Human FSH isoforms: carbohydrate complexity as determinant of in-vitro bioactivity

Differences in sialic acid content of the hormone have been considered the main determinant of FSH polymorphism. The aim of the present study was to investigate the effect of variations in the oligosaccharide structure of the intrapituitary human FSH (hFSH) glycosylation variants on their intrinsic...

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Bibliographic Details
Published in:Molecular and cellular endocrinology 2001-03, Vol.174 (1), p.41-49
Main Authors: Creus, Silvina, Chaia, Zulema, Pellizzari, Eliana H, Cigorraga, Selva B, Ulloa-Aguirre, Alfredo, Campo, Stella
Format: Article
Language:English
Subjects:
Animals
Carbohydrate complexity
Carbohydrate Sequence
Chromatography, Affinity
Concanavalin A
Follicle Stimulating Hormone - chemistry
Follicle Stimulating Hormone - genetics
Follicle Stimulating Hormone - pharmacology
Follicle-stimulating hormone (human pituitary)
FSH bioactivity
FSH isoforms
Genetic Variation
Humans
Lectins
N-Acetylneuraminic Acid
Oligosaccharides - chemistry
Pituitary Gland - chemistry
Plant Lectins
Polymorphism, Genetic
Protein Binding - drug effects
Protein Isoforms - chemistry
Protein Isoforms - genetics
Protein Isoforms - pharmacology
Rats
Wheat Germ Agglutinins
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Summary:Differences in sialic acid content of the hormone have been considered the main determinant of FSH polymorphism. The aim of the present study was to investigate the effect of variations in the oligosaccharide structure of the intrapituitary human FSH (hFSH) glycosylation variants on their intrinsic biological activity. FSH charge isoforms obtained after chromatofocusing were further separated by lectin affinity chromatography [Concanavalin A (ConA), Wheat germ agglutinin (WGA), Lentil lectin (LcH)]. Isolated isoforms were separately tested for in-vitro bioactivity in a rat Sertoli cell aromatization bioassay. Our results show that: (1) FSH microheterogeneity is due not only to variations in the sialic acid content of the hormone but also to differences in the internal structure of the carbohydrate chains, and (2) variations in the sialic acid content as well as differences in the complexity of the glycans determine the full biological expression of FSH glycosylation variants.
ISSN:0303-7207
1872-8057
DOI:10.1016/S0303-7207(00)00453-6