FSH mutants

Drug – bio-affecting and body treating compositions – Antigen – epitope – or other immunospecific immunoeffector – Hormone or other secreted growth regulatory factor,...

Reexamination Certificate

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C514S002600, C530S397000, C530S398000, C530S300000

Reexamination Certificate

active

07740862

ABSTRACT:
FSH mutants with increased glycosylation and longer half-lives are described. The use of FSH mutants for inducing folliculogenesis in human patients is also described.

REFERENCES:
patent: 5864488 (1999-01-01), Isaacs et al.
patent: WO 91/16922 (1991-11-01), None
patent: WO 01/58493 (2001-08-01), None
patent: WO 2004/050679 (2004-06-01), None
patent: WO 2005/020934 (2005-03-01), None
patent: WO 2007/084441 (2007-07-01), None
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Weenen, C. et al. “Long-acting follicle-stimulating hormone analogs containing N-linked glycosylation exhibited increased bioactivity compared with O-linked analogs in female rates”Journal of Clinical Endocrinology and Metabolism, Oct. 2004, pp. 5204-5212, vol. 89, No. 10.
Chappel, S. et al. “Follicle stimulating hormone and its receptor: future perspectives”Human Reproduction, 1998, pp. 18-35 and 47-51, vol. 12, Supplement No. 3.
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.
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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.
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.
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.
D'Antonio, M. et al. “Biological characterization of recombinant human follicle stimulating hormone isoforms”Human Reproduction, 1999, pp. 1160-1167, vol. 14, No. 5.
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.
Yoo, J. et al. “COOH-terminal Amino Acids of the α Subunit Play Common and Different Roles in Human Choriogonadotropin and Follitropin”The Journal of Biological Chemistry, Jun. 25, 1993, pp. 13034-13042, vol. 268, No. 18.

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