Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF ) Freely available
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (14)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by D'Antonio, M.
Right arrow Articles by Papoian, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by D'Antonio, M.
Right arrow Articles by Papoian, R.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Human Reproduction, Vol. 14, No. 5, 1160-1167, May 1999
© 1999 European Society of Human Reproduction and Embryology

Biological characterization of recombinant human follicle stimulating hormone isoforms

M. D'Antonio1, F. Borrelli, A. Datola, R. Bucci, M. Mascia, P. Polletta, D. Piscitelli and R. Papoian

Istituto di Ricerca C.Serono SpA, Via Valle Caia 22, I-00040 Ardea (Rome), Italy

It has been established that follicle stimulating hormone (FSH) circulates in the bloodstream as a heterogeneous population of molecules. Individual FSH isoforms, while displaying identical amino acid sequences, differ in their extent of post-translational modification. As a result of these variations, the FSH isoforms exhibit differences in overall charge, degree of sialic acid or sulphate incorporation, receptor binding affinity and plasma half-life. Taking advantage of the fact that these forms can be separated from each other on the basis of their charge, we have evaluated in rats the metabolic clearance rates of the acidic [with an isoelectric point (pI) <=ISOdia<= 4.8] and the less acidic (pI > 4.8) isoforms of recombinant human FSH (rhFSH) obtained after chromatofocusing. The less acidic isoform group was found to have a faster clearance from the circulation in rats as compared with the acidic isoform group. This finding is in agreement with the lower bioactivity in vivo (as determined by the Steelman–Pohley assay) of the less acidic isoform group, compared with the acidic one. The mass spectra of the two groups of isoforms showed a difference in the sialic acid content thus highlighting the importance of these residues on the in-vivo activity of FSH. Conversely, when the two groups of isoforms were tested in vitro by using the Y1 human FSH receptor (Y1 hFSHR) assay and a reporter gene assay, no significant differences in the biological activities between these preparations were detected when test concentrations were based on mass.

Key words: biopotency/FSH/Gonal-F/isoforms/metabolic clearance rates

1 To whom correspondence should be addressed at present address: Istituto di Ricerca C.Serono SpA, Via Rubes 5, I-10010 Colleretto Giacosa (Turin), Italy


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Hum Reprod UpdateHome page
B.C.J.M. Fauser, B.M.J.L. Mannaerts, P. Devroey, A. Leader, I. Boime, and D.T. Baird
Advances in recombinant DNA technology: corifollitropin alfa, a hybrid molecule with sustained follicle-stimulating activity and reduced injection frequency
Hum. Reprod. Update, May 1, 2009; 15(3): 309 - 321.
[Abstract] [Full Text] [PDF]

Home page
 J. Clin. Endocrinol. Metab.Home page
C. Weenen, J. E. Pena, S. V. Pollak, J. Klein, L. Lobel, R. K. Trousdale, S. Palmer, E. G. Lustbader, R. T. Ogden, and J. W. Lustbader
Long-Acting Follicle-Stimulating Hormone Analogs Containing N-Linked Glycosylation Exhibited Increased Bioactivity Compared with O-Linked Analogs in Female Rats
J. Clin. Endocrinol. Metab., October 1, 2004; 89(10): 5204 - 5212.
[Abstract] [Full Text] [PDF]

Home page
 J. Clin. Endocrinol. Metab.Home page
S. Perlman, B. van den Hazel, J. Christiansen, S. Gram-Nielsen, C. B. Jeppesen, K. V. Andersen, T. Halkier, S. Okkels, and H. T. Schambye
Glycosylation of an N-Terminal Extension Prolongs the Half-Life and Increases the in Vivo Activity of Follicle Stimulating Hormone
J. Clin. Endocrinol. Metab., July 1, 2003; 88(7): 3227 - 3235.
[Abstract] [Full Text] [PDF]

Home page
 Hum ReprodHome page
Z. Kilani, A. Dakkak, S. Ghunaim, G.E. Cognigni, C. Tabarelli, L. Parmegiani, and M. Filicori
A prospective, randomized, controlled trial comparing highly purified hMG with recombinant FSH in women undergoing ICSI: ovarian response and clinical outcomes
Hum. Reprod., June 1, 2003; 18(6): 1194 - 1199.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
A. Gervais, Y.-a. Hammel, S. Pelloux, P. Lepage, G. Baer, N. Carte, O. Sorokine, J.-m. Strub, R. Koerner, E. Leize, et al.
Glycosylation of human recombinant gonadotrophins: characterization and batch-to-batch consistency
Glycobiology, March 1, 2003; 13(3): 179 - 189.
[Abstract] [Full Text] [PDF]

Home page
 Hum ReprodHome page
R. Schats, P.D. Sutter, S. Bassil, J.A.M. Kremer, H. Tournaye, J. Donnez, and o. b. o. T. F. a. A. study group
Ovarian stimulation during assisted reproduction treatment: a comparison of recombinant and highly purified urinary human FSH
Hum. Reprod., August 1, 2000; 15(8): 1691 - 1697.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.