ArticleMolecular and cellular endocrinology2015
Production, purification, and characterization of recombinant hFSH glycoforms for functional studies.
Article in Molecular and cellular endocrinology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 49 citations in OpenAlex.
- Hypo-glycosylated FSH enhances the ovarian microenvironment for follicular development compared to fully glycosylated FSH.Cell communication and signaling : CCS · 2025Article
- Article
- Oocyte quality is enhanced by hypoglycosylated FSH through increased cell-to-cell interaction during mouse follicle development.Development (Cambridge, England) · 2023Article
- Differential effects of follicle-stimulating hormone glycoforms on the transcriptome profile of cultured rat granulosa cells as disclosed by RNA-seq.bioRxiv : the preprint server for biology · 2023Article
- Human FSH Glycoform α-Subunit AsparagineFrontiers in endocrinology · 2022Article
- Identification of N-glycans with GalNAc-containing antennae from recombinant HIV trimers by ion mobility and negative ion fragmentation.Analytical and bioanalytical chemistry · 2021Article
- Hypo-glycosylated hFSH drives ovarian follicular development more efficiently than fully-glycosylated hFSH: enhanced transcription and PI3K and MAPK signaling.Human reproduction (Oxford, England) · 2021Article
- Identification and Relative Quantification of hFSH Glycoforms in Women's Sera via MS-PRM-Based Approach.Pharmaceutics · 2021Article
- A Novel Follitropin Analog Inhibits Follitropin Activity In Vitro.Pharmaceutics · 2021Article
- Rate of rebound in follicle growth after cessation of ovarian stimulation in initial non-responders: a prospective cohort study.Journal of ovarian research · 2021Article
- Interplay Between mTOR and Hippo Signaling in the Ovary: Clinical Choice Guidance Between Different Gonadotropin Preparations for Better IVF.Frontiers in endocrinology · 2021Review
- Differential FSH Glycosylation Modulates FSHR Oligomerization and Subsequent cAMP Signaling.Frontiers in endocrinology · 2021Article
- Optimising Follicular Development, Pituitary Suppression, Triggering and Luteal Phase Support During Assisted Reproductive Technology: A Delphi Consensus.Frontiers in endocrinology · 2021Article
- In vitro ovarian follicle growth: a comprehensive analysis of key protocol variables†.Biology of reproduction · 2020Review
- Bioactivity of recombinant hFSH glycosylation variants in primary cultures of porcine granulosa cells.Molecular and cellular endocrinology · 2020Article
- Human Recombinant FSH and Its Biosimilars: Clinical Efficacy, Safety, and Cost-Effectiveness in Controlled Ovarian Stimulation for In Vitro Fertilization.Pharmaceuticals (Basel, Switzerland) · 2020Review
- In Vitro Impact of FSH Glycosylation Variants on FSH Receptor-stimulated Signal Transduction and Functional Selectivity.Journal of the Endocrine Society · 2020Article
- FSH for the Treatment of Male Infertility.International journal of molecular sciences · 2020Review
- Recombinant FSH glycoforms are bioactive in mouse preantral ovarian follicles.Reproduction (Cambridge, England) · 2019Article
- Follicle-Stimulating Hormone Glycobiology.Endocrinology · 2019Review
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Previously, our laboratory demonstrated the existence of a β-subunit glycosylation-deficient human FSH glycoform, hFSH(21). A third variant, hFSH(18), has recently been detected in FSH glycoforms isolated from purified pituitary hLH preparations. Human FSH(21) abundance in individual female pituitaries progressively decreased with increasing age. Hypo-glycosylated glycoform preparations are significantly more active than fully-glycosylated hFSH preparations. The purpose of this study was to produce, purify and chemically characterize both glycoform variants expressed by a mammalian cell line. Recombinant hFSH was expressed in a stable GH3 cell line and isolated from serum-free cell culture medium by sequential, hydrophobic and immunoaffinity chromatography. FSH glycoform fractions were separated by Superdex 75 gel-filtration. Western blot analysis revealed the presence of both hFSH(18) and hFSH(21) glycoforms in the low molecular weight fraction, however, their electrophoretic mobilities differed from those associated with the corresponding pituitary hFSH variants. Edman degradation of FSH(21/18)-derived β-subunit before and after peptide-N-glycanase F digestion confirmed that it possessed a mixture of both mono-glycosylated FSHβ subunits, as both Asn(7) and Asn(24) were partially glycosylated. FSH receptor-binding assays confirmed our previous observations that hFSH(21/18) exhibits greater receptor-binding affinity and occupies more FSH binding sites when compared to fully-glycosylated hFSH(24). Thus, the age-related reduction in hypo-glycosylated hFSH significantly reduces circulating levels of FSH biological activity that may further compromise reproductive function. Taken together, the ability to express and isolate recombinant hFSH glycoforms opens the way to study functional differences between them both in vivo and in vitro.
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