Islet Amyloid Polypeptide—Hen or EGG in Type 2 Diabetes Pathogenesis?

References

• Westermark P. Quantitative studies of amyloid in the islets of Langerhans. Upsala J Med Sci 1972; 77: 91–4
   PubMed Web of Science ®Google Scholar
• Westermark P, Grimelius L. The pancreatic islet cell in insular amyloidosis in human diabetic and non-diabetic adults. Acta Pathol Microbiol Scand A 1973; 81: 291–300
   PubMedGoogle Scholar
• Betsholtz C, Svensson V, Rorsman F, et al. Islet amyloid polypeptide: cDNA cloning and identification of an amyloidogenic region associated with the species-specific occurence of age-related diabetes mellitus. Exp Cell Res 1989; 183: 484–93
   PubMed Web of Science ®Google Scholar
• Westermark P, Johnson K H, O'Brien T D, Betsholtz C. Islet amyloid polypeptide—a novel controversy in diabetes research. Diabetologia 1992; 35: 297–303
   PubMedGoogle Scholar
• Bretherton-Watt D, Bloom S. Is islet amyloid polypeptide the cause of type-2 diabetes?. TEM 1991; 2: 203–6
   PubMedGoogle Scholar
• Leighton B, Cooper G JS. The role of amylin in the insulin resistance of non-insulin-dependent diabetes mellitus. TIBS 1990; 15: 295–9
   PubMedGoogle Scholar
• Sanke T, Bell G I, Sample C, Rubenstein A H, Steiner D F. An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing. J Biol Chem 1988; 263: 17243–6
   PubMed Web of Science ®Google Scholar
• Mosselman S, Hoppener J WM, Lips C JM, Jansz H S. The complete islet amyloid polypeptide precursor is encoded by two exons. FEBS Lett 1989; 247: 154–8
   PubMed Web of Science ®Google Scholar
• Betsholtz C, Christmanson L, Engstrom U, et al. Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species. FEBS Lett 1989; 251: 261–4
   PubMed Web of Science ®Google Scholar
• Nishi M, Chan S J, Nagamatsu S, Bell G I, 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 1989; 86: 5738–42
   PubMed Web of Science ®Google Scholar
• Betsholtz C, Christmanson L, Engström U, et al. The structure of cat islet amyloid polypeptide (IAPP) and identification of amino acid residues of potential significance for islet amyloid formation. Diabetes 1990; 39: 118–22
   PubMed Web of Science ®Google Scholar
• Westermark P, Engstrom U, Johnson K H, Westermark G T, Betsholtz C. Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation. Proc Natl Acad Sci USA 1990; 87: 5036–40
   PubMed Web of Science ®Google Scholar
• Jordan K, Murtaugh M P, O'Brien T D, Westermark P, Betsholtz C, Johnson K H. Canine IAPP cDNA sequence provides important clues regarding diabetogenesis and amyloidogenesis in type 2 diabetes. Biochem Biophys Res Commun 1990; 169: 502–8
   PubMed Web of Science ®Google Scholar
• Nishi M, Bell G I, Steiner D F. Islet amyloid polypeptide (amylin): no evidence of an abnormal precursor sequence in 25 type 2 (non-insulin-dependent) diabetic patients. Diabetologia 1990; 33: 628–30
   PubMed Web of Science ®Google Scholar
• Westermark P, Wernstedt C, Wilander E, Hayden D W, O'Brien T D, 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 1987; 84: 8628–32
   PubMedGoogle Scholar
• Cooper G JS, Willis A C, Clark A, Turner R C, Sim R B, Reid K BM. Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc Natl Acad Sci USA 1987; 84: 8628–32
   PubMed Web of Science ®Google Scholar
• Braas K M, Harakall S A, Quafik L, Eipper B A, May V. Expression of peptidylglycine a-amidating monooxygenase: an in situ hybridization and immunocytochemical study. Endocrinology 1992; 130: 2778–87
   PubMedGoogle Scholar
• Nishi M, Sanke T, Senio S, et al. Human islet amyloid polypeptide gene: complete nucleotide sequence, chromosomal localization, and evolutionary history. Mol Endocrinol 1989; 3: 1775–81
   PubMed Web of Science ®Google Scholar
• Christmanson L, Rorsman F, Stenman G, Westermark P, Betsholtz C. The human islet amyloid polypeptide gene. Organization, chromosomal localization and identification of a promoter region. FEBS Lett 1990; 267: 160–6
   PubMedGoogle Scholar
• Van Mansfeld A DM, Mosselman S, Hoppener J WM. Islet amyloid polypeptide: structure and upstream sequences of the IAPP genes in rat and man. Biochim Biophys Acta 1990; 1087: 235–40
   PubMedGoogle Scholar
• Mosselman S, Höppener J WM, Zandberg J, et al. Islet amyloid polypeptide: identification and chromosomal localization of the human gene. FEBS Lett 1988; 239: 227–32
   PubMed Web of Science ®Google Scholar
• Madsen O, Nielsen J H, Michelsen B, et al. Islet amyloid polypeptide (IAPP/amylin) and insulin expression are controlled differently in primary and transformed islet cells. Mol Endocrinol 1991; 5: 143–8
   PubMedGoogle Scholar
• Ferrier G JM, Pierson A M, Jones P M, Bloom S R, Girgis S I, Legon S. Expression of the rat amylin (IAPP/DAP) gene. J Mol Endocrinol 1989; 3: R1–R4
   PubMed Web of Science ®Google Scholar
• Nakasato M, Asai J, Kangawa K, Matsukura S, Matsuo H. Establishment of radioimmunoassay for human islet amyloid polypeptide and its tissue content and plasma concentration. Biochem Biophys Res Commun 1989; 164: 394–9
   PubMedGoogle Scholar
• Asai J, Nakazato M, Miyazato M, Kangawa K, Matsuo H, Matsukura S. Regional distribution and molecular forms of rat islet amyloid polypeptide. Biochem Biophys Res Commun 1990; 169: 788–95
   PubMed Web of Science ®Google Scholar
• Toshimori H, Narita R, Nakazato M, et al. Islet amyloid polypeptide (IAPP) in the gastrointestinal tract and pancreas of man and rat. Cell Tissue Res 1990; 262: 401–6
   PubMed Web of Science ®Google Scholar
• Lukinius A, Wilander E, Westermark G T, Engstrom U, Westermark P. Colocalization of islet amyloid polypeptide and insulin in the B cell secretory granules of the human pancreatic islets. Diabetologia 1989; 32: 240–4
   PubMed Web of Science ®Google Scholar
• Kanatsuka A, Makino H, Ohsawa H, et al. Secretion of islet amyloid polypeptide in response to glucose. FEBS Lett 1989; 259: 199–201
   PubMed Web of Science ®Google Scholar
• Nakazato M, Miyazato M, Asai J, et al. Islet amyloid polypeptide, a novel pancreatic peptide, is a circulating hormone secreted under glucose stimulation. Biochem Biophys Res Commun 1990; 169: 713–8
   PubMed Web of Science ®Google Scholar
• Hartter E, Svoboda T, Ludvik B, et al. Basal and stimulated plasma levels of pancreatic amylin indiate its co-secretion with insulin in humans. Diabetologia 1991; 34: 52–4
   PubMed Web of Science ®Google Scholar
• Sanker T, Hanabusa T, Nakano Y, et al. Plasma islet amyloid polypeptide (amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients. Diabetologia 1991; 34: 129–32
   PubMedGoogle Scholar
• Mitsukawa T, Takemura J, Asai J, et al. Islet amyloid polypeptide response to glucose, insulin and somatostatin analogue administration. Diabetes 1990; 39: 639–42
   PubMed Web of Science ®Google Scholar
• Fehmann H C, Weber V, Göke R, Göke B, Arnold R. Co-secretion of amylin and insulin from isolated rat pancreas. FEBS Lett 1990; 262: 279–81
   PubMed Web of Science ®Google Scholar
• Inoue K, Hisatomi A, Umeda F, Nawata H. Amylin release from perfused rat pancreas in response to glucose and arginine. Diabetes Res Clin Pract 1990; 10: 189–92
   PubMedGoogle Scholar
• Kahn S E, D'Alessio D A, Schwartz M W, et al. Evidence of co-secretion of islet amyloid polypeptide and insulin by B-cells. Diabetes 1990; 39: 634–8
   PubMed Web of Science ®Google Scholar
• Butler P C, Chou J, Carter W B, et al. Effects of meal ingestion on plasma amylin concentration in NIDDM and non-diabetic humans. Diabetes 1990; 39: 752–6
   PubMed Web of Science ®Google Scholar
• van Jaarsveld B C, Hackeng W HL, Niewenhuis M G, Erkelens D W, Geerdink R A, Lips C JM. Islet amyloid polypeptide in human plasma. Lancet 1990; 1: 60
   Google Scholar
• Gill A M, Yen T T. Effects of ciglitazone on endogeneous plasma islet amyloid polypeptide and insulin sensitivity in obese-diabetic viable yellow mice. Life Sci 1991; 48: 703–10
   PubMedGoogle Scholar
• Jamal H, Bretherton-Watt D, Suda K, Ghatei M A, Blook S R. Islet amyloid polypeptide-like immunoreactivity (amylin) in rats treated with dexamethasone and streptozo-tocin. J Endocrinol 1990; 126: 425–9
   PubMedGoogle Scholar
• Tokuyama Y, Kanatsuka A, Ohsawa H, et al. Hypersecretion of islet amyloid polypeptide from pancreatic islets of ventromedial hypothalamic-lesioned rats and obese Zucker rats. Endocrinology 1991; 128: 2739–41
   PubMedGoogle Scholar
• O'Brien T D, Westermark P, Johnson K H. Islet amyloid polypeptide and insulin secretion from isolated perfused pancreas of fed, fasted, glucose-treated and dexamethasone-treated rats. Diabetes 1991; 40: 1701–6
   PubMed Web of Science ®Google Scholar
• Bretherton-Watt D, Ghatei M A, Bloom S R, et al. Altered islet amyloid polypeptide (amylin) gene expression in rat models of diabetes. Diabetologia 1989; 32: 881–3
   PubMed Web of Science ®Google Scholar
• Ogawa A, Harris V, McCorkie S W, Unger R H, Luskey K L. Amylin secretion from the rat pancreas and its selective loss after streptozotocin treatment. J Clin Invest 1990; 85: 973–6
   PubMed Web of Science ®Google Scholar
• Ohsawa H, Kanatsuka A, Yamaguchi T, Makino H, Yoshida S. Islet amyloid polypeptide inhibits glucose-stimulated insulin secretion from isolated rat pancreatic islets. Biochem Biophys Res Commun 1989; 160: 961–7
   PubMed Web of Science ®Google Scholar
• Silvestre R A, Peiro E, D'gano P, Miralles P, Marco J. Inhibitory effect of rat amylin on the insulin responses to glucose and arginine in the perfused rat pancreas. Regul Pept 1990; 31: 23–31
   PubMedGoogle Scholar
• O'Brien T D, Westermark P, Johnson K H. Islet amyloid polypeptide (IAPP) does not inhibit glucose-stimulated insulin secretion from isolated perfused rat pancreas. Biochem Biophys Res Commun 1990; 170: 1223–8
   PubMed Web of Science ®Google Scholar
• Nagamatsu S, Carrol R, Grodsky G M, Steiner D F. Lack of islet amyloid polypeptide regulation of insulin biosynthesis or secretion in normal rat islets. Diabetes 1990; 39: 871–4
   PubMed Web of Science ®Google Scholar
• Fehmann H-C, Weber V, Göke R, Göke B, Eissele R, Arnold R. Islet amyloid polypeptide (IAPP: amylin) influences the endocrine but not the exocrine pancreas. Biochem Biophys Res Commun 1990; 167: 1102–8
   PubMed Web of Science ®Google Scholar
• Ghatei M A, Datta H K, Zaidi M, et al. Amylin and amylin-amide lack and acute effect on blood glucose and insulin. J Endocrinol 1990; 124: R9–R11
   PubMedGoogle Scholar
• Pettersson M, Ahren B. Insulin and glucagon secretion in rats: effects of calcitonin gene-related peptide. Regul Pept 1988; 23: 37–50
   PubMedGoogle Scholar
• Morishita T, Yamaguchi A, Fujita T, Chiba T. Activation of adenylate cyclase by islet amyloid polypetide with COOH-terminal amide via calcitonin gene-related peptide receptors on rat liver plasma membranes. Diabetes 1990; 39: 875–7
   PubMed Web of Science ®Google Scholar
• Leighton B, Cooper G JS. Pancreatic amylin and calcitonin gene-related peptide cause resistance to insulin in skeletal muscle in vitro. Nature 1988; 335: 632–5
   PubMed Web of Science ®Google Scholar
• Johnson K H, O'Brien T D, Jordan K, Betsholtz C, Westermark P. The putative hormone islet amyloid polypeptide (IAPP) induces impaired glucose tolerance in cats. Biochem Biophys Res Commun 1990; 167: 507–13
   PubMed Web of Science ®Google Scholar
• Sowa R, Sanke T, Hirayama J, et al. Islet amyloid polypeptide amide causes peripheral insulin resistance in vivo in dogs. Diabetologia 1990; 33: 118–20
   PubMed Web of Science ®Google Scholar
• Frontoni S, Bong Choi S, Banduch D, Rossetti L. In vivo insulin resistance induced by amylin primarily through inhibition of insulin-stimulated glycogen synthesis in skeletal muscle. Diabetes 1991; 40: 568–73
   PubMed Web of Science ®Google Scholar
• Leighton B, Foot E. The effects on amylin on carbohydrate metabolism in skeletal muscle in vitro and in vivo. Biochem J 1990; 269: 19–23
   PubMedGoogle Scholar
• Zierath J, Galuska D, Engström Å, et al. Synthetic human islet amyloid polypeptide inhibits insulin and phorbol ester-stimulated glucose transport in in vitro incubated human muscle strips. Diabetologia 1992; 35: 26–31
   PubMed Web of Science ®Google Scholar
• Deems R O, Deacon R W, Young D A. Amylin activates glycogen phosphorylase and inactivates glycogen synthase via a cAMP-independent mechanism. Biochem Biophys Res Commun 1991; 174: 716–20
   PubMedGoogle Scholar
• Young A A, Mott D M, Stone K, Cooper G JS. Amylin activates glycogen phosphorylase in the isolated soleus muscle of the rat. FEBS Lett 1991; 281: 149–51
   PubMed Web of Science ®Google Scholar
• Datta H K, Zaidi M, Wimalawansa S J, et al. In vivo and in vitro effects of amylin and amylin-amide on calcium metabolism in the rat and rabbit. Biochem Biophys Res Commun 1989; 162: 876–81
   PubMed Web of Science ®Google Scholar
• Morley J E, Flood J F. Amylin decreases food intake in mice. Peptides 1991; 12: 865–7
   PubMed Web of Science ®Google Scholar
• Balasubramaniam A, Renugopalakrishnan V, Stein M, Fisher J E, Chance W T. Syntheses, structures and anorectic effects of human and rat amylin. Peptides 1991; 12: 919–23
   PubMedGoogle Scholar
• Chance W T, Balasubramaniam A, Zhang A, Wimalawamsa S J, Fisher J E. Anorexia following the intrahypothalamic administration of amylin. Brain Res 1991; 539: 352–5
   PubMed Web of Science ®Google Scholar
• Stephens T W, Heath W F, Hermeling R N. Presence of liver CGRP/amylin receptors in only nonparenchymal cells and absence of direct regulation of rat liver glucose metabolism by CGRP/amylin. Diabetes 1991; 40: 395–400
   PubMedGoogle Scholar