Chemistry: natural resins or derivatives; peptides or proteins; – Peptides of 3 to 100 amino acid residues – 11 to 14 amino acid residues in defined sequence
Reexamination Certificate
2006-04-04
2006-04-04
Murphy, Joseph (Department: 1646)
Chemistry: natural resins or derivatives; peptides or proteins;
Peptides of 3 to 100 amino acid residues
11 to 14 amino acid residues in defined sequence
C530S300000, C514S002600, C514S014800
Reexamination Certificate
active
07022815
ABSTRACT:
Novel parathyroid hormone(PTH) polypeptide derivatives are disclosed, as are pharmaceutical compositions containing said polypeptides, and synthetic and recombinant methods for producing said polypeptides. Also disclosed are methods for treating mammalian conditions characterized by decreases in bone mass using therapeutically effective pharmaceutical compositions containing said polypeptides. Also disclosed are methods for screening candidate compounds of the invention for antagonistic or agonistic effects on parathyroid hormone receptor action. Also disclosed are diagnostic and therapeutic methods of said compounds.
REFERENCES:
patent: 4086196 (1978-04-01), Tregear
patent: 4698328 (1987-10-01), Neer et al.
patent: 4736866 (1988-04-01), Leder et al.
patent: 4761406 (1988-08-01), Flora et al.
patent: 5393869 (1995-02-01), Nakagawa et al.
patent: 5501979 (1996-03-01), Geller et al.
patent: 5656465 (1997-08-01), Panicali et al.
patent: 5693616 (1997-12-01), Krstenansky et al.
patent: 5723577 (1998-03-01), Dong
patent: 5741486 (1998-04-01), Pathak et al.
patent: 5763416 (1998-06-01), Bonadio et al.
patent: 5836905 (1998-11-01), Lemelson et al.
patent: 5917123 (1999-06-01), McTiernan et al.
patent: 5922927 (1999-07-01), Bujard et al.
patent: 0 477 885 (1992-04-01), None
patent: 0 561 412 (1993-09-01), None
patent: 0 748 817 (1996-12-01), None
patent: WO 92/17581 (1992-10-01), None
patent: WO 95/11988 (1995-05-01), None
patent: WO 97/02834 (1997-01-01), None
patent: WO 00/31266 (2000-06-01), None
Luck MD et al. The (1-14) fragment of parathyroid hormone (PTH) activates intact and amino-terminally truncate PTH-1 receptors. Mol Endocrinol. May 1999;13(5):670-80.
Voet et al. Biochemistry. 1990. John Wiley & Sons, Inc. pp. 126-128 and 228-234.
Mickle JE et al. Genotype-phenotype relationships in cystic fibrosis. Med Clin North Am. May 2000;84(3):597-607.
Yan et al., Two-amino acid molecular switch in an epithelial morphogen that regulates binding to two distinct receptors. Science 290: 523-527, 2000.
Altschul, S.F., et al., “Basic Local Alignment Search Tool,”J. Mol. Biol. 215:403-410, Academic Press (1990).
Azarani, A., et al., “Structurally Diverse N-terminal Peptides of Parathyroid Hormone (PTH) and PTH-related Peptide (PTHRP) Inhibit the Na+/H+Exchanger NHE3 Isoform by Binding to the PTH/PTHRP Receptor Type I and Activating Distinct Signaling Pathways,”J. Biol. Chem. 271:14931-14936, American Society for Biochemistry and Molecular Biology (1996).
Barbier, J.-R., et al., “Bioactivities and Secondary Structures of Constrained Analogues of Human Parathyroid Hormone: Cyclic Lactams of the Receptor Binding Region,”J. Med. Chem. 40:1373-1380, The American Chemical Society (1997).
Bisello, A., et al., “Parathyroid Hormone-Receptor Interactions Identified Directly by Photocross-linking and Molecular Modeling Studies,”J. Biol. Chem. 273:22498-22505, American Society for Biochemistry and Molecular Biology (Aug. 1998).
Born, W., et al., “Inhibition of Parathyroid Hormone Bioactivity by Human Parathyroid Hormone (PTH)-(3-84) and PTH-(8-84) Synthesized inEscherichia coli,” Endocrinol. 123:1848-1853, The Endocrine Society (1988).
Broadus, A.E., and Stewart, A.F., “Parathyroid Hormone-Related Protein: Structure, Processing and Physiological Actions,” inThe Parathyroids. Basic and Clinical Concepts, Bilezikian, J.P., et al., eds., Raven Press, N.Y., pp. 259-294 (1994).
Caulfield, M.P., et al., “The Bovine Renal Parathyroid Hormone (PTH) Receptor Has Equal Affinity for Two Different Amino Acid Sequences: The Receptor Binding Domains of PTH and PTH-Related Protein Are Located within the 14-34 Region,”Endocrinol. 127:83-87, The Endocrine Society (1990).
Cenatiempo, Y., “Prokaryotic gene expression in vitro transcription—translation coupled systems,”Biochimie 68:505-515, Elsevier (1986).
Chorev, M., et al., “Modifications of Position 12 in Parathyroid Hormone and Parathyroid Hormone Related Protein: Toward the Design of Highly Potent Antagonists,”Biochem. 29:1580-1586, The American Chemical Society (1990).
Cohen, F.E., et al., “Analogues of Parathyroid Hormone Modified at Positions 3 and 6,”J. Biol. Chem. 266:1997-2004, American Society for Biochemistry and Molecular Biology (1991).
Cwirla, S. E., et al., “Peptide Agonist of the Thrombopoetin Receptor as Potent as the Natural Cytokine,”Science 276:1696-1699, American Association for the Advancement of Science (Jun. 1997).
Dong, M., et al., “Demonstration of a Direct Interaction between Residue 22 in the Carboxyl-terminal Half of Secretin and the Amino-terminal Tail of the Secretin Receptor Using Photoaffinity Labeling,”J. Biol. Chem. 274:903-909, American Society for Biochemistry and Molecular Biology (Jan. 1999).
Fairwell, T., et al., “Total Solid-Phase Synthesis, Purification, and Characterization of Human Parathyroid Hormone-(1-84),”Biochem. 22:2691-2697, The American Chemical Society (1983).
Gardella, T.J., et al., “Expression of Human Parathyroid Hormone-(1-84) inEscherichia colias a Factor X-cleavable Fusion Protein,”J. Biol. Chem. 265:15854-15859, American Society for Biochemistry and Molecular Biology (1990).
Gardella, T.J., et al., “Mutational Analysis of the Receptor-activating Region of Human Parathyroid Hormone,”J. Biol. Chem. 266:13141-13146, American Society for Biochemistry and Molecular Biology (1991).
Gardella, T.J., et al., “Analysis of Parathyroid Hormone's Principal Receptor-Binding Region by Site-Directed Mutagenesis and Analog Design,”Endocrinol. 132:2024-2030, The Endocrine Society (1993).
Gardella, T.J., et al., “Parathyroid Hormone (PTH)-PTH-related Peptide Hybrid Peptides Reveal Functional Interactions between 1-14 and 15-34 Domains of the Ligand,”J. Biol. Chem. 270:6584-6588, American Society for Biochemistry and Molecular Biology (1995).
Goltzmann, D., et al., “Analysis of the Requirements for Parathyroid Hormone Action in Renal Membranes with the Use of Inhibiting Analogues,”J. Biol. Chem. 250:3199-3203, American Society for Biochemistry and Molecular Biology (1975).
Gombert, F.O., et al., “Alanine and D-Amino Acid Scan of Human Parathyroid Hormone,” inPeptides: Chemistry, Structure and Biology, Kaumaya, P.T.P. and Hodges, R.S., eds., Mayflower Scientific Ltd., England, UK, pp. 661-662 (1996).
Gottesman, S., “Bacterial Regulation: Global Regulatory Networks,”Ann. Rev. Genet. 18:415-441, Annual Reviews, Inc. (1984).
Goud, N.A., et al., Solid-Phase Synthesis and Biologic Activity of Human Parathyroid Hormone(1-84),J. Bone Min. Res. 6:781-789, Mary Ann Liebert, Inc. (1991).
Hoare, S.R.J., et al., “Measurement of Agonist and Antagonist Ligand-Binding Parameters at the Human Parathyroid Hormone Type 1 Receptor: Evaluation of Receptor States and Modulation by Guanine Nucleotide,”J. Pharmacol. Exp. Ther. 289:1323-1333, American Society for Pharmacology and Experimental Therapeutics (Jun. 1999).
Holtmann, M.H., et al., “Critical Contributions of Amino-terminal Extacellular Domains in Agonist Biding and Activation of Secretin and Vasoactive Intestinal Polypeptide Receptors,”J. Biol. Chem. 270: 14394-14398, American Society for Biochemistry and Molecular Biology (1995).
Holtmann, M. H., et al., “Molecular Basis and Species Specificity of High Affinity Binding of Vasoactive Intestinal Polypeptide by the Rat Secretin Receptor,”J. Pharmacol. Exp Ther. 279:555-560, American Society for Pharmacology and Experimental Therapeutics (1996).
Horiuchi, N., et al., “A Parathyroid Hormone Inhibitor in vivo: Design and Biological Evaluation of a Hormone Analog,”Science 220:1053-1055, American Association for the Advancement of Science (1983).
Izaki, K., “Plasmid Induced Heavy Metal Resistance in Bateria,”Jpn. J. Bacteriol. 33:729-742, Japanese Society for Bacteriology (1978) [in Japanese].
Gardella Thomas J.
Jüppner Harald
Kronenberg Henry M.
Potts, Jr. John T.
Murphy Joseph
Sterne Kessler Goldstein & Fox P.L.L.C.
The General Hospital Corporation
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