Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2011-01-11
2011-01-11
Allen, Marianne P (Department: 1647)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C435S069700, C530S350000
Reexamination Certificate
active
07867973
ABSTRACT:
The object of the present invention is to provide a follistatin variant capable of specifically inhibiting GDF-8 activity without inhibiting activin activity. The present invention provides a follistatin variant polypeptide, which (a) comprises follistatin domain I; (b) does not comprise an amino acid sequence that is represented by formula (I): Cys-(X1)a-Cys-(X2)b-Cys-(X3)c-Cys-(X4)d-Cys-(X5)e-Cys-(X6)f-Cys-(X7)g-Cys-(X8)h-Cys-(X9)i-Cys (SEQ ID NO: 30) wherein X1, X2, X3, X4, X5, X6, X7, X8, and X9each independently represents the same or a different naturally occurring amino acid residue other than cysteine, “a” represents an integer between 2 and 6, “b” represents an integer between 3 and 7, “c” represents an integer between 7 and 11, “d” represents an integer between 0 and 4, “e” represents an integer between 1 and 6, “f” and “g” represent integers between 8 and 12, “h” represents an integer between 4 and 8, and “i” represents an integer between 11 and 15) and has 50% or more homology with the amino acid sequence of SEQ ID NO: 2 or SEQ ID NO: 29; and (c) selectively inhibits GDF-8 activity as compared with its inhibition of activin activity.
REFERENCES:
patent: 5182375 (1993-01-01), Ling et al.
patent: 5545616 (1996-08-01), Woodruff
patent: 6004937 (1999-12-01), Wood et al.
patent: 6096506 (2000-08-01), Lee et al.
patent: 2002/0157126 (2002-10-01), Lee et al.
patent: 2003/0162714 (2003-08-01), Hill et al.
patent: 2003/0162717 (2003-08-01), Schacter et al.
patent: 1355881 (2002-06-01), None
patent: 99/42573 (1999-08-01), None
patent: 99/45949 (1999-09-01), None
patent: 00/43781 (2000-07-01), None
patent: 01/05820 (2001-01-01), None
patent: 2001/0032871 (2001-05-01), None
patent: 01/53350 (2001-07-01), None
patent: 02/10214 (2002-02-01), None
patent: 02/055077 (2002-07-01), None
patent: 03/072715 (2003-09-01), None
McPherron et al., “Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member,”Nature, 387(6628):83-90 (1997).
Nakamura et al., “Activin-Binding Protein from Rat Ovary Is Follistatin,”Science, 247(4944):836-838 (1990).
Lee et al., “Regulation of myostatin activity and muscle growth,”Proc. Natl. Acad. Sci. USA, 98(16):9306-9311 (2001).
Shiozaki et al., “Evidence for the participation of endogenous activin A/erythroid differentiation factor in the regulation of erythropoisis,”Proc. Natl. Acad. Sci. USA, 89(5):1553-1556 (1992).
Zimmers et al., “Induction of Cachexia in Mice by Systemically Administered Myostatin,”Science, 296(5572):1486-1488 (2002).
Gonzalez-Cadavid et al., “Organization of the human myostatin gene and expression in healthy men and HIV-infected men with muscle wasting,”Proc. Natl. Acad. Sci. USA, 95(25):14938-14943 (1998).
Wagner et al., “Loss of Myostatin Attenuates Severity of Muscular Dystrophy in mdx Mice,”Ann. Neurol., 52(6):832-836 (2002).
McPherron et al., “Suppression of body fat accumulation in myostatin-deficient mice,”The Journal of Clinical Investigation, 109(5):595-601 (2002).
Uchida Tohru et al., “A Novel Epidermal Growth Factor-like Molecule Containing Two Follistatin Modules Stimulates Tyrosine Phophorylation of erbB-4 in MKN28 Gastric Cancer Cells”, Biochemical Biophysical Research Communications, vol. 266, pp. 593-602 (1999).
Liang Gangning et al., “The Gene for a Novel Transmembrane Protein Containing Epidermal Growth Factor and Follistatin Domain is Frequently Hypermethylated in Human Tumor Cells”, Cancer Research, vol. 60, pp. 4907-4912 (2000).
Shimasaki Shun'ichi et al., “Primary Structure of the Human Follistatin Precursor and its Genomic Organization”, Proc. Natl. Acad. Sci. USA, vol. 85, pp. 4218-4222 (1988).
Robertson D.M. et al., “The Isolation of Polypeptides with FSH Suppressing Activity from Bovine Follicular Fluid which are Structurally Different to Inhibin”, Biochemical and Biophysical Research Communications, vol. 149, No. 2, pp. 744-749 (1987).
Ueno Naoto et al., “Isolation and Partial Characterization of Follistatin: A Single-Chain Mr35, 000 Monomeric Protein that Inhibits the Release of Follicle-Stimulating Hormone”, Proc. Natl. Acad. Sci. USA, vol. 84, pp. 8282-8286 (1987).
Inouye et al. Biochemical and Biophysical Research Communications, vol. 179, No. 1, pp. 352-358, 1991.
Sidis et al. The Journal of Biological Chemistry, vol. 276, No. 21, pp. 17718-17726, 2001.
Tsuchida et al., J. Biol. Chem. (2000), vol. 275, No. 52, pp. 40788-40796.
Sidis et al., Endrocrinology, (2002), vol. 143, pp. 1613-1624.
Office Action in counterpart Japanese application No. 2004-355294, dated Oct. 19, 2010.
English Translation of Office Action in counterpart Japanese application No. 2004-355294, dated Oct. 19, 2010.
Murakami Tatsuya
Tsuchida Kunihiro
Allen Marianne P
Greenblum & Bernstein P.L.C.
Techno Networks Shikoku Co., Ltd.
LandOfFree
Follistatin variant polypeptide does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Follistatin variant polypeptide, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Follistatin variant polypeptide will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-2674087