Bioactivity of recombinant hFSH glycosylation variants in primary cultures of porcine granulosa cells

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Issue Date
2020-06-15
Authors
Liang, Aixin
Plewes, Michele R.
Hua, Guohua
Hou, Xiaoying
Blum, Haley R.
Przygrodzka, Emilia
George, Jitu W.
Clark, Kendra L.
Bousfield, George R.
Butnev, Viktor Y.
Advisor
Citation

Liang, Aixin; Plewes, Michele R.; Hua, Guohua; Hou, Xiaoying; Blum, Haley R.; Przygrodzka, Emilia; George, Jitu W.; Clark, Kendra L.; Bousfield, George R.; Butnev, Viktor Y.; May, Jeffrey V.; Davis, John S. 2020. Bioactivity of recombinant hFSH glycosylation variants in primary cultures of porcine granulosa cells. Molecular and Cellular Endocrinology, 2020:pp 110911

Abstract

Previous studies have reported hypo-glycosylated FSH and fully-glycosylated FSH to be naturally occurring in humans, and these glycoforms exist in changing ratios over a woman's lifespan. The precise cellular and molecular effects of recombinant human FSH (hFSH) glycoforms, FSH21 and FSH24, have not been documented in primary granulosa cells. Herein, biological responses to FSH21 and FSH24 were compared in primary porcine granulosa cells. Hypo-glycosylated hFSH21 was significantly more effective than fully-glycosylated hFSH24 at stimulating cAMP accumulation and protein kinase A (PKA) activity, leading to the higher phosphorylation of CREB and β-Catenin. Compared to fully-glycosylated hFSH24, hypo-glycosylated hFSH21 also induced greater levels of transcripts for HSD3B, STAR and INHA, and higher progesterone production. Our results demonstrate that hypo-glycosylated hFSH21 exerts more robust activation of intracellular signals associated with steroidogenesis than fully-glycosylated hFSH24 in primary porcine granulosa cells, and furthers our understanding of the differing bioactivities of FSH glycoforms in the ovary.

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