulating hormone (hFSH; Bousfield et al, 2007). However small glycoproteins with only one occupied site can often give several peaks corresponding to specific glycoforms.…”

Section: General Comments On the Analysis Of Intact Glycoproteinsmentioning

confidence: 99%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Harvey

2011

Mass Spectrometry Reviews

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This review is the fifth update of the original review, published in 1999, on the application of MALDI mass spectrometry to the analysis of carbohydrates and glycoconjugates and brings coverage of the literature to the end of 2008. The first section of the review covers fundamental studies, fragmentation of carbohydrate ions, use of derivatives and new software developments for analysis of carbohydrate spectra. Among newer areas of method development are glycan arrays, MALDI imaging and the use of ion mobility spectrometry. The second section of the review discusses applications of MALDI MS to the analysis of different types of carbohydrate. Specific compound classes that are covered include carbohydrate polymers from plants, N- and O-linked glycans from glycoproteins, biopharmaceuticals, glycated proteins, glycolipids, glycosides and various other natural products. There is a short section on the use of MALDI mass spectrometry for the study of enzymes involved in glycan processing and a section on the use of MALDI MS to monitor products of the chemical synthesis of carbohydrates with emphasis on carbohydrate-protein complexes and glycodendrimers. Corresponding analyses by electrospray ionization now appear to outnumber those performed by MALDI and the amount of literature makes a comprehensive review on this technique impractical. However, most of the work relating to sample preparation and glycan synthesis is equally relevant to electrospray and, consequently, those proposing analyses by electrospray should also find material in this review of interest.

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“…Although the structural and functional specificity of each hormone resides in the b-subunit, there is evidence suggesting that both subunits contact the receptor [13]. The gonadotropin is decorated with N-linked oligosaccharides attached to aAsn52 and aAsn78, and bAsn7 and bAsn24 [1,3,5,12,14,15]. Oligosaccharides in glycoprotein hormones play important roles including folding, secretion, and maintenance of heterodimer stability; they also determine the metabolic clearance rate of the hormone and influence on the activation of its cognate receptor [10].…”

Section: Follicle-stimulating Hormone and Follicle-stimulating Hormonmentioning

confidence: 99%

“…One striking example has been recently reported. Glycosylation of the primate FSH bsubunit exhibits a particular glycoform which possesses only a-subunit oligosaccharides and that is more active in vitro than the tetraglycosylated variant [15,19].…”

Section: Follicle-stimulating Hormone and Follicle-stimulating Hormonmentioning

confidence: 99%

Multiple facets of follicle-stimulating hormone receptor function

Ulloa‐Aguirre

Zariñán

Pasapera

et al. 2007

Endocr

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Follicle-stimulating hormone (FSH) is a glycoprotein hormone produced by the anterior pituitary gland. This gonadotropin plays an essential role in reproduction. Its receptor (FSHR) belongs to the superfamily of G protein-coupled receptors (GPCR), specifically the family of rhodopsin-like receptors. Agonist binding to the FSHR triggers the rapid activation of multiple signaling cascades, mainly the cAMP-adenylyl cyclase-protein kinase A cascade, that impact diverse biological effects of FSH in the gonads. As in other G protein-coupled receptors, the several cytoplasmic domains of the FSHR are involved in signal transduction and termination of the FSH signal. Here we summarize some recent information on the signaling cascades activated by FSH as well as on the role of the intracytoplasmic domains of the FSHR in coupling to membrane and cytosolic proteins linked to key biological functions regulated by the FSH-FSHR system.

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All-or-none N-glycosylation in primate follicle-stimulating hormone β-subunits

Cited by 65 publications

References 30 publications

Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells

Effect of sialylation and complexity of FSH oligosaccharides on inhibin production by granulosa cells

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Multiple facets of follicle-stimulating hormone receptor function

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