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Front Endocrinol (Lausanne). 2018 May 09;9:216. doi: 10.3389/fendo.2018.00216. eCollection 2018.

[No title available]

Frontiers in endocrinology

George R Bousfield, Jeffrey V May, John S Davis, James A Dias, T Rajendra Kumar

Affiliations

  1. Department of Biological Sciences, Wichita State University, Wichita, KS, United States.
  2. Department of Obstetrics and Gynecology, University of Nebraska Medical Center, Omaha, NE, United States.
  3. Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE, United States.
  4. Nebraska-Western Iowa Health Care System, Omaha, NE, United States.
  5. Department of Biomedical Sciences, School of Public Health, University at Albany, Albany, NY, United States.
  6. Department of Obstetrics and Gynecology, University of Colorado Anschutz Medical Campus, Aurora, CO, United States.

PMID: 29867757 PMCID: PMC5960776 DOI: 10.3389/fendo.2018.00216

Abstract

Human follicle-stimulating hormone (FSH) exhibits both macro- and microheterogeneity in its carbohydrate moieties. Macroheterogeneity results in three physiologically relevant FSHβ subunit variants, two that possess a single N-linked glycan at either one of the two βL1 loop glycosylation sites or one with both glycans. Microheterogeneity is characterized by 80 to over 100 unique oligosaccharide structures attached to each of the 3 to 4 occupied N-glycosylation sites. With respect to its receptor, partially glycosylated (hypo-glycosylated) FSH variants exhibit higher association rates, greater apparent affinity, and greater occupancy than fully glycosylated FSH. Higher receptor binding-activity is reflected by greater

Keywords: N-glycosylation; bone; female Infertility; follicle-stimulating hormone; pituitary

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