Role of glycosylation in function of follicle-stimulating hormone

The oligosaccharide structures of heterodimeric glycoprotein hormones, such as follicle-stimulating hormone (FSH), have been shown to play an important role in the biosynthesis, secretion, metabolic fate, and regulation of potency of the hormone. The oligosaccharide structures attached to each subunit of the protein seem to exhibit distinct roles in some of these functions. Glycans attached to the α-subunit are critical for dimer assembly, integrity, and secretion, as well as for signal transduction; although β-subunit glycans are also important for dimer assembly and secretion, they play a crucial role in clearance of the dimer from the circulation. Alternative glycosylation of FSH and other glycoprotein hormones not only may affect the metabolic clearance and net in vivo biopotency of the hormone, but also offers the interesting possibility that some glycosylation variants of the hormone may provoke differential or even unique effects at the target cell level. Glycosylation of FSH is regulated by hypothalamic and/or end products from the glands under the control of this hormone. In particular, estrogens regulate terminal sialylation and thus some functional properties of the gonadotropin influenced by sialic acid. Through these extrapituitary inputs, the gonadotroph may regulate not only the amount but also the intensity of the gonadotropin signal to be secreted by the pituitary in a given physiological condition.