Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Reexamination Certificate
2006-10-19
2008-08-05
Carlson, Karen Cochrane (Department: 1656)
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
C530S303000, C530S402000, C530S421000, C530S333000
Reexamination Certificate
active
07407932
ABSTRACT:
Methods for use of an exendin, an exendin agonist, or a modified exendin or exendin agonist having an exendin or exendin agonist linked to one or more polyethylene glycol polymers, for example, for lowering glucagon levels and/or suppressing glucagon secretion in a subject are provided. These methods are useful in treating hyperglucagonemia and other conditions that would be benefited by lowering plasma glucgon or suppressing glucagon secretion.
REFERENCES:
patent: 4179337 (1979-12-01), Frank et al.
patent: 5264372 (1993-11-01), Beaumont et al.
patent: 5424286 (1995-06-01), Eng
patent: 5686511 (1997-11-01), Bobo
patent: 5839443 (1998-11-01), Rose et al.
patent: 6051557 (2000-04-01), Drucker
patent: 6376549 (2002-04-01), Fine et al.
patent: 6451974 (2002-09-01), Hansen
patent: 6924264 (2005-08-01), Prickett et al.
patent: 2005/0026834 (2005-02-01), Cox et al.
patent: 199731732 (1998-01-01), None
patent: WO-95/07098 (1995-03-01), None
patent: WO-97/46584 (1997-12-01), None
patent: WO-98/05351 (1998-02-01), None
patent: WO-98/30231 (1998-07-01), None
patent: WO-99/07404 (1999-02-01), None
patent: WO-99/25727 (1999-05-01), None
patent: WO-99/25728 (1999-05-01), None
patent: WO-99/40788 (1999-08-01), None
patent: WO-00/41546 (2000-07-01), None
patent: WO-00/41548 (2000-07-01), None
Delgado et al. (1992) “The uses and properties of PEG-linked proteins”, Crit. Rev. Ther. Drug Carrier. Syst., vol. 9, issues 3-4, pp. 249-304.
Doyle et al. (2005) “In vivo biological activity of exendin (1-30)”, Endocrine, Vo. 27, No. 1, pp. 1-9.
Merriam-Webster (2007, updated) Diacid, http://www.m-w.com/cgi-bin/dictionary, p. 1.
Buse et al. (2002) Amylin Replacement With Pramlintide in Type 1 and Type 2 Diabetes: A Physiological Approach to Overcome Barriers With Insulin Therapy, Clin. Dibetes, vol. 20, pp. 137-144.
Schaschke N. (2007) (2S,3S)-Oxirane-2,3-dicarboxylic acid: a privileged platform for probing human cysteine cathepsins. J Biotechnol., vol. 129, No. 2, pp. 308-315.
Dicarboxylic acids (2007, updated) Dicarboxylic acids, http://www.cyberlipid.org/fa/acid0004.htm, pp. 1-5.
Bloom, S.R. et al. (1987) “Glucagonoma syndrome” Am. J. Med. vol. 82, pp. 25-36.
Byrne, M.M., et al., “Lessons from Human Studies with Glucagon-like Peptide-1: Potential of the Gut Hormone for Clinical Use,” Front. Diabetes, 13:219-33(1997).
Chen, Y.E., et al., “Tissue-specific Expression of Unique mRNAs That Encode Proglucagon-derived Peptides or Exendin 4 in the Lizard,” Journal of Biological Chemistry, 272(7): 4108-4115 (1997).
Creutzfeldt, W.O.C., et al., “Glucagonostatic Actions and Reduction of Fasting Hyperglycemia by Exogenous Glucagon-like Peptide I(7-36) Amide in Type I Diabetic Patients,” Diabetes Care 19(6):580-6 (1996).
D'Alessio, et al., “Elimination of the Action of Glucagon-like Peptide 1 Causes an Impairment of Glucose Tolerance after Nutrient Ingestion by Healthy Baboons,” J. Clin. Invest., 97:133 38 (1996).
Daniel, O. et al., “Use of Glucagon in the Treatment of Acute Diverticultis,” British Medical Journal, 3:720-2, (1974).
Drucker, D.J. “Glucaton-like peptides” Diabetes, vol. 47, pp. 159-169 (1998).
Egan, J.M., et al., “Glucagon-like Peptide-1 Restores Acute Phase Insulin Release to Aged Rats,” Diabetologia, 40(Supp 1):A130 abstract 505 (1997).
Eissele, et al., “Rat Gastric Somatostatin and Gastrin Release: Interactions of Exendin-4 and Truncated Glucagon-like Peptide-1 (GLP-1) Amide,” Life Sci., 55(8):629 34 (1994).
Eng, J., et al., “Purification and Structure of Exendin-3, a New Pancreatic Secretagogue Isolated from Heloderma horridum venom,” J. Biol. Chem., 265(33):20259 62 (1990).
Eng, J., et al., “Isolation and Characterization of Exendin-4, an Exendin-3 Analogue, from Heloderma suspectum Venom,” J. Biol. Chem., 267(11):7402 05 (1992).
Eng, J., “Prolonged Effect of Exendin-4 on Hyperglycemia of db/db mice,” Diabetes, 45(Supp 2):152A (abstract 554) (1996).
Francis, et al., “PEGylation of Cytokines and Other Therapeutic Proteins and Peptides: the Importance of Biological Optimisation of Coupling Techniques,” International Journal.
Glauser, et al., “Intravenous Glucagon in the Management of Esophageal Food Obstruction,” JACEP, 8:228-231 (1979).
Goke, et al. “Exendin-4 Is a High Potency Agonist and Truncated Exendin-(9-39)-amide an Antagonist at the Glucagon-like Peptide 1-(7-36)-amide Receptor of Insulin-secreting β-Cells,” J. Biol. Chem., 268(26):19650 55 (1993).
Malhotra, et al., “Exendin-4, a New Peptide from Heloderma Suspectum Venom, Potentiates Cholecystokinin-Induced Amylase Release from Rat Pancreatic Acini,” Regulatory Peptides, 41:149 56 (1992).
Markletter, Aug. 24, 1998 (p. n/a).
O'Halloran, et al., “Glucagon-like Peptide-1 (7-36)-NH2: A Physiological Inhibitor of Gastric Acid Secretion in Man,” J. Endocrinol. 126(1):169 73 (1990).
Ørskov, et al., “Biological Effects and Metabolic Rates of Glucagonlike Peptide-1 7-36 Amide and Glucagonlike Peptide-1 7-37 in Healthy Subjects Are Indistinguishable,” Diabet.
Parhes, D.G. et al. (2001) “Insulinotropic actions oif exendin-4 and glucagon-like peptide-1 in vivo and in vitro” Metabolis, vol. 50, pp. 583-589.
Passa, P., et al., “Mechanisms Suppressing Glucagon Secretion in Glucagonomas,” Diabetologia, 19(3):305 [abstract 298] (1980).
Raufman, et al. “Truncated Glucagon-like Peptide-1 Interacts with Exendin Receptors in Dispersed Acini from Guinea Pig Pancreas,” J. Biol. Chem., 267(30):21432 37 (1992).
Schepp, et al., “Exendin-4 and Exendin-(9-39)NH2: Agonist and Antagonist, Respectively, at the Rat Parietal Cell Receptor for Glucagon-like Peptide-1-(7-36)NH2,” Eur. J. Pharm.
Schjoldager, et al., “GLP-1 (Glucagon-like Peptide 1) and Truncated GLP-1, Fragments of Human Proglucagon, Inhibit Gastric Acid Secretion in Humans,” Dig. Dis. Sci., 34(5):703.
Singh, et al., “Use of 125l-[Y39]exendin-4 to Characterize Exendin Receptors on Dispersed Pancreatic Acini and Gastric Chief Cells from Guinea Pig,” Regul. Pep., 53:47 59 (1994).
Stower, et al., “A Trial of Glucagon in the Treatment of Painful Biliary Tract Disease,” Br. J. Surg., 69:591 2 (1982).
Thorens, “Expression Cloning of the Pancreatic β Cell Receptor for the Gluco-Incretin Hormone Glucagon-like Peptide 1,” Proc. Natl. Acad. Sci. USA, 89:8641 45 (1992).
Turton, M.D., et al., “A Role for Glucagon-like Peptide-1 in the Central Regulation of Feeding,” Nature, 379:69-72 (1996).
Wettergren, et al., “Truncated GLP-1 (Proglucagon 78-107-Amide) Inhibits Gastric and Pancreatic Functions in Man,” Dig. Dis. Sci., 38(4):665 73 (1993).
Willms, et al., Gastric Emptying, Glucose Responses, and Insulin Secretion after a Liquid Test Mal: Effects of Exogenous Glucagon-Like Peptide-1 (GLP-1)-(7-36) Amide in Type.
Gedulin Bronislava
Young Andrew A.
Amylin Pharmaceuticals Inc.
Carlson Karen Cochrane
Liu Samuel W
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