Human FSH Glycoform α-Subunit Asparagine⁵² Glycans: Major Glycan Structural Consistency, Minor Glycan Variation in Abundance.

ABSTRACT: Follicle-stimulating hormone (FSH), an α/β heterodimeric glycoprotein hormone, consists of functionally significant variants resulting from the presence or absence of either one of two FSHβ subunit N-glycans. The two most abundant variants are fully-glycosylated FSH24 (based on 24 kDa FSHβ band in Western blots) and hypo-glycosylated FSH21 (21 kDa band, lacks βAsn²⁴ glycans). Due to its ability to bind more rapidly to the FSH receptor and occupy more FSH binding sites than FSH24, hypo-glycosylated FSH21 exhibits greater biological activity. Endoglycosidase F1-deglycosylated FSH bound to the complete extracellular domain of the FSH receptor crystallized as a trimeric complex. It was noted that a single biantennary glycan attached to FSHα Asn⁵² might preemptively fill t

SUBMITTER: Butnev VY 

PROVIDER: S-EPMC9623679 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature