Historical Background

Advances in Pharmacology

Volumn 52, Issue , 2005, Pages 1-18

  Young, Andrew ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

AMYLIN; AMYLOID;

AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; GENETICS; HISTORY; HUMAN; INSULINOMA; ISOLATION AND PURIFICATION; MOLECULAR GENETICS; PANCREAS TUMOR; REVIEW; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; AMYLOID; ANIMALS; HISTORY, 20TH CENTURY; HUMANS; INSULINOMA; MOLECULAR SEQUENCE DATA; PANCREATIC NEOPLASMS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 33645227988     PISSN: 10543589     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1054-3589(05)52001-5     Document Type: Review

References (169)

1. USAN council. List No. 392. New names. Amlintide. Anonymous. Clin. Pharmacol. Ther. 61 (1997) 500
2. Anonymous. USAN Council. List No. 419. New names. Pramlintide acetate. Clin. Pharmacol. Ther. 66 (1999) 332
3. Ahren B., and Pettersson M. Calcitonin gene-related peptide (CGRP) and amylin and the endocrine pancreas. Int. J. Pancreatol. 6 (1990) 1-15
4. Ahren B., Oosterwijk C., Lips C.J., and Hoppener J.W. Transgenic overexpression of human islet amyloid polypeptide inhibits insulin secretion and glucose elimination after gastric glucose gavage in mice. Diabetologia 41 (1998) 1374-1380
5. Ahronheim J.H. The nature of the hyaline material in the pancreatic islands in diabetes mellitus. Am. J. Pathol. 19 (1943) 873-882
6. Albrandt K., Mull E., Cooper G.J.S., and Johnson M.J. cDNA cloning of canine amylin and detection of tissue transcripts by PCR amplification. Diabetes 40 35A (1991) (abstract 137).
7. Ar'Rajab A., and Ahren B. Effects of amidated rat islet amyloid polypeptide on glucose-stimulated insulin secretion in vivo and in vitro in rats. Eur. J. Pharmacol. 192 (1991) 443-445
8. Artozqui M.E., Botella S.M., Camblor M., Breton L.I., and Moreno E.B. Amylin: its potential role in the etiopathogenicity of diabetes mellitus. Ann. Med. Interna 10 (1993) 200-202
9. Ashburn T.T., and Lansbury P.T. Interspecies sequence variations affect the kinetics and thermodynamics of amyloid formation-peptide models of pancreatic amyloid. J. Am. Chem. Soc. 115 (1993) 11012-11013
10. Badman M.K., Shennan K.I.J., Jermany J.L., Docherty K., and Clark A. Processing of pro-islet amyloid polypeptide (proIAPP) by the prohormone convertase PC2. FEBS Lett. 378 (1996) 227-231
11. Barakat A., Skoglund G., Boissard C., Rosselin G., and Marie J.C. Calcitonin gene-related peptide and islet amyloid polypeptide stimulate insulin secretion in RINm5F cells through a common receptor coupled to a generation of cAMP. Biosci. Rep. 14 (1994) 1-13
12. Bennet W.M., Beis C.S., Ghatei M.A., Byfield P.G.H., and Bloom S.R. Amylin tonally regulates arginine-stimulated insulin secretion in rats. Diabetologia 37 (1994) 436-438
13. Betsholtz C., Christmansson L., Engstrom U., Rorsman F., Svensson V., Johnson K.H., and Westermark P. Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species. FEBS Lett. 251 (1989) 261-264
14. Betsholtz C., Christmanson L., Engstrom U., Rorsman F., Jordan K., O'Brien T.D., Murtaugh M., Johnson K.H., and Westermark P. Structure of cat islet amyloid polypeptide and identification of amino acid residues of potential significance for islet amyloid formation. Diabetes 39 (1990) 118-122
15. Betsholtz C., Christmanson L., Gebre-Medhin S., and Westermark P. Islet amyloid polypeptide-Hen or egg in type 2 diabetes pathogenesis?. Acta Oncol. 32 (1993) 149-154
16. Bloom S.R. Paracrine regulation of regulatory peptides. Biomed. Res. 15 (1994) 1-4
17. Bretherton-Watt D., Gilbey S.G., Ghatei M.A., Beacham J., and Bloom S.R. Failure to establish islet amyloid polypeptide (amylin) as a circulating beta cell inhibiting hormone in man. Diabetologia 33 (1990) 115-117
18. Bretherton-Watt D., Ghatei M.A., Jamal H., Gilbey S.G., Jones P.M., and Bloom S.R. The physiology of calcitonin gene-related peptide in the islet compared with that of islet amyloid polypeptide (amylin). Ann. N Y Acad. Sci. 657 (1992) 299-312
19. Bretherton-Watt D., Gilbey S.G., Ghatei M.A., Beacham J., Macrae A.D., and Bloom S.R. Very high concentrations of islet amyloid polypeptide are necessary to alter the insulin response to intravenous glucose in man. J. Clin. Endocrinol. Metab. 74 (1992) 1032-1035
20. Broderick C.L., and Gold G. Human and rat amylin have no effect on insulin secretion in isolated rat islets or in HIT cells. Diabetes 40 (1991) 233A
21. Broderick C.L., Brooke G.S., DiMarchi R.D., and Gold G. Human and rat amylin have no effects on insulin secretion in isolated rat pancreatic islets. Biochem. Biophys. Res. Commun. 177 (1991) 932-938
22. Butler P.C. Islet amyloid and its potential role in the pathogenesis of type II diabetes mellitus. In: LeRoith D., Taylor S.I., and Olefsky J.M. (Eds). "Diabetes Mellitus" (1996), Lippincott-Raven Publishers, Philadelphia 113-117
23. Christmanson L., Betsholtz C., Leckstrom A., Engstrom U., Cortie C., Johnson K.H., Adrian T.E., and Westermark P. Islet amyloid polypeptide in the rabbit and European hare: Studies on its relationship to amyloidogenesis. Diabetologia 36 (1993) 183-188
24. Chuang L.M., Wu H.P., Jou T.S., Tai T.Y., and Lin B.J.I. Inhibitory effect of islet amyloid polypeptide on glucose-induced proinsulin biosynthesis in rat insulinoma cells. Pancreas 7 (1992) 472-476
25. Clark A. Islet amyloid: An enigma of type 2 diabetes. Diabet. Met. Rev. 8 (1992) 117-132
26. Clark A., Cooper G.J.S., Lewis C.E., Morris J.F., Willis A.C., Reid K.B., and Turner R.C. Islet amyloid formed from diabetes-associated peptide may be pathogenic in type-2 diabetes. Lancet 2 (1987) 231-234
27. Clark A., De Koning E., Hansen B., Bodkin N., and Morris J.F. Islet amyloid in glucose intolerant and spontaneous diabetic 'Macaca mulatta' monkeys. In: Shafrir E. (Ed). "Frontiers in Diabetes Research: Lessons from Animal Diabetes III" (1991), Smith-Gordon Limited, London 502-506
28. Clark A., Badman M.K., and deKoning E.J.P. Islet amyloid, islet amyloid polypeptide, islet function and glucose metabolism in diabetes. Diabet. Ann. 9 (1995) 33-56
29. Clark A., Charge S.B.P., Badman M.K., and deKoning E.J.P. Islet amyloid in type 2 (non-insulin-dependent) diabetes. APMIS 104 (1996) 12-18
30. Clark A., Charge S.B.P., Badman M.K., Mac Arthur D.A., and deKoning E.J.P. Islet amyloid polypeptide: Actions and role in the pathogenesis of diabetes. Biochem. Soc. Trans. 24 (1996) 594-599
31. Cook J.T.E., Patel P.P., Clark A., Hoppener J.W.M., Lips C.J.M., Mosselman S., O'Rahilly S., Page R.C., Wainscoat J.S., and Turner R.C. Non-linkage of the islet amyloid polypeptide gene with type-2 (non-insulin-dependent) diabetes mellitus. Diabetologia 34 (1991) 103-108
32. Cooper G.J.S., Willis A.C., Clark A., Turner R.C., Sim R.B., and Reid K.B. Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc. Natl. Acad. Sci. USA 84 (1987) 8628-8632
33. Cooper G.J.S., Leighton B., Dimitriadis G.D., Parry-Billings M., Kowalchuk J.M., Howland K., Rothbard J.B., Willis A.C., and Reid K.B. Amylin found in amyloid deposits in human type 2 diabetes mellitus may be a hormone that regulates glycogen metabolism in skeletal muscle. Proc. Natl. Acad. Sci. USA 85 (1988) 7763-7766
34. Cooper G.J.S., Day A.J., Willis A.C., Roberts A.N., Reid K.B., and Leighton B. Amylin and the amylin gene: Structure, function and relationship to islet amyloid and to diabetes mellitus. Biochim. Biophys. Acta 1014 (1989) 247-258
35. Cooper G.J.S., Leighton B., Willis A.C., and Day A.J. The amylin superfamily: A novel grouping of biologically active polypeptides related to the insulin A-chain. Prog. Growth Factor Res. 1 (1989) 99-105
36. Couce M., Kane L.A., OBrien T.D., Charlesworth J., Soeller W., McNeish J., Kreutter D., Roche P., and Butler P.C. Treatment with growth hormone and dexamethasone in mice transgenic for human islet amyloid polypeptide causes islet amyloidosis and beta-cell dysfunction. Diabetes 45 (1996) 1094-1101
37. de Koning E.J.P., Bodkin N.L., Hansen B.C., and Clark A. Diabetes-mellitus in Macaca-mulatta monkeys is characterised by islet amyloidosis and reduction in beta-cell population. Diabetologia 36 (1993) 378-384
38. de Koning E.J.P., Verbeek J.S., Esapa C., Laube B., and Clark A. Amyloid fibrils are formed from proislet amyloid polypeptide in transgenic mouse insulinoma cells. Diabetologia 42 (1999) A145
39. Dégano P., Peiro E., Silvestre R.A., Coma I., Salas M., and Marco J. Insulin responses of the amylin-infused rat pancreas to glucose vasoactive intestinal polypeptide and arginine. Diabetologia 34 (1991) A42
40. Dégano P., Salas M., Peiro E., Silvestre R.A., and Marco J. On the mechanism of the inhibitory effect of amylin on insulin secretion: Study in the perfused rat pancreas. Diabetologia 35 (1992) A115
41. Dégano P., Silvestre R.A., Salas M., Peiró E., and Marco J. Amylin inhibits glucose-induced insulin secretion in a dose-dependent manner. Study in the perfused rat pancreas. Regul. Pept. 43 (1993) 91-96
42. Ehrlich J.C., and Ratner I.M. Amyloidosis of the islets of langerhans. Am. J. Pathol. 38 (1961) 49-59
43. Fan L., Westermark G., Chan S.J., and Steiner D.F. Altered gene structure and tissue expression of islet amyloid polypeptide in the chicken. Mol. Endocrinol. 8 (1994) 713-721
44. Fehmann H.C., Weber V., Göke R., Göke B., Eissele R., and Arnold R. Islet amyloid polypeptide (IAPP;amylin) influences the endocrine but not the exocrine rat pancreas. Biochem. Biophys. Res. Commun. 167 (1990) 1102-1108
45. Fürnsinn C., Leuvenink H., Roden M., Nowotny P., and Waldhäusl W. Inhibition of glucose induced insulin secretion by amylin in rats in vivo. Diabetologia 35 (1992) A29
46. Fürnsinn C., Leuvenink H., Roden M., Nowotny P., Schneider B., Rohac M., Pieber T., Clodi M., and Waldhausl W. Islet amyloid polypeptide inhibits insulin secretion in conscious rats. Am. J. Physiol. 267 (1994) E300-E305
47. Gebre-Medhin S., Mulder H., Pekny M., Westermark G., Tornell J., Westermark P., Sundler F., Ahren B., and Betsholtz C. Increased insulin secretion and glucose tolerance in mice lacking islet amyloid polypeptide (amylin). Biochem. Biophys. Res. Commun. 250 (1998) 271-277
48. Gedulin B., Larson E., Provost S., and Koda J. The selective amylin antagonist, AC187, enhances the insulin response during intravenous glucose tolerance tests in anesthetized rats. Diabetes 42 Suppl. 1 (1993) 229A
49. Ghatei M.A., Datta H.K., Zaidi M., Bretherton-Watt D., Wimalawansa S.J., MacIntyre I., and Bloom S.R. Amylin and amylin-amide lack an acute effect on blood glucose and insulin. J. Endocrinol. 124 (1990) R9-R11
50. Gilbey S.G., Bretherton-Watt D., Beacham J., Ghatei M.A., and Bloom S.R. High dose amylin in man: Unexpected failure to affect intravenous glucose tolerance. BDA Diab. Med. 6 (1989) 5A
51. Göke R., McGregor G.P., and Göke B. Amylin alters biological effects of GLP-1 in the ß-cell. Digestion 54 (1993) 355-356
52. Göke R., McGregor G.P., and Göke B. Amylin alters the biological action of the incretin hormone GLP-1 (7-36)amide. Life Sci. 53 (1993) 1367-1372
53. Gold G., Dimarchi R.D., Broderick C.L., Bue J.M., Brooke G.S., and Yen T.T. Human amylin has no effect on either rate of insulin release or concentration of glucose in rodents. Diabetes 39 (1990) 142A
54. Hansen B. Primate animal models of non-insulin-dependent diabetes mellitus. In: LeRoith D., Taylor S.I., and Olefsky J.M. (Eds) (1996), Lippincott-Raven Publishers, Philadelphia 595-603
55. Hellman U., Wernstedt C., Westermark P., O'Brien T.D., Rathbun W.B., and Johnson K.H. Amino acid sequence from degu islet amyloid-derived insulin shows unique sequence characteristics. Biochem. Biophys. Res. Commun. 169 (1990) 571-577
56. Higham C.E., Lawrie L., Shennan K.I.J., Birch N., Docherty K., and Clark A. Synthetic pro-islet amyloid polypeptide is cleaved by recombinant prohormone convertases, PC2 and PC3 in vitro. Diabetologia 42 (1999) A145
57. Howard C.F. Spontaneous diabetes in macaca nigra: Relevance to human being with NIDDM. In: Camerini-Davalos R.A. (Ed) (1988), Plenum Press, New York 33-41
58. Hull R.L., Andrikopoulos S., Verchere C.B., Vidal J., Wang F., Cnop M., Prigeon R.L., and Kahn S.E. Increased dietary fat promotes islet amyloid formation and beta-cell secretory dysfunction in a transgenic mouse model of islet amyloid. Diabetes 52 (2003) 372-379
59. Inoue K., Hiramatsu S., Hisatomi A., Umeda F., and Nawata H. Effects of amylin on the release of insulin and glucagon from the perfused rat pancreas. Horm. Metab. Res. 25 (1993) 135-137
60. Jakob W. Unterschungen über die Amyloidose der Karnivoren unter besonderer Berücksichtigung der Altersamyloidose (Studies of amyloidosis of carnivora with special reference to amyloidosis of age). Zbl. Vet. Med. Series A (1970) 818-829
61. Janes S., Gaeta L., Beaumont K., Beeley N., and Rink T. The selection of pramlintide for clinical evaluation. Diabetes 45 (1996) 235A
62. Johnson K.H., O'Brien T.D., Hayden D.W., Mahoney W.C., Wernstedt C., and Westermark P. Relationships of islet amyloid polypeptide (IAPP) to spontaneous diabetes in adult cats. In: Isobe T., Araki S., Uchino F., Kito S., and Tsubura E. (Eds) (1988), Plenum Press, New York 673-678
63. Johnson K.H., O'Brien T.D., Betsholtz C., and Westermark P. Islet amyloid, islet-amyloid polypeptide, and diabetes mellitus. N. Engl. J. Med. 321 (1989) 513-518
64. Johnson K.H., O'Brien T.D., Jordan K., Betsholtz C., and Westermark P. The putative hormone islet amyloid polypeptide (IAPP) induces impaired glucose tolerance in cats. Biochem. Biophys. Res. Commun. 167 (1990) 507-513
65. Johnson K.H., O'Brien T.D., and Westermark P. Newly identified pancreatic protein islet amyloid polypeptide. What is its relationship to diabetes?. Diabetes 40 (1991) 310-314
66. Johnson K.H., Wernstedt C., O'Brien T.D., and Westermark P. Amyloid in the pancreatic islets of the cougar (Felis concolor) is derived from islet amyloid polypeptide (IAPP). Comp. Biochem. Physiol. B 98 (1991) 115-119
67. Johnson K.H., Jordan K., O'Brien T.D., Murtaugh M.P., Wernstedt C., Betsholtz C., and Westermark P. Factors affecting diabetogenesis and amyloidogenesis are provided by studies of IAPP in the dog and cat. In: Natvig J.B., et al. (Ed) (1991), Kluwer Academic Publishers, Norvell, MA 445-448
68. Johnson K.H., O'Brien T.D., Betsholtz C., and Westermark P. Islet amyloid polypeptide: Mechanisms of amyloidogenesis in the pancreatic islets and potential roles in diabetes mellitus. Lab. Invest. 66 (1992) 522-535
69. Jordan K., Murtaugh M.P., O'Brien T.D., Westermark P., Betsholtz C., and Johnson K.H. Canine IAPP cDNA sequence provides important clues regarding diabetogenesis and amyloidogenesis in type 2 diabetes. Biochem. Biophys. Res. Commun. 169 (1990) 502-508
70. Jordan K.C., O'Brien T.D., and Johnson K.H. Sequence of raccoon IAPP supports importance of a specific structural motif in the development of pancreatic islet amyloidosis. Amyloid Intl. J. Exp. Clin. Invest. 1 (1994) 160-164
71. Kahn S.E., Andrikopoulos S., Verchere C.B., Wang F., Hull R.L., and Vidal J. Oophorectomy promotes islet amyloid formation in a transgenic mouse model of type II diabetes. Diabetologia 43 (2000) 1309-1312
72. Kajio H., Kobayashi T., Hara M., Nakanishi K., Sugimoto T., Murase T., Akanuma Y., Kosaka K., Shibasaki Y., et al. Islet amyloid polypeptide (IAPP) gene analysis in a Japanese diabetic with marked islet amyloid deposition. Diabet. Res. Clin. Pract. 15 (1992) 45-48
73. Kamaeva O.I. Amylin and amyloidosis of the pancreatic islets and their significance in the etiology and pathogenesis of diabetes mellitus type 2. Ter. Arkh. 65 (1993) 14-17
74. Kapurniotu A., Bernhagen J., Al-Abed Y., and Bucala R. Amyloidogenic properties of AGE-modified amylin: Role in the amyloid deposition and islet cell dysfunction of Type II diabetes. Diabetes 45 (1996) 39A
75. Katafuchi T., Hamano K., Kikumoto K., and Minamino N. Identification of second and third calcitonin receptor-stimulating peptides in porcine brain. Biochem. Biophys. Res. Commun. 308 (2003) 445-451
76. Katafuchi T., Kikumoto K., Hamano K., Kangawa K., Matsuo H., and Minamino N. Calcitonin receptor-stimulating peptide, a new member of the calcitonin gene-related peptide family. Its isolation from porcine brain, structure, tissue distribution, and biological activity. J. Biol. Chem. 278 (2003) 12046-12054
77. Kitamura K., Kangawa K., Kawamoto M., Ichiki Y., Nakamura S., Matsuo H., and Eto T. Adrenomedullin: A novel hypotensive peptide isolated from human pheochromocytoma. Biochem. Biophys. Res. Commun. 192 (1993) 553-560
78. Kogire M., Ishizuka J., Thompson J.C., and Greeley G.H. Inhibitory action of islet amyloid polypeptide and calcitonin gene-related peptide on release of insulin from the isolated perfused rat pancreas. Pancreas 6 (1991) 459-463
79. Kulkarni R.N., Smith D.M., Ghatei M.A., Jones P.M., and Bloom S.R. Investigation of the effects of antisense oligodeoxynucleotides to islet amyloid polypeptide mRNA on insulin release, content and expression. J. Endocrinol. 151 (1996) 341-348
80. Leaming R., Johnson A., Hook G., Hanley R., and Baron A. Amylin modulates insulin secretion in humans. Studies with an amylin antagonist. Diabetologia 38 (1995) A113
81. Leffert J.D., Newgard C.B., Okamoto H., Milburn J.L., and Luskey K.L. Rat amylin: Cloning and tissue-specific expression in pancreatic islets. Proc. Natl. Acad. Sci. USA 86 (1989) 3127-3310
82. Lehman-deGaeta L.S., Willis A.C., Young A.A., Foot E.A., Albrecht E., Leighton B., Rink T.J., and Cooper G.J.S. Variability of chemically synthesized human amylin. Diabetes 40 (1991) 236A
83. Lewis C.E., Clark A., Ashcroft S.J., Cooper G.J.S., and Morris J.F. Calcitonin gene-related peptide and somatostatin inhibit insulin release from individual rat B cells. Mol. Cell Endocrinol. 57 (1988) 41-49
84. MacNamara C.M., Barrow B.A., Manley S.E., Levy J.C., Clark A., and Turner R.C. Parallel changes of proinsulin and islet amyloid polypeptide in glucose intolerance. Diabet. Res. Clin. Pract. 50 (2000) 117-126
85. Marco J., and Silvestre R. Effect of amylin on islet cell secretion. Exp. Clin. Endocrinol. Diabet. 105 (1997) 68
86. Marco J., Peiro E., Dégano P., Miralles P., and Silvestre R.E. Amylin inhibits insulin secretion in the perfused rat pancreas. Diabetes 39 (1990) 136A
87. Marzban L., Park K., and Verchere C.B. Islet amyloid polypeptide and type 2 diabetes. Exp. Gerontol. 38 (2003) 347-351
88. McCarthy M.I., Hitman G.A., Mohan V., Ramachandran A., Snehalatha C., and Viswanathan M. The islet amyloid polypeptide gene and non-insulin-dependent diabetes mellitus in south Indians. Diabet. Res. Clin. Pract. 18 (1992) 31-34
89. Mosselman S., Hoppener J.W.M., Zandberg J., vanMansfeld A.D.M., Guerts-van Kessel A.H.M., Lips C.J.M., and Jansz H.S. Islet amyloid polypeptide: Identification and chromosomal localization of the human gene. FEBS Lett. 23 (1988) 227-232
90. Mosselman S., Hoppener J.W.M., Lips C.J.M., and Jansz H.S. The complete islet amyloid polypeptide precursor encoded by two exons. FEBS Lett. 247 (1989) 154-158
91. Moyses C., Thompson R.G., and Kolterman O.G. Pramlintide, a human amylin analogue: A new approach to glycaemic control in patients with diabetes requiring insulin. First World Congress on Prevention of Diabetes and its Complications, April 25-28 1996, Lyngby, Denmark (1996) 151
92. Murakami M., Suzuki S., Sato Y., Shintami S., Abe S., Suzuki K., Ishuzuka J., and Toyota T. Effects of amylin on insulin secretion from RIN m5F cells. Diabetes 39 (1990) 266A
93. Nagamatsu S., Carroll R., and Steiner D.F. IAPP effects on pancreatic beta cell function in normal rat islets and BTC3 cell line. Diabetes 39 (1990) 67A
94. Nagamatsu S., Carroll R.J., Grodsky G.M., and Steiner D.F. Lack of islet amyloid polypeptide regulation of insulin biosynthesis or secretion in normal rat islets. Diabetes 39 (1990) 871-874
95. Nagamatsu S., Nishi M., and Steiner D.F. Effects of islet amyloid polypeptide (IAPP) on insulin biosynthesis or secretion in rat islets and mouse beta TC3 cells. Biosynthesis of IAPP in mouse beta TC3 cells. Diabet. Res. Clin. Pract. 15 (1992) 49-55
96. Nakazato M., Asai J., Kangawa K., Matsukura S., and Matsuo H. Establishment of radioimmunoassay for human islet amyloid polypeptide and its tissue content and plasma concentration. Biochem. Biophys. Res. Commun. 164 (1989) 394-399
97. Nishi M., and Steiner D.F. Cloning the complementary DNA's encoding islet amyloid polypeptide, insulin and glucagon precursors from a new world rodents, the Degu, Octodo. Mol. Endocrinol. 4 (1990) 1192-1198
98. Nishi M., Bell G.I., and Steiner D.F. Sequence of a cDNA encoding syrian hamster islet amyloid polypeptide precursor. Nucl. Acids Res. 18 (1990) 6726
99. Nishi M., Sanke T., Nagamaatsu S., Bell G.I., and Steiner D.F. Islet amyloid polypeptide: A new β cell secretory product related to islet amyloid deposits. J. Biol. Chem. 265 (1990) 4173-4176
100. Nishi M., Chan S.J., Nagamatsu S., Bell G.I., and Steiner D.F. 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 (1989) 5738-5742
101. O'Brien T.D., Westermark P., and Johnson K.H. Islet amyloid polypeptide (IAPP) does not inhibit glucose-stimulated insulin secretion from isolated perfused rat pancreas. Biochem. Biophys. Res. Commun. 170 (1990) 1223-1228
102. O'Brien T.D., Butler P.C., Westermark P., and Johnson K.H. Islet amyloid polypeptide: A review of its biology and potential roles in the pathogenesis of diabetes mellitus. Vet. Pathol. 30 (1993) 317-332
103. O'Brien T.D., Westermark P., Betsholtz C., and Johnson K.H. Islet amyloid polypeptide: Biology and role in the pathogenesis of islet amyloidosis and diabetes mellitus. In: Shafrir E. (Ed) (1993), Smith Gordon/Nixhimura, UK 117 Biennial review volume: 1992
104. O'Harte F.P.M., AbdelWahab Y.H.A., Conlon J.M., and Flatt P.R. Glycated IAPP shows a reduced inhibitory action on insulin secretion. Biochem. Soc. Trans. 26 (1998) S6
105. Ohagi S., Nishi M., Bell G.I., Ensinck J.W., and Steiner D.F. Sequences of islet amyloid polypeptide precursors of an old world monkey, the pig-tailed macaque (macaca-nemestrina), and the dog (canis-familiaris). Diabetologia 34 (1991) 555-558
106. Ohsawa H., Kanatsuka A., Mizuno Y., Tokuyama Y., Takada K., Mikata A., Makino H., and Yoshida S. Islet amyloid polypeptide-derived amyloid deposition increases along with the duration of type 2 diabetes mellitus. Diabet. Res. Clin. Pract. 15 (1992) 17-21
107. Ohsawa H., Kanatsuka A., Yamaguchi T., Makino H., and Yoshida S. Islet amyloid polypeptide inhibits glucose-stimulated insulin secretion from isolated rat pancreatic islets. Biochem. Biophys. Res. Commun. 160 (1989) 961-967
108. Opie E.L. On the relation of chronic interstitial pancreatitis to the islands of Langerhans and to diabetes mellitus. J. Exp. Med. 5 (1900) 397-428
109. Opie E.L. The relation of diabetes mellitus to lesions of the pancreas: Hyaline degeneration of the islands of Langerhans. J. Exp. Med. 5 (1900) 527-540
110. Panagiotidis G., Salehi A.A., Westermark P., and Lundquist I. Homologous islet amyloid polypeptide: Effects on plasma levels of glucagon, insulin and glucose in the mouse. Diabet. Res. Clin. Pract. 18 (1992) 167-171
111. Pearse A.G.E., Ewen S.W.B., and Polak J.M. The genesis of apudamyloid in endocrine polypeptide tumours: Histochemical distinction from immunamyloid. Virchows Arch. B Cell Pathol. 10 (1972) 93-107
112. Peiró E., Dégano P., Silvestre R.A., and Marco J. Inhibition of insulin release by amylin is not mediated by changes in somatostatin output. Life Sci. 49 (1991) 761-765
113. Percy A.J., Trainor D.A., Rittenhouse J., Phelps J., and Koda J.E. Development of sensitive immunoassays to detect amylin and amylin-like peptides in unextracted plasma. Clin. Chem. 42 (1996) 576-585
114. Pettersson M., and Ahren B. Failure of islet amyloid polypeptide to inhibit basal and glucose-stimulated insulin secretion in model experiments in mice and rats. Acta Physiol. Scand. 138 (1990) 389-394
115. Porte D., Howard C., Westermark P., and Clark A. X-Discussion: Pancreatic islet amyloid polypeptide (IAPP, amylin). In: Shafrir E. (Ed) (1991), Smith-Gordon Limited, London 516-519
116. Rittenhouse J., Chait B.T., Bierle J.R., Janes S.M., Park D.R., Phelps J.L., Fineman M.S., Qin J., and Koda J.E. Heterogeneity of naturally-occurring human amylin due to glycosylation. Diabetes 45 (1996) 234A
117. Roberts A., Leighton B., Todd J.A., Cockburn D., Schofield P.N., Sutton R., Holt S., Boyd Y., Day A.J., Foot E.A., Willis A.C., Reid K.B.M., and Cooper G.J.S. Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus. Proc. Natl. Acad. Sci. USA 86 (1989) 9662-9666
118. Rodriguez-Gallardo J., Silvestre R.A., Salas M., and Marco J. Rat amylin versus human amylin: Effects on insulin secretion in the perfused rat pancreas. Med. Sci. Res. 23 (1995) 569-570
119. Rosenfeld M.G., Mermod J.J., Amara S.G., Swanson L.W., Sawchenko P.E., Rivier J., Vale W.W., and Evans R.M. Production of a novel neuropeptide encoded by the calcitonin gene via tissue-specific RNA processing. Nature 304 (1983) 129-135
120. Sakagashira S., Sanke T., Hanabusa T., Tabata H., Jiko H., Ohagi S., Kumagaye K.Y., Nakajima K., and Nanjo K. A missense mutation of amylin gene (Ser20Gly) in Japanese patients with non-insulin-dependent diabetes mellitus. Program and Abstracts, 10th International Congress of Endocrinology (1996) 979
121. Sakagashira S., Hiddinga H.J., Tateishi K., Sanke T., Hanabusa T., Nanjo K., and Eberhardt N.L. S20g mutant amylin exhibits increased in vitro amyloidogenicity and increased intracellular cytotoxicity compared to wild-type amylin. Am. J. Pathol. 157 (2000) 2101-2109
122. Salas M., Silvestre R.A., Gutiérrez E., Fontels T., Garcia-Hermida O., and Marco J. Potentiation of the insulin response to glucose by an amylin antagonist (8-32 salmon calcitonin). Diabetologia 37 (1994) A116
123. Salas M., Silvestre R.A., Garcia-Hermida O., Fontela T., Rodriguez-Gallardo J., and Marco J. Inhibitory effect of amylin (islet amyloid polypeptide) on insulin response to non-glucose stimuli: Study in perfused rat pancreas. Diabet. Metab. 21 (1995) 269-273
124. Sandler S., and Stridsberg M. Chronic exposure of cultured rat pancreatic islets to elevated concentrations of islet amyloid polypeptide (IAPP) causes a decrease in islet DNA content and medium insulin accumulation. Regul. Pept. 53 (1994) 103-109
125. Sanke T., Bell G.I., Sample C., Rubenstein A.H., and Steiner D.F. An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing. J. Biol. Chem. 263 (1988) 17243-17246
126. Sanke T., Sakagashira S., Hanabusa T., Tabata H., Jiko H., Ohagi S., Nakajima K., and Nanjo K. Significance of a missense mutation (Ser20Gly) of amylin (IAPP) gene in early onset NIDDM in the Japanese population. Diabetes 45 (1996) 228A
127. Silvestre R.A., Peiro E., Dégano P., Iglesias A., Miralles P., and Marco J. Rat amylin inhibits insulin release without affecting glucagon and somatostatin output in the rat pancreas. Diabetologia 33 (1990) A40
128. Silvestre R.A., Peiró E., Dégano P., Miralles P., and Marco J. Inhibitory effect of rat amylin on the insulin responses to glucose and arginine in the perfused rat pancreas. Regul. Pept. 31 (1990) 23-31
129. Silvestre R.A., Dégano P., Salas M., Peiro E., and Marco J. Calcitonin gene-related peptide (CGRP) and amylin inhibition of insulin release is reversed by the 8-37 CGRP fragment. Diabetologia 35 (1992) A29
130. Silvestre R.A., Salas M., Dégaño P., Fontela T., García-Hermida O., and Marco J. Prevention of the inhibitory effect of amylin on GIP-induced insulin release by Pertussis toxin pretreatment. Diabetologia 36 (1993) A136
131. Silvestre R.A., Salas M., Degano P., Peiro E., and Marco J. Reversal of the inhibitory effects of calcitonin gene-related peptide (CGRP) and amylin on insulin secretion by the 8-37 fragment of human CGRP. Biochem. Pharmacol. 45 (1993) 2343-2347
132. Silvestre R.A., Salas M., Garcia-Hermida O., Fontela T., Degano P., and Marco J. Amylin (islet amyloid polypeptide) inhibition of insulin release in the perfused rat pancreas: Implication of the adenylate cyclase/cAMP system. Regul. Pept. 50 (1994) 193-199
133. Silvestre R.A., Salas M., Rodriguez-Gallardo J., Garcia-Hermida O., Fontela T., and Marco J. Effect of (8-32). Salmon calcitonin, an amylin antagonist, on insulin, glucagon and somatostatin release: Study in the perfused pancreas of the rat. Br. J. Pharmacol. 117 (1996) 347-350
134. Silvestre R.A., Rodríguez-Gallardo J., Gutiérrez E., and Marco J. Influence of glucose concentration on the inhibitory effect of amylin on insulin secretion: Study in the perfused rat pancreas. Regul. Pept. 68 (1997) 31-35
135. Smith D.M., and Bloom S.R. Paracrine/autocrine control of the islet and the amylin family. Biochem. Soc. Trans. 23 (1995) 336-340
136. Soeller W.C., Parker J.C., Emeigh-Hart S.G., Kreutter D.K., and Stevenson R.W. Glucose intolerance and late-onset hyperglycemia in A^{vy}/a mice expressing a human islet amyloid polypeptide (huIAPP) transgene. Diabetes 45 (1996) 77A
137. Soeller W.C., Parker J.C., Janson J., Nelson R.T., Carty M.D., Torchia A.J., Orena S.J., Stock J., McNeish J., Stevenson R.W., and Kreutter D.K. Two distinct diabetogenic roles for IAPP revealed by elevated expression of human and rodent homologues in transgenic mice. Diabetes 45 (1996) 161A
138. Stridsberg M., Berne C., Sandler S., Wilander E., and Oberg K. Inhibition of insulin secretion, but normal peripheral insulin sensitivity, in a patient with a malignant endocrine pancreatic tumour producing high amounts of an islet amyloid polypeptide-like molecule. Diabetologia 36 (1993) 843-849
139. Suzuki S., Murakami M., Abe S., Satoh Y., Shintani S., Ishizuka J., Suzuki K., Thompson J.C., and Toyota T. The effects of amylin on insulin secretion from Rin m5F cells and glycogen synthesis and lipogenesis in rat primary cultured hepatocytes. Diabet. Res. Clin. Pract. 15 (1992) 77-84
140. Tedstone A.E., Nezzer T., Hughes S.J., Clark A., and Matthews D.R. The effects of islet amyloid peptide and calcitonin gene-related peptide on insulin secretion in anaesthetised rats and from isolated rat islets. BDA Diab. Med. 6 (1989) A38
141. Tedstone A.E., Nezzer T., Hughes S.J., Clark A., and Matthews D.R. The effect of islet amyloid polypeptide (amylin) and calcitonin gene-related peptide on glucose removal in the anaesthetized rat and on insulin secretion from rat pancreatic islets in vitro. Biosci. Rep. 10 (1990) 339-345
142. Tokuyama Y., Kanatsuka A., Suzuki Y., Yamaguchi T., Taira M., Makino H., and Yoshida S. Islet amyloid polypeptide gene: No evidence of abnormal promoter region in thirty-five type 2 diabetic patients. Diabet. Res. Clin. Pract. 22 (1994) 99-105
143. van Mansfeld A.D.M., Mosselman S., Hoppener J.W.M., Zandberg J., van Teeffelen H.A.A.M., Baas P.D., Lips C.J.M., and Jansz H.S. Islet amyloid polypeptide: Structure and upstream sequence of the IAPP gene in rat and man. Biochim. Biophys. Acta 1087 (1990) 235-240
144. Verchere C.B., DAlessio D.A., Palmiter R.D., Weir G.C., Bonner Weir S., Baskin D.G., and Kahn S.E. Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic beta cell expression of human islet amyloid polypeptide. Proc. Natl. Acad. Sci. USA 93 (1996) 3492-3496
145. Verchere C.B., DAlessio D.A., Wang S., Andrikopoulos S., and Kahn S.E. Transgenic overproduction of islet amyloid polypeptide (amylin) is not sufficient for islet amyloid formation. Horm. Metab. Res. 29 (1997) 311-316
146. Wagoner P.K., Dukes I.D., and Worley III J.F. Amylin inhibition of glucose-induced changes in electrical activity, intracellular calcium and insulin release in mouse beta-cells. Diabetes 41 (1992) 103A
147. Wagoner P.K., Chen C., Worley J.F., Dukes I.D., and Oxford G.S. Amylin modulates ß-cell glucose sensing via effects on stimulus-secretion coupling. Proc. Natl. Acad. Sci. USA 90 (1993) 9145-9149
148. Wang F., Westermark G., Gasslander T., and Permert J. Effect of islet amyloid polypeptide on somatostatin inhibition of insulin secretion from isolated rat pancreatic islets. Regul. Pept. 72 (1997) 61-67
149. Wang Z.-L., Bennet W.M., Ghatei M.A., Byfield P.G.H., Smith D.M., and Bloom S.R. Influence of islet amyloid polypeptide and the 8-37 fragment of islet amyloid polypeptide on insulin release from perifused rat islets. Diabetes 42 (1993) 330-335
150. Weir G.C., and Bonner-Weir S. Insulin secretion in non-insulin-dependent diabetes mellitus. In: LeRoith D., Taylor S.I., and Olefsky J.M. (Eds) (1996), Lippincott-Raven Publishers, Philadelphia 503-508
151. Westermark P. Quantitative studies on amyloid in the islets of Langerhans. Ups. J. Med. Sci. 77 (1972) 91-94
152. Westermark P. Amyloid and polypeptide hormones: What is their interrelationship?. Amyloid Intl. J. Exp. Clin. Invest. 1 (1994) 47-60
153. Westermark P., and Johnson K.H. The pathogenesis of maturity-onset diabetes mellitus: Is there a link to islet amyloid polypeptide?. Bioessays 9 (1988) 30-33
154. Westermark P., and Wilander E. Islet amyloid in Type 2 (non-insulin-dependent) diabetes is related to insulin. Diabetologia 24 (1983) 342-346
155. Westermark P., Wernstedt C., Wilander E., and Sletten K. A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas. Biochem. Biophys. Res. Commun. 140 (1986) 827-831
156. Westermark P., Wernstedt C., O'Brien T.D., Hayden D.W., and Johnson K.H. Islet amyloid in type 2 human diabetes mellitus and adult diabetic cats contains a novel putative polypeptide hormone. Am. J. Pathol. 127 (1987) 414-417
157. Westermark P., Wernstedt C., Wilander E., Hayden D.W., O'Brien T.D., and Johnson K.H. Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc. Natl. Acad. Sci. USA 84 (1987) 3881-3885
158. Westermark P., Johnson K.H., Sletten K., Wilander E., and Wernstedt C. The nature of the amyloid in the Islets of Langerhans: A novel polypeptide hormone?. In: Isobe T., Araki S., Uchino F., Kito S., and Tsubura E. (Eds) (1988), Plenum Press, New York 667-671
159. Westermark P., Engstrom U., Johnson K.H., Westermark G.T., and Betsholtz C. Islet amyloid polypeptide: Pinpointing amino acid residues linked to amyloid fibril formation. Proc. Natl. Acad. Sci. USA 87 (1990) 5036-5040
160. Westermark P., Betsholtz C., Dominguez H.L., O'Brien T.D., and Johnson K.H. Islet amyloid polypeptide in humans and cats. In: Shafrir E. (Ed) (1991), Smith-Gordon Limited, London 499-501
161. Westermark P., Johnson K.H., O'Brien T.D., and Betsholtz C. Islet amyloid polypeptide-A novel controversy in diabetes research. Diabetologia 35 (1992) 297-303
162. Westermark P., Eizirik D.L., Pipeleers D.G., Hellerstrom C., and Andersson A. Rapid deposition of amyloid in human islets transplanted into nude mice. Diabetologia 38 (1995) 543-549
163. Wolffen-Buttel B.H.R., and Van Haeften T.W. Review-non-insulin-dependent diabetes-mellitus-Defects in insulin secretion. Eur. J. Clin. Invest. 23 (1993) 69-79
164. Young A.A., Carlo P., Rink T.J., and Wang M.-W. 8-37hCGRP, an amylin receptor antagonist, enhances the insulin response and perturbs the glucose response to infused arginine in anesthetized rats. Mol. Cell Endocrinol. 84 (1992) R1-R5
165. Young A.A., Gedulin B., Wolfe-Lopez D., Greene H.E., Rink T.J., and Cooper G.J.S. Amylin and insulin in rat soleus muscle: Dose responses for cosecreted noncompetitive antagonists. Am. J. Physiol. 263 (1992) E274-E281
166. Young A.A., Gedulin B., Larson E., and Rink T.J. Evidence from studies using a specific blocker for a metabolic effect of endogenous amylin in vivo. Diabetologia 36 suppl. 1 (1993) A136
167. Young A.A., Gedulin B., Gaeta L.S.L., Prickett K.S., Beaumont K., Larson E., and Rink T.J. Selective amylin antagonist suppresses rise in plasma lactate after intravenous glucose in the rat-Evidence for a metabolic role of endogenous amylin. FEBS Lett. 343 (1994) 237-241
168. Young A.A., Wang M.W., Gedulin B., Rink T.J., Pittner R., and Beaumont K. Diabetogenic effects of salmon calcitonin are attributable to amylin-like activity. Metabolism 44 (1995) 1581-1589
169. Young A.A., Vine W., Gedulin B.R., Pittner R., Janes S., Gaeta L.S.L., Percy A., Moore C.X., Koda J.E., Rink T.J., and Beaumont K. Preclinical pharmacology of pramlintide in the rat: Comparisons with human and rat amylin. Drug Dev. Res. 37 (1996) 231-248