Evidence map›Paper›PMID 25915568›Full record

ArticleThe Journal of clinical endocrinology and metabolism2015

Hypoglycosylated hFSH Has Greater Bioactivity Than Fully Glycosylated Recombinant hFSH in Human Granulosa Cells.

Chao Jiang, Xiaoying Hou, Cheng Wang, Jeffrey V May, Viktor Y Butnev, George R Bousfield, John S Davis

Open access · greenAbstract readComparative Study
In one paragraph

Article in The Journal of clinical endocrinology and metabolism, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
7.6field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

42 citing papers in PubMed, 72 citations in OpenAlex.

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  11. Human FSH Glycoform α-Subunit AsparagineFrontiers in endocrinology · 2022
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Chao JiangThe Olson Center for Women's Health, Department of Obstetrics and Gynecology (C.J., X.H., C.W., J.S.D.), University of Nebraska Medical Center, Omaha, Nebraska 68198; Nebraska-Northwest Iowa VA Medical Center (X.H., J.S.D.), Omaha, Nebraska 68105; Department of Biological Sciences (J.V.M., V.Y.B., G.R.B.), Wichita State University, Wichita, Kansas 67260; and Department of Biochemistry and Molecular Biology (J.S.D.), University of Nebraska Medical Center, Omaha, Nebraska 68198.
Xiaoying HouThe Olson Center for Women's Health, Department of Obstetrics and Gynecology (C.J., X.H., C.W., J.S.D.), University of Nebraska Medical Center, Omaha, Nebraska 68198; Nebraska-Northwest Iowa VA Medical Center (X.H., J.S.D.), Omaha, Nebraska 68105; Department of Biological Sciences (J.V.M., V.Y.B., G.R.B.), Wichita State University, Wichita, Kansas 67260; and Department of Biochemistry and Molecular Biology (J.S.D.), University of Nebraska Medical Center, Omaha, Nebraska 68198.
Cheng WangThe Olson Center for Women's Health, Department of Obstetrics and Gynecology (C.J., X.H., C.W., J.S.D.), University of Nebraska Medical Center, Omaha, Nebraska 68198; Nebraska-Northwest Iowa VA Medical Center (X.H., J.S.D.), Omaha, Nebraska 68105; Department of Biological Sciences (J.V.M., V.Y.B., G.R.B.), Wichita State University, Wichita, Kansas 67260; and Department of Biochemistry and Molecular Biology (J.S.D.), University of Nebraska Medical Center, Omaha, Nebraska 68198.
Jeffrey V MayThe Olson Center for Women's Health, Department of Obstetrics and Gynecology (C.J., X.H., C.W., J.S.D.), University of Nebraska Medical Center, Omaha, Nebraska 68198; Nebraska-Northwest Iowa VA Medical Center (X.H., J.S.D.), Omaha, Nebraska 68105; Department of Biological Sciences (J.V.M., V.Y.B., G.R.B.), Wichita State University, Wichita, Kansas 67260; and Department of Biochemistry and Molecular Biology (J.S.D.), University of Nebraska Medical Center, Omaha, Nebraska 68198.
Viktor Y ButnevThe Olson Center for Women's Health, Department of Obstetrics and Gynecology (C.J., X.H., C.W., J.S.D.), University of Nebraska Medical Center, Omaha, Nebraska 68198; Nebraska-Northwest Iowa VA Medical Center (X.H., J.S.D.), Omaha, Nebraska 68105; Department of Biological Sciences (J.V.M., V.Y.B., G.R.B.), Wichita State University, Wichita, Kansas 67260; and Department of Biochemistry and Molecular Biology (J.S.D.), University of Nebraska Medical Center, Omaha, Nebraska 68198.
George R BousfieldThe Olson Center for Women's Health, Department of Obstetrics and Gynecology (C.J., X.H., C.W., J.S.D.), University of Nebraska Medical Center, Omaha, Nebraska 68198; Nebraska-Northwest Iowa VA Medical Center (X.H., J.S.D.), Omaha, Nebraska 68105; Department of Biological Sciences (J.V.M., V.Y.B., G.R.B.), Wichita State University, Wichita, Kansas 67260; and Department of Biochemistry and Molecular Biology (J.S.D.), University of Nebraska Medical Center, Omaha, Nebraska 68198.
John S DavisThe Olson Center for Women's Health, Department of Obstetrics and Gynecology (C.J., X.H., C.W., J.S.D.), University of Nebraska Medical Center, Omaha, Nebraska 68198; Nebraska-Northwest Iowa VA Medical Center (X.H., J.S.D.), Omaha, Nebraska 68105; Department of Biological Sciences (J.V.M., V.Y.B., G.R.B.), Wichita State University, Wichita, Kansas 67260; and Department of Biochemistry and Molecular Biology (J.S.D.), University of Nebraska Medical Center, Omaha, Nebraska 68198.
Wichita State University · USOmaha VA Medical Center · USUniversity of Nebraska Medical Center · US

Funding

The Aging Pituitary/Gonadal AxisP01AG029531 · NIA · WICHITA STATE UNIVERSITY · PI JOHN S DAVIS · 2009 to 2026
$25.9M
GPR30 Mediated-Estrogen Action on Ovarian Physiology and Ovarian CancerK99HD059985 · NICHD · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI WANG, CHENG · 2010 to 2011
$180k
NIA NIH HHS NIH 1P01 AG029531NIA NIH HHS P01 AG029531NICHD NIH HHS K99 HD059985
6 · The paper itself

Abstract

contextPrevious studies suggest that aging in women is associated with a reduction in hypoglycosylated forms of FSH.

objectiveExperiments were performed to determine whether glycosylation of the FSHβ subunit modulates the biological activity of FSH in human granulosa cells. DESIGN AND

settingRecombinant human FSH (hFSH) derived from GH3 pituitary cells was purified into fractions containing hypoglycosylated hFSH(21/18) and fully glycosylated hFSH(24). The response to FSH glycoforms was evaluated using the well-characterized, FSH-responsive human granulosa cell line, KGN at an academic medical center.

interventionsGranulosa cells were treated with increasing concentrations of fully- or hypoglycosylated FSH glycoforms for periods up to 48 hours. MAIN OUTCOME MEASURE(S): The main outcomes were indices of cAMP-dependent cell signaling and estrogen and progesterone synthesis.

resultsWe observed that hypoglycosylated FSH(21/18) was significantly more effective than fully glycosylated FSH(24) at stimulating cAMP accumulation, protein kinase A (PKA) activity, and cAMP response element binding protein (CREB) (S133) phosphorylation. FSH(21/18) was also much more effective than hFSH(24) on the stimulation CREB-response element-mediated transcription, expression of aromatase and STAR proteins, and synthesis of estrogen and progesterone. Adenoviral-mediated expression of the endogenous inhibitor of PKA, inhibited FSH(21/18)- and FSH(24)-stimulated CREB phosphorylation, and steroidogenesis.

conclusionsHypoglycosylated FSH(21/18) has greater bioactivity than fully glycosylated hFSH(24), suggesting that age-dependent decreases in hypoglycosylated hFSH contribute to reduced ovarian responsiveness. Hypoglycosylated FSH may be useful in follicle stimulation protocols for older patients using assisted reproduction technologies.

Indexed as

Carbohydrate SequenceCells, CulturedCyclic AMPCyclic AMP-Dependent Protein KinasesCyclic AMP Response Element-Binding ProteinEnzyme ActivationFemaleFollicle Stimulating Hormone, HumanGlycosylationGranulosa CellsHumansPhosphorylationProtein IsoformsRecombinant ProteinsCyclic AMPCyclic AMP-Dependent Protein KinasesCyclic AMP Response Element-Binding ProteinFollicle Stimulating Hormone, HumanProtein IsoformsRecombinant Proteins

Identifiers

PMID25915568
PMCPMC4454802
OpenAlexW2004820795

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.