Evidence map›Paper›PMID 34071747›Full record

ArticlePharmaceutics2021

Identification and Relative Quantification of hFSH Glycoforms in Women's Sera via MS-PRM-Based Approach.

Chiara Melchiorre, Cerina Chhuon, Vincent Jung, Joanna Lipecka, Francesca Di Rella, Alessandro Conforti, Angela Amoresano, Andrea Carpentieri, Ida Chiara Guerrera

Abstract read
In one paragraph

Article in Pharmaceutics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Review
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

9 authors.

Chiara MelchiorreDepartment Chemical Sciences, University of Naples Federico II, Monte S. Angelo-Cinthia, 80126 Naples, Italy.
Cerina ChhuonProteomics Platform Necker, Université de Paris-Structure Fédérative de Recherche Necker, INSERM US24/CNRS UMS3633, 75015 Paris, France.
Vincent JungProteomics Platform Necker, Université de Paris-Structure Fédérative de Recherche Necker, INSERM US24/CNRS UMS3633, 75015 Paris, France.ORCID 0000-0003-0530-1737
Joanna LipeckaProteomics Platform Necker, Université de Paris-Structure Fédérative de Recherche Necker, INSERM US24/CNRS UMS3633, 75015 Paris, France.
Francesca Di RellaDepartment of Senology, Istituto Nazionale Tumori IRCCS "Fondazione G. Pascale", 80131 Naples, Italy.ORCID 0000-0003-3271-4828
Alessandro ConfortiDepartment of Neuroscience, Reproductive Science and Odontostomatology, University of Naples Federico II, 80138 Naples, Italy.
Angela AmoresanoDepartment Chemical Sciences, University of Naples Federico II, Monte S. Angelo-Cinthia, 80126 Naples, Italy.
Andrea CarpentieriDepartment Chemical Sciences, University of Naples Federico II, Monte S. Angelo-Cinthia, 80126 Naples, Italy.ORCID 0000-0002-1944-5355
Ida Chiara GuerreraProteomics Platform Necker, Université de Paris-Structure Fédérative de Recherche Necker, INSERM US24/CNRS UMS3633, 75015 Paris, France.ORCID 0000-0002-4832-6793

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Follicle-stimulating hormone (FSH) is a glycohormone synthesized by adenohypophysis, and it stimulates ovulation in women and spermatogenesis in men by binding to its receptor (FSHR). FSHR is involved in several mechanisms to transduce intracellular signals in response to the FSH stimulus. Exogenous FSH is currently used in the clinic for ovarian hyperstimulation during in vitro fertilization in women, and for treatment of infertility caused by gonadotropin deficiency in men. The glycosylation of FSH strongly affects the binding affinity to its receptor, hence significantly influencing the biological activity of the hormone. Therefore, the accurate measurement and characterization of serum hFSH glycoforms will contribute to elucidating the complex mechanism of action by which different glycoforms elicit distinct biological activity. Nowadays ELISA is the official method with which to monitor serum hFSH, but the test is unable to distinguish between the different FSH glycovariants and is therefore unsuitable to study the biological activity of this hormone. This study presents a preliminary alternative strategy for identifying and quantifying serum hFSH glycoforms based on immunopurification assay and mass spectrometry (MS), and parallel reaction monitoring (PRM) analysis. In this study, we provide an MS-PRM data acquisition method for hFSH glycopeptides identification with high specificity and their quantification by extracting the chromatographic traces of selected fragments of glycopeptides. Once set up for all its features, the proposed method could be transferred to the clinic to improve fertility treatments and follow-ups in men and women.

Indexed as

FSHglycosylationPRM–mass spectrometry

Identifiers

PMID34071747
PMCPMC8226871

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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.