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

Author:

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.ORCID

Funder

National Institutes of Health

Olson Center for Women's Health

Senior Research Career Scientist Award

Merit Review Award

Publisher

Elsevier BV

Subject

Endocrinology,Molecular Biology,Biochemistry

Reference46 articles.

1. Role of FSH glycan structure in the regulation of Sertoli cell inhibin production;Andreone;Reproduction,2017

2. Specific roles for the asparagine-linked carbohydrate residues of recombinant human follicle stimulating hormone in receptor binding and signal transduction;Bishop;Mol. Endocrinol.,1994

3. Macro- and micro-heterogeneity in pituitary and urinary follicle stimulating hormone glycosylation;Bousfield;J. Glycom. Lipidom.,2014

4. Hypo-glycosylated human follicle-stimulating hormone (hFSH(21/18)) is much more active in vitro than fully-glycosylated hFSH (hFSH(24));Bousfield;Mol. Cell. Endocrinol.,2014

5. In vivo and in vitro impact of carbohydrate variation on human follicle-stimulating hormone function;Bousfield;Front. Endocrinol.,2018

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