Biological activity and metabolic clearance of recombinant human follicle stimulating hormone produced in Sp2/0 myeloma cells

Chin, C. K., Schofield, P. R., Robertson, D. M., Gray, P. P., Chotigeat, W. and Mahler, S. M. (1996) Biological activity and metabolic clearance of recombinant human follicle stimulating hormone produced in Sp2/0 myeloma cells. Cytotechnology, 21 2: 171-182. doi:10.1007/BF02215667


Author Chin, C. K.
Schofield, P. R.
Robertson, D. M.
Gray, P. P.
Chotigeat, W.
Mahler, S. M.
Title Biological activity and metabolic clearance of recombinant human follicle stimulating hormone produced in Sp2/0 myeloma cells
Journal name Cytotechnology   Check publisher's open access policy
ISSN 0920-9069
Publication date 1996-01-01
Year available 1996
Sub-type Article (original research)
DOI 10.1007/BF02215667
Open Access Status
Volume 21
Issue 2
Start page 171
End page 182
Total pages 12
Place of publication DORDRECHT
Publisher KLUWER ACADEMIC PUBL
Language eng
Subject 03 Chemical Sciences
09 Engineering
Abstract Human follicle stimulating hormone is a pituitary glycoprotein that is essential for the maintenance of ovarian follicle development and testicular spermatogenesis. Like other members of the glycoprotein hormone family, it contains a common a subunit and a hormone specific beta subunit. Each subunit contains two glycosylation sites. The specific structures of the oligosaccharides of human follicle stimulating hormone have been shown to influence both the in vitro and in vivo bioactivity. Since the carbohydrate structure of a protein reflects the glycosylation apparatus of the host cells in which the protein is expressed, we examined the isoform profiles, in vitro bioactivity and metabolic clearance of a preparation of purified recombinant human follicle stimulating hormone derived from a stable, transfected Sp2/0 myeloma cell line, and pituitary human follicle stimulating hormone. Isoelectric focussing and chromatofocussing studies of human follicle stimulating hormone preparations both showed a more basic isoform profile for the recombinant human follicle stimulating hormone compared to that of pituitary human follicle stimulating hormone. The recombinant human follicle stimulating hormone had a significantly higher radioreceptor activity compared to that of pituitary human follicle stimulating hormone, consistent with a greater in vitro potency. Pharmacokinetic studies in rats indicated a similar terminal half life (124 min) to that of the pituitary human follicle stimulating hormone (119 min). Preliminary carbohydrate analysis showed recombinant human follicle stimulating hormone to contain high mannose and/or hybrid type, in addition to complex type carbohydrate chains, terminating with both alpha 2,3 and alpha 2,6 linked sialic acids. These results demonstrate that recombinant human follicle stimulating hormone made in the Sp2/0 myeloma cells is sialylated, has a more basic isoform profile, and has a greater in vitro biological potency compared to those of the pituitary human follicle stimulating hormone.
Keyword Biotechnology & Applied Microbiology
Cell Biology
Hfsh
Sp2/0 Myeloma
Isoform Profile
In Vitro Bioactivity
Hamster Ovary Cells
Plasminogen-activator
Immunological Properties
Glycoprotein Hormones
Hepatic-clearance
Invitro Bioassay
Human Pituitary
Beta-subunit
Follitropin
Isoforms
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Australian Institute for Bioengineering and Nanotechnology Publications
 
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Created: Tue, 14 Aug 2007, 02:36:53 EST