Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai
Patent
1997-07-14
1999-12-07
Celsa, Bennett
Drug, bio-affecting and body treating compositions
Designated organic active ingredient containing
Peptide containing doai
514 24, 514866, 530324, A61K 3816, A61K 3828, C07K 1400
Patent
active
059983671
ABSTRACT:
Agonist analogues of amylin and related pharmaceutical compositions, and methods of treatment of diabetes and other insulin-requiring states, as well as methods of treatment of hypoglycemia, are provided.
REFERENCES:
patent: 5112945 (1992-05-01), Westermark et al.
patent: 5116948 (1992-05-01), Westermark et al.
patent: 5124314 (1992-06-01), Cooper
patent: 5175145 (1992-12-01), Cooper
patent: 5234906 (1993-08-01), Young et al.
patent: 5266561 (1993-11-01), Cooper et al.
patent: 5280014 (1994-01-01), Cooper et al.
patent: 5281581 (1994-01-01), Cooper et al.
patent: 5298605 (1994-03-01), Westermark et al.
patent: 5321008 (1994-06-01), Beaumont et al.
patent: 5367052 (1994-11-01), Cooper et al.
patent: 5405831 (1995-04-01), MacIntyre et al.
patent: 5424221 (1995-06-01), Westermark et al.
patent: 5424394 (1995-06-01), Gaeta et al.
patent: 5508260 (1996-04-01), Beaumont et al.
patent: 5527771 (1996-06-01), Beaumont et al.
patent: 5641744 (1997-06-01), Cooper et al.
patent: 5656590 (1997-08-01), Rink et al.
patent: 5686411 (1997-11-01), Gaeta et al.
Bell, Molecular Defects in Diabetes-Mellitus, Diabetes 40: 413-422 (1991).
Clark, A., et al., Islet Amyloid Formed From Diabetes-Associated Peptide May Be Pathogenic in Type-2 Diabetes, Lancet ii; 231-234 (1987).
Cooper, G.J.S., et al., Amylin and Non-Insulin-Dependent (Type 2) Diabetes Mellitus, In Diabetes 1988, ed. Larkins, R., Zimmet, P. & Chishol, D. (Elsevier, Amsterdam), pp. 493-496 (1989).
Cooper, G.J.S., et al., Purification and Characterization of a Peptide From Amyloid-Rich Pancreases of Type 2 Diabetic Patients, Proc. Natl. Acad. Sci. (USA) 84: 8628-8632 (1987).
Doherty, Endogenous Vasoactive Peptides, Annual Reports in Medicinal Chemistry, 26: 83-92 (1991).
Glenner et al., Amyloid Fibrils Formed From a Segment of the Pancreatic Islet Amyloid Protein, Biochem, Biophys. Res. Commun. 155: 608-614 (1988).
Gustavsson et al., Normal Transthyretin and Synthetic Transthyretin Fragments Form Amyloid-Like Fibrils In Vitro, Biochem. Biophys. Res. Commun. 175: 1159-1164 (1991).
Hilbich, et al., Aggregation and Secondary Structure of Synthetic Amyloid Beta-A4 Peptides of Alzheimer's Disease, J. Mol. Biol. 218: 149-163 (1991).
Johnson, et al., Amyloid In The Pancreatic-Islets of The Cougar (Felis-Concolor) Is Derived From Islet Amyloid Polypeptide (IAPP), Comp. Biochem. Physiol. 98: 115-119 (1991).
Johnson, et al., Newly Identified Pancreatic Protein Islet Amyloid Polypeptide--What Is Its Relationship to Diabetes?, Diabetes 40: 310-314 (1991).
O'Brien, et al.,Islet Amyloid Polypeptide and Insulin Secretion from Isolated Perfused Pancreas of Fed, Fasted, Glucose-Treated, and Dexamethasone-Treated Rats, Diabetes 40: 1701-1706 (1991).
Ohagi et al., Sequences of Islet Amyloid Polypeptide Precursors of an Old-World Monkey, The Pig-Tailed Macaque (Macaca-Nemestrina), and The Dog (Canis familiaris), Diabetologia 34 555-558 (1991).
Porte, Beta Cells in Type II Diabetes Mellitus, Diabetes 40: 166-180 (1991).
Steiner, et al., Is Islet Amyloid Polypeptide A Significant Factor In Pathogenesis or Pathophysiology of Diabetes?, Diabetes 40: 305-309 (1991).
Stridsberg and Wilander, Islet Amyloid Polypeptide (IAPP)--A Short Review, Acta Oncologica 30: 451-456 (1991).
Westermark et al., Islet Amyloid Polypeptide: Pinpointing Amino Acid Residues Linked to Amyloid Fibril Formation, Proc. Natl. Acad. Sci. (USA) 87:5036-5040 (1990).
Roberts et al., PNAS USA vol. 86(24) 9662-6 (Dec. 1989).
Cooper et al., PNAS USA vol. 85 pp. 7763-7766 (Oct. 1988).
Dayhoff et al., Atlas of Protein Sequence & Structure, 1972 vol. 5 pp. 89-99 ("A Model of Evolutionary Change in Proteins").
Goodman & Gilman, Pharmacological Basis of Therapeutics, 6th Ed. pp. 1514-1519 (MacMillan Publishing, 1980).
Betsholtz et al., "Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species," FEBS Letts. 251:261-264 (1989).
Betsholtz et al., "Islet Amyloid Polypeptide (IAPP): cDNA Cloning and Identification of an Amyloidogenic Region Associated with the Species-Specific Occurrence of Age-Related Diabetes Mellitus," Exp. Cell Res. 183:484-493 (1989).
Betsholtz et al., "Factors Affecting Diabetogenesis and Amyloidogenesis are Provided by Studies of IAPP in the Dog and Cat," In Natvig, J.B. et al. (Editors). Amyloid and Amyloidogenesis, 1990. Norwall, Mass.:Kluwer Academic Publishers, 1991; 445-448.
Cooper et al., "Amylin and the amylin gene: structure, function and relationship to islet amyloid and to diabetes mellitus," Biochem Biophys. Acta 1014:247-258 (1989).
Cooper et al., "The amylin superfamily: A novel grouping of biologically active polypeptides related to the insulin A-chain," Progress in Growth Factor Research 1:99-105 (1989).
Dayhoff et al., "Atlas of Protein Sequence and Structure," vol. 5, pp. 89-99 (1972).
Deems et al., "Amylin and CGRO (8-37) fragments reverse amylin-induced inhibition of 14C-glycogen accumulation," Biochem. Biophys. Res. Commun. 181:116-120 (1991).
Goodman & Gilman, "The Pharmacological Basis of Therapeutics," 6th Ed., pp. 1514-1519 (1980).
Hubbard et al., "Solution structures of calcitonin-gene-related-peptide analogues of calcitonin-gene-related peptide and amylin," Biochem. J. 275:785-788 (1991).
Johnson et al., "Islet Amyloid Polypeptide: Mechanisms of Amyloidogenesis in the Pancreatic Islets and Potential Roles in Diabetes Mellitus," Laboratory Investigation 66: 522-535 (1992).
Johnson et al., "Islet Amyloid, Islet-Amyloid Polypeptide, and Diabetes Mellitus," New. Engl. J. Med. 321:513-518 (1989).
Jordan et al., "Canine IAPP cDNA Sequence Provides Important Clues Regarding Diabetogenesis and Amyloidogenesis in Type 2 Diabetes," Biochem. Biophys. Res. Commun. 169:502-508 (1990).
Leffert, et al., "Rat amylin: cloning and tissue-specific expression in pancreatic islets," Proc. Natl Acad Sci USA 86: 3127-3130 (1989).
Michi et al., "Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone," Proc. Natl. Acad. Sci. (USA) 86:5738-5742 (1989).
Nishi et al., "Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone," Proc. Natl. Acad. Sci. (USA) 86:5738-5742 (1989).
Poyner, "Pharmacology of receptors for calcitonin gene-related peptide and amylin," Tips 16:424 (1995).
Saldanha and Mahadevan, "Molecular model-building of amylin and alpha calcitonin gene related polypeptide hormones using a combination of knowledge sources," Protein Engineering 4:539-543 (1991).
Westermark, et al., "A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas," Biochem. Biophys. Res. Commun. 140 (3): 827-31 (1986).
Westermark, et al., "Islet amyloid in type 2 human diabetes mellitus and adult diabetic cats contains a novel putative polypeptide hormone," Am. J. Pathol. 127 (3): 414-7 (1987).
Westermark et al., "Islet amyloid polypeptide (IAPP) and pro-IAPP immunoreactivitity in human islets of Langerhans," Diabetes Res. & Clin. Pract. 7:219-226 (1989).
Westermark et al., "Islet amyloid polypeptide in humans and cats," In: Shafrir, E., (Editor). Frontiers in diabetes research: Lessons from animal diabetes III. London: Smith-Gordon Limited, 1991: p. 499-501.
Albrecht Elisabeth
Gaeta Laura S. L.
Jones Howard
Amylin Corporation
Celsa Bennett
LandOfFree
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