Role of FSH glycan structure in the regulation of Sertoli cell inhibin production?.

AMBAO V; CIGORRAGA SB; ANDREONE L; LORETI N; PELLIZZARI EH; CAMPO S

Modena

Congreso; Fourth International Conference on Gonadotropins and Receptors; 2017

FSH is synthesized and secreted as a family of glycosylation variants, which differ from each other in the oligosaccharide composition and in the ability to induce biological responses. During the last years, inhibin B (Inh B) has been considered a reliable marker of Sertoli cell function; its production is stimulated by FSH and factors produced in the seminiferous tubules. The aim of the present study was to investigate the role of FSH oligosaccharide structure on the regulation of monomeric (Pro-C) and dimeric inhibin (Inh B) production at two maturation stages of the Sertoli cell. The effect of native recombinant human FSH (rhFSH) and its glycosylation variants was evaluated in vitro on immature Sertoli cells, isolated from 8-day-old rats, and cells in the process of terminal maturation, isolated from 20-day-old rats. rhFSH charge analogues were isolated by preparative Isoelectric Focusing (IEF) and Concanavalin A (Con-A) was used to isolate rhFSH glycoforms on the basis of their oligosaccharide complexity. Native rhFSH stimulated Pro-αC in a dose-dependent manner but did not induce changes in basal Inh B production in immature Sertoli cells. The less acidic/sialylated rhFSH charge analogues preparation (BA) resulted a more potent stimulus than the more acidic/sialylated one (AC) for Pro-αC production (p