FSH glycosylation variant D3N

Details FSH glycosylation variant D3N FSH glycosylation variant D3N

2011-06-07

2011-06-07

Shafer, Shulamith H (Department: 1647)

Drug, bio-affecting and body treating compositions

Designated organic active ingredient containing

Peptide containing doai

C424S198100, C424S185100, C424S195110, C435S325000, C435S069400, C435S360000, C530S398000, C530S397000, C530S399000

Reexamination Certificate

active

07956034

ABSTRACT:
FSH mutant with increased glycosylation and longer half-life is described. The use of this FSH mutant for inducing folliculogenesis in human patients is also described.

REFERENCES:
patent: WO 01/58493 (2001-08-01), None
patent: WO 2004/050679 (2004-06-01), None
patent: WO 2005/020934 (2005-03-01), None
Bishop, L.A. et al. “Both of the β-Subunit Carbohydrate Residues of Follicle-Stimulating Hormone Determine the Metabolic Clearance Rate and in Vivo Potency”Endocrinology, 1995, pp. 2635-2640, vol. 136, No. 6.
Chappel, S. et al. “Follicle stimulating hormone and its receptor: future perspectives”Human Reproduction, 1998, pp. 18-35 and 47-51, vol. 13, Supplement No. 3.
D'Antonio, M. et al. “Biological characterization of recombinant human follicle stimulating hormone isoforms”Human Reproduction, 1999, pp. 1160-1167, vol. 14, No. 5.
Furuhashi, M. et al. “Effect of AdditionalN-Glycosylation Signal in theN-Terminal Region on Intracellular Function of the Human Gonadotropin α-Subunit”Endocrine Journal, Jun. 2003, pp. 245-253, vol. 50, No. 3.
Galway, A. B. et al. “In Vitro and in Vivo Bioactivity of Recombinant Human Follicle-Stimulating Hormone and Partially Deglycosylated Variants Secreted by Transfected Eukaryotic Cell Lines”Endocrinology, 1990, pp. 93-100, vol. 127, No. 1.
Grossman, M. et al. “Site-Directed Mutagenesis of Amino Acids 33-44 of the Common α-Subunit Reveals Different Structural Requirements for Heterodimer Expression among the Glycoprotein Hormones and Suggests that Cyclic Adenosine 3′,5′-Monophosphate Production and Growth Promotion are Potentially Dissociable Functions of Human Thyrotropin”Molecular Endocrinology, 1996, pp. 769-779, vol. 10, No. 6.
Liu, C. et al. “Site-directed Alanine Mutagenesis of Phe33, Arg35, and Arg42-Ser43-Lys44in the Human Gonadotropin α-Subunit”The Journal of Biological Chemistry, Oct. 15, 1993, pp. 21613-21617, vol. 268, No. 29.
Perlman, S. et al. “Glycosylation of an N-Terminal Extension Prolongs the Half-Life and Increases the in Vivo Activity of Follicle Stimulating Hormone”Journal of Clinical Endocrinology and Metabolism, Jul. 2003, pp. 3227-3235, vol. 88, No. 7.
Roth, K.E. et al. “Scanning-alanine mutagenesis of long loop residues 33-53 in follicle stimulating hormone beta subunit”Molecular and Cellular Endocrinology, 1995, pp. 143-149, vol. 109.
Valove, F.M. et al. “Receptor Binding and Signal Transduction are Dissociable Functions Requiring Different Sites on Follicle Stimulating Hormone”Endocrinology, 1994, pp. 2657-2661, vol. 135, No. 6.
Weenen, C. et al. “Long-Acting Follicle-Stimulating Hormone Analogs Containing N-Linked Glycosylation Exhibited Increased Bioactivity Compared with O-Linked Analogs in Female Rats”Journal of Clinical Endocrinology and Metabolism, Oct. 2004, pp. 5204-5212, vol. 89, No. 10.
Yoo, J. et al. “COOH-terminal Amino Acids of the α Subunit Play Common and Different Roles in HumanChoriogonadotropinandFollitropin”The Journal of Biological Chemistry, Jun. 25, 1993, pp. 13034-13042, vol. 268, No. 18.
Database Geneseq [Online], Jan. 29, 2002, “Human FSH-alpha subunit mutant D3N/Q5T”, XP-002439754, Database Accession No. AAM51736, p. 1.
Database Geneseq [Online], Jan. 29, 2002, “Human FSH-alpha subunit mutant D3N/Q5S”, XP-002439755, Database Accession No. AAM51735, p. 1.

Affiliated with

Also associated with

Rating

FSH glycosylation variant D3N does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with FSH glycosylation variant D3N, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and FSH glycosylation variant D3N will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-2698115