The cloning of the human follicle stimulating hormone receptor and its expression in COS-7, CHO, and Y-1 cells

Kelton, Christie; Cheng, Shirley V.; Nugent, Noreen P.; Schweickhardt, Rene; Rosenthal, Judy L.; Overton, Susan A.; Wands, Gregory D.; Kuzeja, Jennifer B.; Luchette, Carol A.; Chappel, Scott C.

doi:10.1016/0303-7207(92)90220-z

Cited by 132 publications

(61 citation statements)

References 29 publications

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“…LH and FSH bioactivities of recombinant hormones were estimated by the in vitro stimulation of progesterone production respectively in mouse Leydig tumoral cells MLTC-1 (ATCCCRL 2065) and in a mouse adrenal cortex tumor stably expressing the human FSH receptor, referred to as Y1 cells (kindly given by Ares Serono, Geneva, Switzerland) (Kelton et al 1992). For the in vitro LH bioassay, about 1·5 10 5 MLTC-1 cells per well were incubated at 37 C in 0·5 ml supplemented RPMI growth medium (10% FBS, 50 µg/ml gentamicin, 10 units/ml penicillin and 10 µg/ml streptomycin) in 48-well plates until 80% confluency.…”

Section: In Vitro Lh and Fsh Bioassaysmentioning

confidence: 99%

Biological activities of recombinant equine luteinizing hormone/chorionic gonadotropin (eLH/CG) expressed in Sf9 and Mimic insect cell lines

Legardinier¹,

Duonor-Cérutti²,

Devauchelle³

et al. 2005

Journal of Molecular Endocrinology

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Equine luteinizing hormone (eLH) and chorionic gonadotropin (eCG) are composed of identical and polypeptide chains, but eCG subunits are much more heavily glycosylated and sialylated. Consequently, eCG exhibits a much longer half-life than eLH in blood. Recombinant eLH/CG, expressed in Sf9 and Mimic insect cells, were compared with one another and to the natural hormones eCG and eLH. Mimic cells are stably-transformed Sf9 cells, expressing five mammalian genes encoding glycosyltransferases involved in the synthesis of complex N-carbohydrate chains. Recombinant eLH/CG expressed in Mimic cells exhibited a higher apparent molecular weight (MW) than that expressed in Sf9 cells, suggesting that its N-glycosylation was, as expected, more complete. Nevertheless, the two recombinant eLH/CG exhibited lower MW than natural eCG from pregnant mare plasma. The two eLH/CG produced in Sf9 and Mimic cells were found to be active in in vitro LH and FSH bioassays, with potencies similar to those of eCG. By contrast, they exhibited no significant in vivo bioactivity, neither in the specific follicle-stimulating hormone (FSH) assay nor in the specific eCG assay. Although recombinant eLH/CG produced in Mimic cells bears more elaborate carbohydrate chains than recombinant eLH/CG from Sf9 cells, it exhibits no significant in vivo bioactivity, probably because of insufficient terminal sialylation of its carbohydrate chains, leading to its rapid removal from blood.

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Section: In Vitro Lh and Fsh Bioassaysmentioning

confidence: 99%

Biological activities of recombinant equine luteinizing hormone/chorionic gonadotropin (eLH/CG) expressed in Sf9 and Mimic insect cell lines

Legardinier¹,

Duonor-Cérutti²,

Devauchelle³

et al. 2005

Journal of Molecular Endocrinology

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“…Gonadotropins bind to classical Gprotein-associated seven-transmembrane domain receptors (Minegishi et al, 1991;Kelton et al, 1992). The receptors are unique in having a large extracellular domain, comprising nearly a half of the receptor protein, which is involved in hormone recognition and binding (Tilly et al, 1992;Nagayama et al, 1991).…”

Section: Gonadotropinsmentioning

confidence: 99%

The gonadotropins: Tissue-specific angiogenic factors?

Reisinger

Baal

McKinnon

et al. 2007

Molecular and Cellular Endocrinology

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“…The presence of conserved splice acceptor sites, such as a CAGG nucleotide sequence, may shorten the exons if it is located within the exons or caused incomplete intron splicing. 22 Splicing events result in a change of ORF, starting with the branch point.…”

Section: Fsh Receptor Gene Expressionmentioning

confidence: 99%