Islet amyloid polypeptide in pancreatic islets from type 2 diabetic subjects

References

• Opie EL. THE RELATION OF DIABETES MELLITUS TO LESIONS OF THE PANCREAS. HYALINE DEGENERATION OF THE ISLANDS OF LANGERHANS. J Exp Med 1901; 5:527 - 40; http://dx.doi.org/10.1084/jem.5.5.527; PMID: 19866956
   PubMedGoogle Scholar
• Ehrlich JC, Ratner IM. Amyloidosis of the islets of Langerhans. A restudy of islet hyalin in diabetic and non-diabetic individuals. Am J Pathol 1961; 38:49 - 59; PMID: 13726023
   PubMed Web of Science ®Google Scholar
• Clark A, Wells CA, Buley ID, Cruickshank JK, Vanhegan RI, Matthews DR, et al. Islet amyloid, increased A-cells, reduced B-cells and exocrine fibrosis: quantitative changes in the pancreas in type 2 diabetes. Diabetes Res 1988; 9:151 - 9; PMID: 3073901
   PubMedGoogle Scholar
• Röcken C, Linke RP, Saeger W. Immunohistology of islet amyloid polypeptide in diabetes mellitus: semi-quantitative studies in a post-mortem series. Virchows Arch A Pathol Anat Histopathol 1992; 421:339 - 44; http://dx.doi.org/10.1007/BF01660981; PMID: 1413495
   PubMedGoogle Scholar
• Westermark P, Wernstedt C, Wilander E, 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 1986; 140:827 - 31; http://dx.doi.org/10.1016/0006-291X(86)90708-4; PMID: 3535798
   PubMed Web of Science ®Google Scholar
• Cooper GJ, Willis AC, Clark A, Tumer RC, Sim RB, Reid KB. Purification and characterization of a peptide from amyloid-rich pancreas of type 2 diabetic pancreas. Proc Natl Acad Sci U S A 1987; 84:8628 - 32; http://dx.doi.org/10.1073/pnas.84.23.8628
   PubMed Web of Science ®Google Scholar
• Kahn SE, Andrikopoulos S, Verchere CBN. Islet amyloid: a long-recognized but underappreciated pathological feature of type 2 diabetes. Diabetes 1999; 48:241 - 53; http://dx.doi.org/10.2337/diabetes.48.2.241; PMID: 10334297
   PubMed Web of Science ®Google Scholar
• Höppener JW, Ahrén B, Lips CJ. Islet amyloid and type 2 diabetes mellitus. N Engl J Med 2000; 343:411 - 9; http://dx.doi.org/10.1056/NEJM200008103430607; PMID: 10933741
   PubMed Web of Science ®Google Scholar
• Kruger DF, Gatcomb PM, Owen SK. Clinical implications of amylin and amylin deficiency. Diabetes Educ 1999; 25:389 - 97, quiz 398; http://dx.doi.org/10.1177/014572179902500310; PMID: 10531859
   PubMed Web of Science ®Google Scholar
• Tomita T. Islet amyloid polypeptide in pancreatic islets from type 1 diabetic subjects. Islets 2011; 3:166 - 74; http://dx.doi.org/10.4161/isl.3.4.15875; PMID: 21633185
   PubMed Web of Science ®Google Scholar
• Weyer C, Maggs DG, Young AA, Kolterman OG. Amylin replacement with pramlintide as an adjunct to insulin therapy in type 1 and type 2 diabetes mellitus: a physiological approach toward improved metabolic control. Curr Pharm Des 2001; 7:1353 - 73; http://dx.doi.org/10.2174/1381612013397357; PMID: 11472273
   PubMed Web of Science ®Google Scholar
• Buse JB, Weyer C, Maggis DC. Amylin replacement with Pramlintide in type 1 and type 2 diabetes: a physiological approach to overcome barriers with insulin therapy. Clin Diabetes 2002; 20:137 - 44; http://dx.doi.org/10.2337/diaclin.20.3.137
   Google Scholar
• Fineman M, Weyer C, Maggs DG, Strobel S, Kolterman OG. The human amylin analog, pramlintide, reduces postprandial hyperglucagonemia in patients with type 2 diabetes mellitus. Horm Metab Res 2002; 34:504 - 8; http://dx.doi.org/10.1055/s-2002-34790; PMID: 12384827
   PubMed Web of Science ®Google Scholar
• Hull RL, Westermark GT, Westermark P, Kahn SE. Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes. J Clin Endocrinol Metab 2004; 89:3629 - 43; http://dx.doi.org/10.1210/jc.2004-0405; PMID: 15292279
   PubMed Web of Science ®Google Scholar
• Lorenzo A, Razzaboni B, Weir GC, Yankner BA. Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus. Nature 1994; 368:756 - 60; http://dx.doi.org/10.1038/368756a0; PMID: 8152488
   PubMed Web of Science ®Google Scholar
• Jaikaran ET, Clark A. Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology. Biochim Biophys Acta 2001; 1537:179 - 203; PMID: 11731221
   PubMed Web of Science ®Google Scholar
• Marzban L, Park K, Verchere CB. Islet amyloid polypeptide and type 2 diabetes. Exp Gerontol 2003; 38:347 - 51; http://dx.doi.org/10.1016/S0531-5565(03)00004-4; PMID: 12670620
   PubMed Web of Science ®Google Scholar
• Hayden MR. Islet amyloid, metabolic syndrome, and the natural progressive history of type 2 diabetes mellitus. JOP 2002; 3:126 - 38; PMID: 12221327
   PubMedGoogle Scholar
• Kloppel G, Lenzen S. Anatomy and physiology of the endocrine pancreas. In: Kloppel, G, Heitz, PU Editors. Pancreatic Pathology. Edinburgh, Churchill-Livingstone: 1984; 133-153.
   Google Scholar
• DeFronzo RA. Pathogenesis of type 2 diabetes mellitus. Med Clin North Am 2004; 88:787 - 835, ix; http://dx.doi.org/10.1016/j.mcna.2004.04.013; PMID: 15308380
   PubMed Web of Science ®Google Scholar
• Tomita T. Immunocytochemical localization of capase-3 in pancreatic islets from type 2 diabetic subjects. Pathology 2010; 42:432 - 7; http://dx.doi.org/10.3109/00313025.2010.493863
   PubMed Web of Science ®Google Scholar
• Clark A, Nilsson MR. Islet amyloid: a complication of islet dysfunction or an aetiological factor in Type 2 diabetes?. Diabetologia 2004; 47:157 - 69; http://dx.doi.org/10.1007/s00125-003-1304-4; PMID: 14722650
   PubMed Web of Science ®Google Scholar
• Tomita T. Amyloidosis of pancreatic islets in primary amyloidosis (AL type). Pathol Int 2005; 55:223 - 7; http://dx.doi.org/10.1111/j.1440-1827.2005.01815.x; PMID: 15826250
   PubMed Web of Science ®Google Scholar
• Mirzabekov TA, Lin MC, Kagan BL. Pore formation by the cytotoxic islet amyloid peptide amylin. J Biol Chem 1996; 271:1988 - 92; http://dx.doi.org/10.1074/jbc.271.4.1988; PMID: 8567648
   PubMed Web of Science ®Google Scholar
• Anguiano M, Nowak RJ, Lansbury PT Jr.. Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes. Biochemistry 2002; 41:11338 - 43; http://dx.doi.org/10.1021/bi020314u; PMID: 12234175
   PubMed Web of Science ®Google Scholar
• Janson J, Ashley RH, Harrison D, McIntyre S, Butler PC. The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. Diabetes 1999; 48:491 - 8; http://dx.doi.org/10.2337/diabetes.48.3.491; PMID: 10078548
   PubMed Web of Science ®Google Scholar
• Engel MFM, Khemtémourian L, Kleijer CC, Meeldijk HJ, Jacobs J, Verkleij AJ, et al. Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane. Proc Natl Acad Sci U S A 2008; 105:6033 - 8; http://dx.doi.org/10.1073/pnas.0708354105; PMID: 18408164
   PubMed Web of Science ®Google Scholar
• Haataja L, Gurlo T, Huang CJ, Butler PC. Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis. Endocr Rev 2008; 29:303 - 16; http://dx.doi.org/10.1210/er.2007-0037; PMID: 18314421
   PubMed Web of Science ®Google Scholar
• Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003; 300:486 - 9; http://dx.doi.org/10.1126/science.1079469; PMID: 12702875
   PubMed Web of Science ®Google Scholar
• Bonner-Weir S, O’Brien TD. Islets in type 2 diabetes: in honor of Dr. Robert C. Turner. Diabetes 2008; 57:2899 - 904; http://dx.doi.org/10.2337/db07-1842; PMID: 18971437
   PubMed Web of Science ®Google Scholar
• Westermark P. Fine structure of islets of Langerhans in insular amyloidosis. Virchows Arch A Pathol Pathol Anat 1973; 359:1 - 18; http://dx.doi.org/10.1007/BF00549079; PMID: 4632997
   PubMedGoogle Scholar
• Woessner JF Jr. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J 1991; 5:2145 - 54; PMID: 1850705
   PubMed Web of Science ®Google Scholar
• Birkedal-Hansen H, Moore WG, Bodden MK, Windsor LJ, Birkedal-Hansen B, DeCarlo A, et al. Matrix metalloproteinases: a review. Crit Rev Oral Biol Med 1993; 4:197 - 250; PMID: 8435466
   PubMedGoogle Scholar
• Stetler-Stevenson WG, Aznavoorian S, Liotta LA. Tumor cell interactions with the extracellular matrix during invasion and metastasis. Annu Rev Cell Biol 1993; 9:541 - 73; http://dx.doi.org/10.1146/annurev.cb.09.110193.002545; PMID: 8280471
   PubMed Web of Science ®Google Scholar
• Nagase H, Woessner JF Jr.. Matrix metalloproteinases. J Biol Chem 1999; 274:21491 - 4; http://dx.doi.org/10.1074/jbc.274.31.21491; PMID: 10419448
   PubMed Web of Science ®Google Scholar
• Visse R, Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res 2003; 92:827 - 39; http://dx.doi.org/10.1161/01.RES.0000070112.80711.3D; PMID: 12730128
   PubMed Web of Science ®Google Scholar
• Perez SE, Cano DA, Dao-Pick T, Rougier JP, Werb Z, Hebrok M. Matrix metalloproteinases 2 and 9 are dispensable for pancreatic islet formation and function in vivo. Diabetes 2005; 54:694 - 701; http://dx.doi.org/10.2337/diabetes.54.3.694; PMID: 15734845
   PubMed Web of Science ®Google Scholar
• Tomita T. Caspase-3 immunocytochemical staining for pancreatic endocrine tumors. Hum Pathol 2009; 40:1050 - 2; http://dx.doi.org/10.1016/j.humpath.2009.02.010; PMID: 19427666
   PubMed Web of Science ®Google Scholar
• Tomita T, Iwata K. Gelatinases and inhibitors of gelatinases in pancreatic islets and islet cell tumors. Mod Pathol 1997; 10:47 - 54; PMID: 9021726
   PubMed Web of Science ®Google Scholar
• Tomita T. New markers for pancreatic islets and islet cell tumors. Pathol Int 2002; 52:425 - 32; http://dx.doi.org/10.1046/j.1440-1827.2002.01368.x; PMID: 12167099
   PubMed Web of Science ®Google Scholar
• Kitamoto T, Ogomori K, Tateishi J, Prusiner SB. Formic acid pretreatment enhances immunostaining of cerebral and systemic amyloids. Lab Invest 1987; 57:230 - 6; PMID: 2441141
   PubMed Web of Science ®Google Scholar
• Law E, Lu S, Kieffer TJ, Warnock GL, Ao Z, Woo M, et al. Differences between amyloid toxicity in alpha and beta cells in human and mouse islets and the role of caspase-3. Diabetologia 2010; 53:1415 - 27; http://dx.doi.org/10.1007/s00125-010-1717-9; PMID: 20369225
   PubMed Web of Science ®Google Scholar
• Cohen GM. Caspases: the executioners of apoptosis. Biochem J 1997; 326:1 - 16; PMID: 9337844
   PubMed Web of Science ®Google Scholar
• Guardado-Mendoza R, Davalli AM, Chavez AO, Hubbard GB, Dick E, Majluf-Cruz A. Pancreatic islet amyloidosis, β-cell apoptosis and α-cell proliferation and determinants of islet cell remodeling in type 2 diabetic baboons. Proc Natl Acad Sci U S A 2009; 106:13992 - 7; http://dx.doi.org/10.1073/pnas.0906471106; PMID: 19666551
   PubMed Web of Science ®Google Scholar
• Hirata H, Takahashi A, Kobayashi S, Yonehara S, Sawai H, Okazaki T, et al. Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis. J Exp Med 1998; 187:587 - 600; http://dx.doi.org/10.1084/jem.187.4.587; PMID: 9463409
   PubMed Web of Science ®Google Scholar
• Gown AM, Willingham MC. Improved detection of apoptotic cells in archival paraffin sections: immunohistochemistry using antibodies to cleaved caspase 3. J Histochem Cytochem 2002; 50:449 - 54; http://dx.doi.org/10.1177/002215540205000401; PMID: 11897797
   PubMed Web of Science ®Google Scholar
• Butler AE, Janson J, Bonner-Weir S, Ritzel RT, Rizza RA, Butler PC. β-cell deficit and increased β-cell apoptosis in humans with type 2 diabetes. Diabetes 2003; 52:102 - 10; http://dx.doi.org/10.2337/diabetes.52.1.102; PMID: 12502499
   PubMed Web of Science ®Google Scholar
• Cnop M, Welsh N, Jonas JC, Jorns A, Lenzen S, Eizirik DL. Mechanisms of pancreatic β cell death in type 1 and type 2 diabetes:many differences, few similarities. Diabetes 2005; 54:(Suppl) S97 - 107; http://dx.doi.org/10.2337/diabetes.54.suppl_2.S97
   PubMed Web of Science ®Google Scholar
• Unger RH, Orci L. The essential role of glucagon in the pathogenesis of diabetes mellitus. Lancet 1975; 1:14 - 6; http://dx.doi.org/10.1016/S0140-6736(75)92375-2; PMID: 46337
   PubMed Web of Science ®Google Scholar
• Stefan Y, Grasso S, Perreltm A, Orci L. The pancreatic polypeptide-rich lobe of the human pancreas; definitive identification of its derivation from the ventral pancreatic primordium. Diabetologia 1982; 23:141 - 2; http://dx.doi.org/10.1007/BF01271177; PMID: 6347784
   PubMed Web of Science ®Google Scholar
• Rahier J, Goebbels RM, Henquin JC. Cellular composition of the human diabetic pancreas. Diabetologia 1983; 24:366 - 71; http://dx.doi.org/10.1007/BF00251826; PMID: 6347784
   PubMed Web of Science ®Google Scholar
• Klöppel G, Löhr M, Habich K, Oberholzer M, Heitz PU. Islet pathology and the pathogenesis of type 1 and type 2 diabetes mellitus revisited. Surv Synth Pathol Res 1985; 4:110 - 25; PMID: 3901180
   PubMedGoogle Scholar