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Volumn 38, Issue 5-6, 2006, Pages 726-736

Role of islet amyloid in type 2 diabetes mellitus

Author keywords

Cell failure; Insulin deficiency; Islet amyloid; Islet amyloid polypeptide; Type 2 diabetes mellitus

Indexed keywords

2,4 THIAZOLIDINEDIONE DERIVATIVE; AMYLIN; AMYLOID; METFORMIN; POLYPEPTIDE; ROSIGLITAZONE;

EID: 33644834054     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2005.12.009     Document Type: Review
Times cited : (118)

References (96)
  • 1
    • 18644376240 scopus 로고    scopus 로고
    • Type 2 diabetes, insulin secretion and beta-cell mass
    • B. Ahrén Type 2 diabetes, insulin secretion and beta-cell mass Current Molecular Medicine 5 2005 275 286
    • (2005) Current Molecular Medicine , vol.5 , pp. 275-286
    • Ahrén, B.1
  • 2
    • 0042703654 scopus 로고    scopus 로고
    • Amyloidogenesis: Historical and modern observations point to heparin sulfate proteoglycans as a major culprit
    • J.B. Ancsin Amyloidogenesis: Historical and modern observations point to heparin sulfate proteoglycans as a major culprit Amyloid 10 2003 67 79
    • (2003) Amyloid , vol.10 , pp. 67-79
    • Ancsin, J.B.1
  • 3
    • 17844373857 scopus 로고    scopus 로고
    • Genetics of type 2 diabetes
    • I. Barroso Genetics of type 2 diabetes Diabetic Medicine 22 2005 517 535
    • (2005) Diabetic Medicine , vol.22 , pp. 517-535
    • Barroso, I.1
  • 4
    • 0024400674 scopus 로고
    • Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains difference in islet amyloid formation between species
    • C. Betsholtz, L. Christmansson, U. Engstrom, F. Rorsman, V. Svensson, and K.H. Johnson Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains difference in islet amyloid formation between species FEBS Letters 251 1989 261 264
    • (1989) FEBS Letters , vol.251 , pp. 261-264
    • Betsholtz, C.1    Christmansson, L.2    Engstrom, U.3    Rorsman, F.4    Svensson, V.5    Johnson, K.H.6
  • 5
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • D.R. Booth, M. Sunde, V. Bellotti, C.V. Robinson, W.L. Hutchinson, and P.E. Fraser Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis Nature 385 1997 787 793
    • (1997) Nature , vol.385 , pp. 787-793
    • Booth, D.R.1    Sunde, M.2    Bellotti, V.3    Robinson, C.V.4    Hutchinson, W.L.5    Fraser, P.E.6
  • 6
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • M. Bucciantini, E. Giannoni, F. Chiti, F. Baroni, L. Formigli, and J. Zurdo Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases Nature 416 2002 507 511
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5    Zurdo, J.6
  • 8
    • 2542581025 scopus 로고    scopus 로고
    • Diabetes due to a progressive defect in β-cell mass in rats transgenic for human islet amyloid polypeptide (HIP rat)
    • A.E. Butler, J. Jang, T. Gurlo, M.D. Carty, W.C. Soeller, and P.C. Butler Diabetes due to a progressive defect in β-cell mass in rats transgenic for human islet amyloid polypeptide (HIP rat) Diabetes 53 2004 1509 1516
    • (2004) Diabetes , vol.53 , pp. 1509-1516
    • Butler, A.E.1    Jang, J.2    Gurlo, T.3    Carty, M.D.4    Soeller, W.C.5    Butler, P.C.6
  • 9
    • 0037219411 scopus 로고    scopus 로고
    • Beta-cell deficit and increased beta-cell apoptosis in humans with type 2 diabetes
    • A.E. Butler, J. Janson, S. Bonner-Weir, R. Ritzel, R.A. Rizza, and P.C. Butler Beta-cell deficit and increased beta-cell apoptosis in humans with type 2 diabetes Diabetes 52 2003 102 110
    • (2003) Diabetes , vol.52 , pp. 102-110
    • Butler, A.E.1    Janson, J.2    Bonner-Weir, S.3    Ritzel, R.4    Rizza, R.A.5    Butler, P.C.6
  • 10
    • 0042822112 scopus 로고    scopus 로고
    • Increased β-cell apoptosis prevents adaptive increase in β-cell mass in mouse model of type 2 diabetes. Evidence for role of islet amyloid formation rather than direct action of amyloid
    • A.E. Butler, J. Janson, W.C. Soeller, and P.C. Butler Increased β-cell apoptosis prevents adaptive increase in β-cell mass in mouse model of type 2 diabetes. Evidence for role of islet amyloid formation rather than direct action of amyloid Diabetes 52 2003 2304 2314
    • (2003) Diabetes , vol.52 , pp. 2304-2314
    • Butler, A.E.1    Janson, J.2    Soeller, W.C.3    Butler, P.C.4
  • 11
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • B. Caughey, and P.T. Lansbury Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders Annual Reviews in Neurosciences 26 2003 267 298
    • (2003) Annual Reviews in Neurosciences , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 12
    • 11244311563 scopus 로고    scopus 로고
    • The regulation of amylin and insulin gene expression and secretion
    • M.W. Cluck, C.Y. Chan, and T.E. Adrian The regulation of amylin and insulin gene expression and secretion Pancreas 30 2005 1 14
    • (2005) Pancreas , vol.30 , pp. 1-14
    • Cluck, M.W.1    Chan, C.Y.2    Adrian, T.E.3
  • 13
    • 33644749322 scopus 로고    scopus 로고
    • Mechanisms of pancreatic beta-cell death in type 1 and type 2 diabetes: Many differences, few similarities
    • M. Cnop, N. Welsh, J.C. Jonas, A. Jorns, S. Lenzen, and D.L. Eizirik Mechanisms of pancreatic beta-cell death in type 1 and type 2 diabetes: Many differences, few similarities Diabetes 54 Suppl. 2 2005 S97 S107
    • (2005) Diabetes , vol.54 , Issue.2 SUPPL.
    • Cnop, M.1    Welsh, N.2    Jonas, J.C.3    Jorns, A.4    Lenzen, S.5    Eizirik, D.L.6
  • 15
    • 0037669866 scopus 로고    scopus 로고
    • Impaired glucose tolerance: Is there a case for pharmacologic intervention?
    • A. Costa, I. Conget, and R. Gomis Impaired glucose tolerance: Is there a case for pharmacologic intervention? Treatments in Endocrinology 1 2002 205 210
    • (2002) Treatments in Endocrinology , vol.1 , pp. 205-210
    • Costa, A.1    Conget, I.2    Gomis, R.3
  • 16
    • 0027151935 scopus 로고
    • Diabetes mellitus in Macaca mulatta monkeys is characterised by islet amyloidosis and reduction in beta-cell population
    • E.J. De Koning, N.L. Bodkin, B.C. Hansen, and A. Clark Diabetes mellitus in Macaca mulatta monkeys is characterised by islet amyloidosis and reduction in beta-cell population Diabetologia 36 1993 378 384
    • (1993) Diabetologia , vol.36 , pp. 378-384
    • De Koning, E.J.1    Bodkin, N.L.2    Hansen, B.C.3    Clark, A.4
  • 18
    • 0026602931 scopus 로고
    • The insulin and islet amyloid polypeptide genes contain similar cell-specific promoter elements that bind identical beta-cell nuclear complexes
    • M.S. German, L.G. Moss, J. Wang, and W.J. Rutter The insulin and islet amyloid polypeptide genes contain similar cell-specific promoter elements that bind identical beta-cell nuclear complexes Molecular and Cellular Biology 12 1992 1777 1788
    • (1992) Molecular and Cellular Biology , vol.12 , pp. 1777-1788
    • German, M.S.1    Moss, L.G.2    Wang, J.3    Rutter, W.J.4
  • 19
    • 0030682237 scopus 로고    scopus 로고
    • Amyloidosis: A review of recent diagnostic and therapeutic developments
    • J.D. Gillmore, P.N. Hawkins, and M.B. Pepys Amyloidosis: A review of recent diagnostic and therapeutic developments British Journal of Haematology 99 1997 245 256
    • (1997) British Journal of Haematology , vol.99 , pp. 245-256
    • Gillmore, J.D.1    Hawkins, P.N.2    Pepys, M.B.3
  • 20
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidosis: The β-fibrilloses
    • G.G. Glenner Amyloid deposits and amyloidosis: The β-fibrilloses New England Journal of Medicine 302 1980 1283 1292
    • (1980) New England Journal of Medicine , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 21
    • 0346057932 scopus 로고    scopus 로고
    • Increasing the amphiphilicity of an amyloidogenic peptide changes the beta-sheet structure in the fibrils from antiparallel to parallel
    • D.J. Gordon, J.J. Balbach, R. Tycko, and S.C. Meredith Increasing the amphiphilicity of an amyloidogenic peptide changes the beta-sheet structure in the fibrils from antiparallel to parallel Biophysical Journal 86 2004 428 434
    • (2004) Biophysical Journal , vol.86 , pp. 428-434
    • Gordon, D.J.1    Balbach, J.J.2    Tycko, R.3    Meredith, S.C.4
  • 22
    • 0030882286 scopus 로고    scopus 로고
    • Hyperamylinemia is associated with hyperinsulinemia in the glucose-tolerant, insulin-resistant offspring of two Mexican-American non-insulin-dependent diabetic parents
    • G. Gulli, L. Rossetti, and R.A. DeFronzo Hyperamylinemia is associated with hyperinsulinemia in the glucose-tolerant, insulin-resistant offspring of two Mexican-American non-insulin-dependent diabetic parents Metabolism 46 1997 1157 1161
    • (1997) Metabolism , vol.46 , pp. 1157-1161
    • Gulli, G.1    Rossetti, L.2    Defronzo, R.A.3
  • 23
    • 0033891391 scopus 로고    scopus 로고
    • Processing of synthetic pro-islet amyloid polypeptide (proIAPP) 'amylin' by recombinant prohormone convertase enzymes, PC2 and PC3, in vitro
    • C.E. Higham, R.L. Hull, L. Lawrie, K.I. Shennan, J.F. Morris, and N.P. Birch Processing of synthetic pro-islet amyloid polypeptide (proIAPP) 'amylin' by recombinant prohormone convertase enzymes, PC2 and PC3, in vitro European Journal of Biochemistry 267 2000 4998 5004
    • (2000) European Journal of Biochemistry , vol.267 , pp. 4998-5004
    • Higham, C.E.1    Hull, R.L.2    Lawrie, L.3    Shennan, K.I.4    Morris, J.F.5    Birch, N.P.6
  • 28
    • 0141780910 scopus 로고    scopus 로고
    • Extensive islet amyloid formation is induced by development of type II diabetes mellitus and contributes to its progression: Pathogenesis of diabetes in a transgenic mouse model
    • J.W.M. Höppener, C. Oosterwijk, M.G. Nieuwenhuis, G. Posthuma, J.H.H. Thijssen, and Th.M. Vroom Extensive islet amyloid formation is induced by development of type II diabetes mellitus and contributes to its progression: Pathogenesis of diabetes in a transgenic mouse model Diabetologia 42 1999 427 434
    • (1999) Diabetologia , vol.42 , pp. 427-434
    • Höppener, J.W.M.1    Oosterwijk, C.2    Nieuwenhuis, M.G.3    Posthuma, G.4    Thijssen, J.H.H.5    Vroom, Th.M.6
  • 30
    • 0027451036 scopus 로고
    • Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: Lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycemia or hyperinsulinemia
    • J.W.M. Höppener, J.S. Verbeek, E.J.P. De Koning, C. Oosterwijk, K.L. Van Hulst, and H.J. Visser-Vernooy Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: Lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycemia or hyperinsulinemia Diabetologia 36 1993 1258 1265
    • (1993) Diabetologia , vol.36 , pp. 1258-1265
    • Höppener, J.W.M.1    Verbeek, J.S.2    De Koning, E.J.P.3    Oosterwijk, C.4    Van Hulst, K.L.5    Visser-Vernooy, H.J.6
  • 31
    • 0037315790 scopus 로고    scopus 로고
    • Increased dietary fat promotes islet amyloid formation and beta-cell secretory dysfunction in a transgenic mouse model of islet amyloid
    • R.L. Hull, S. Andrikopoulos, C.B. Verchere, J. Vidal, F. Wang, and M. Cnop 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
    • (2003) Diabetes , vol.52 , pp. 372-379
    • Hull, R.L.1    Andrikopoulos, S.2    Verchere, C.B.3    Vidal, J.4    Wang, F.5    Cnop, M.6
  • 32
    • 21344471091 scopus 로고    scopus 로고
    • Long-term treatment with rosiglitazone and metformin reduces the extent of, but does not prevent, islet amyloid deposition in mice expressing the gene for human islet amyloid polypeptide
    • R.L. Hull, Z.P. Shen, M.R. Watts, K. Kodama, D.B. Carr, and K.M. Utzschneider Long-term treatment with rosiglitazone and metformin reduces the extent of, but does not prevent, islet amyloid deposition in mice expressing the gene for human islet amyloid polypeptide Diabetes 54 2005 2235 2244
    • (2005) Diabetes , vol.54 , pp. 2235-2244
    • Hull, R.L.1    Shen, Z.P.2    Watts, M.R.3    Kodama, K.4    Carr, D.B.5    Utzschneider, K.M.6
  • 33
    • 0034684963 scopus 로고    scopus 로고
    • Fibrillar islet amyloid polypeptide differentially affects oxidative mechanisms and lipoprotein uptake in correlation with cytotoxicity in two insulin-producing cell lines
    • S. Janciauskiene, and B. Ahrén Fibrillar islet amyloid polypeptide differentially affects oxidative mechanisms and lipoprotein uptake in correlation with cytotoxicity in two insulin-producing cell lines Biochemical and Biophysical Research Communications 267 2000 619 625
    • (2000) Biochemical and Biophysical Research Communications , vol.267 , pp. 619-625
    • Janciauskiene, S.1    Ahrén, B.2
  • 34
    • 0033048453 scopus 로고    scopus 로고
    • The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles
    • J. Janson, R.H. Ashley, D. Harrison, S. McIntyre, and P.C. Butler The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles Diabetes 48 1999 491 498
    • (1999) Diabetes , vol.48 , pp. 491-498
    • Janson, J.1    Ashley, R.H.2    Harrison, D.3    McIntyre, S.4    Butler, P.C.5
  • 36
    • 0034700471 scopus 로고    scopus 로고
    • Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
    • C. Janus, J. Pearson, J.A. McLaurin, P.M. Mathews, Y. Jiang, and S.D. Schmidt Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease Nature 408 2000 979 982
    • (2000) Nature , vol.408 , pp. 979-982
    • Janus, C.1    Pearson, J.2    McLaurin, J.A.3    Mathews, P.M.4    Jiang, Y.5    Schmidt, S.D.6
  • 37
    • 9144267018 scopus 로고    scopus 로고
    • Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling
    • S.A. Jayasinghe, and R. Langen Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling Journal of Biological Chemistry 279 2004 48420 48425
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 48420-48425
    • Jayasinghe, S.A.1    Langen, R.2
  • 39
    • 0032489358 scopus 로고    scopus 로고
    • Type 2 diabetes: When insulin secretion fails to compensate for insulin resistance
    • B.B. Kahn Type 2 diabetes: When insulin secretion fails to compensate for insulin resistance Cell 92 1998 593 596
    • (1998) Cell , vol.92 , pp. 593-596
    • Kahn, B.B.1
  • 41
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • R. Kayed, E. Head, J.L. Thompson, T.M. McIntyre, S.C. Milton, and C.W. Cotman Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300 2003 486 489
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntyre, T.M.4    Milton, S.C.5    Cotman, C.W.6
  • 42
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • R. Kayed, Y. Sokolov, B. Edmonds, T.M. McIntyre, S.C. Milton, and J.E. Hall Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases Journal of Biological Chemistry 279 2004 46363 46366
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntyre, T.M.4    Milton, S.C.5    Hall, J.E.6
  • 45
    • 0029816099 scopus 로고    scopus 로고
    • Failure to adequately adapt reduced insulin sensitivity with increased insulin secretion in women with impaired glucose tolerance
    • H. Larsson, and B. Ahrén Failure to adequately adapt reduced insulin sensitivity with increased insulin secretion in women with impaired glucose tolerance Diabetologia 9 1996 1099 1107
    • (1996) Diabetologia , vol.9 , pp. 1099-1107
    • Larsson, H.1    Ahrén, B.2
  • 47
    • 12444334643 scopus 로고    scopus 로고
    • Lipotoxicity, an imbalance between lipogenesis de novo and fatty acid oxidation
    • C. Lelliot, and A.J. Vidal-Puig Lipotoxicity, an imbalance between lipogenesis de novo and fatty acid oxidation International Journal of Obesity 28 Suppl. 4 2004 S22 S28
    • (2004) International Journal of Obesity , vol.28 , Issue.4 SUPPL.
    • Lelliot, C.1    Vidal-Puig, A.J.2
  • 49
    • 0028303844 scopus 로고
    • Pancreatic islet cell toxicity of amylin associated with type 2 diabetes mellitus
    • A. Lorenzo, B. Razzabon, G.C. Weir, and B.A. Yankner Pancreatic islet cell toxicity of amylin associated with type 2 diabetes mellitus Nature 368 1994 756 760
    • (1994) Nature , vol.368 , pp. 756-760
    • Lorenzo, A.1    Razzabon, B.2    Weir, G.C.3    Yankner, B.A.4
  • 51
    • 23744503963 scopus 로고    scopus 로고
    • Processing of pro-islet amyloid polypeptide in the constitutive and regulated secretory pathways of beta cells
    • L. Marzban, G. Trigo-Gonzalez, and C.B. Verchere Processing of pro-islet amyloid polypeptide in the constitutive and regulated secretory pathways of beta cells Molecular Endocrinology 19 2005 2154 2163
    • (2005) Molecular Endocrinology , vol.19 , pp. 2154-2163
    • Marzban, L.1    Trigo-Gonzalez, G.2    Verchere, C.B.3
  • 52
    • 0346099381 scopus 로고    scopus 로고
    • Role of beta-cell prohormone convertase (PC) 1/3 in processing of pro-islet amyloid polypeptide
    • L. Marzban, G. Trigo-Gonzalez, X. Zhu, C.J. Rhodes, P.A. Halban, and D.F. Steiner Role of beta-cell prohormone convertase (PC) 1/3 in processing of pro-islet amyloid polypeptide Diabetes 53 2004 141 148
    • (2004) Diabetes , vol.53 , pp. 141-148
    • Marzban, L.1    Trigo-Gonzalez, G.2    Zhu, X.3    Rhodes, C.J.4    Halban, P.A.5    Steiner, D.F.6
  • 54
    • 84984755327 scopus 로고    scopus 로고
    • Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease
    • D. Morgan, D.M. Diamond, P.E. Gottschall, K.E. Ugen, C. Dickey, and J. Hardy Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease Nature 408 2000 982 985
    • (2000) Nature , vol.408 , pp. 982-985
    • Morgan, D.1    Diamond, D.M.2    Gottschall, P.E.3    Ugen, K.E.4    Dickey, C.5    Hardy, J.6
  • 56
    • 0031471130 scopus 로고    scopus 로고
    • Long-term correction of obesity and diabetes in genetically obese mice by a single intramuscular injection of recombinant adeno-associated virus encoding mouse leptin
    • J.E. Murphy, S. Zhou, K. Giese, L.T. Williams, J.A. Escobedo, and V.J. Dwarki Long-term correction of obesity and diabetes in genetically obese mice by a single intramuscular injection of recombinant adeno-associated virus encoding mouse leptin Proceedings of the National Academy of Sciences USA 94 1997 13921 13926
    • (1997) Proceedings of the National Academy of Sciences USA , vol.94 , pp. 13921-13926
    • Murphy, J.E.1    Zhou, S.2    Giese, K.3    Williams, L.T.4    Escobedo, J.A.5    Dwarki, V.J.6
  • 57
    • 0024427284 scopus 로고
    • Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone
    • M. Nishi, S.J. Chan, S. Nagamatsu, G.I. Bell, and D.F. Steiner Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone Proceedings of the National Academy of Sciences USA 86 1989 5738 5742
    • (1989) Proceedings of the National Academy of Sciences USA , vol.86 , pp. 5738-5742
    • Nishi, M.1    Chan, S.J.2    Nagamatsu, S.3    Bell, G.I.4    Steiner, D.F.5
  • 59
    • 0030229085 scopus 로고    scopus 로고
    • Islet amyloid and islet amyloid polypeptide in cynomolgus macaques (Macaca fascicularis): An animal model of human non-insulin-dependent diabetes mellitus
    • T.D. O'Brien, J.D. Wagner, K.N. Litwak, C.S. Carlson, W.T. Cefalu, and K. Jordan Islet amyloid and islet amyloid polypeptide in cynomolgus macaques (Macaca fascicularis): An animal model of human non-insulin-dependent diabetes mellitus Veterinary Pathology 33 1996 479 485
    • (1996) Veterinary Pathology , vol.33 , pp. 479-485
    • O'Brien, T.D.1    Wagner, J.D.2    Litwak, K.N.3    Carlson, C.S.4    Cefalu, W.T.5    Jordan, K.6
  • 60
    • 0025425551 scopus 로고
    • Islet amyloid polypeptide and calcitonin gene-related peptide immunoreactivity in amyloid and tumor cells of canine pancreatic endocrine tumors
    • T.D. O'Brien, P. Westermark, and K.H. Johnson Islet amyloid polypeptide and calcitonin gene-related peptide immunoreactivity in amyloid and tumor cells of canine pancreatic endocrine tumors Veterinary Pathology 27 1990 194 198
    • (1990) Veterinary Pathology , vol.27 , pp. 194-198
    • O'Brien, T.D.1    Westermark, P.2    Johnson, K.H.3
  • 61
    • 85025386842 scopus 로고
    • The relation of diabetes mellitus to lesions of the pancreas. Hyaline degeneration of the islands of langerhans
    • E.L. Opie The relation of diabetes mellitus to lesions of the pancreas. Hyaline degeneration of the islands of langerhans Journal of Experimental Medicine 5 1901 527 540
    • (1901) Journal of Experimental Medicine , vol.5 , pp. 527-540
    • Opie, E.L.1
  • 63
    • 0035907265 scopus 로고    scopus 로고
    • Identification of a heparin binding domain in the N-terminal cleavage site of pro-islet amyloid polypeptide. Implications for islet amyloid formation
    • K. Park, and C.B. Verchere Identification of a heparin binding domain in the N-terminal cleavage site of pro-islet amyloid polypeptide. Implications for islet amyloid formation Journal of Biological Chemistry 276 2001 16611 16616
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 16611-16616
    • Park, K.1    Verchere, C.B.2
  • 64
    • 21344470854 scopus 로고    scopus 로고
    • Aberrant processing of human proislet amyloid polypeptide results in increased amyloid formation
    • J.F. Paulsson, and G.T. Westermark Aberrant processing of human proislet amyloid polypeptide results in increased amyloid formation Diabetes 54 2005 2117 2125
    • (2005) Diabetes , vol.54 , pp. 2117-2125
    • Paulsson, J.F.1    Westermark, G.T.2
  • 65
    • 0037118028 scopus 로고    scopus 로고
    • Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis
    • M.B. Pepys, J. Herbert, W.L. Hutchinson, G.A. Tennent, H.J. Lachmann, and J.R. Gallimore Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis Nature 417 2002 254 259
    • (2002) Nature , vol.417 , pp. 254-259
    • Pepys, M.B.1    Herbert, J.2    Hutchinson, W.L.3    Tennent, G.A.4    Lachmann, H.J.5    Gallimore, J.R.6
  • 66
    • 0036896505 scopus 로고    scopus 로고
    • Malonyl-CoA signaling, lipid partitioning, and glucolipotoxicity: Role in beta-cell adaptation and failure in the etiology of diabetes
    • M. Prentki, E. Joly, W. El-Assaad, and R. Roduit Malonyl-CoA signaling, lipid partitioning, and glucolipotoxicity: Role in beta-cell adaptation and failure in the etiology of diabetes Diabetes 51 Suppl. 3 2002 S405 S413
    • (2002) Diabetes , vol.51 , Issue.3 SUPPL.
    • Prentki, M.1    Joly, E.2    El-Assaad, W.3    Roduit, R.4
  • 67
    • 0033200446 scopus 로고    scopus 로고
    • Current understanding of feline diabetes. Part 1. Pathogenesis
    • J. Rand Current understanding of feline diabetes. Part 1. Pathogenesis Journal of Feline Medicine and Surgery 1 1999 143 153
    • (1999) Journal of Feline Medicine and Surgery , vol.1 , pp. 143-153
    • Rand, J.1
  • 68
    • 12344323484 scopus 로고    scopus 로고
    • Type 2 diabetes - A matter of β-cell life and death
    • C.J. Rhodes Type 2 diabetes - a matter of β-cell life and death Science 307 2005 380 384
    • (2005) Science , vol.307 , pp. 380-384
    • Rhodes, C.J.1
  • 69
    • 0037120160 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and alpha-hydroxy acid residue containing peptides
    • D.T. Rijkers, J.W.M. Höppener, G. Posthuma, C.J.M. Lips, and R.M. Liskamp Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and alpha-hydroxy acid residue containing peptides Chemistry 8 2002 4285 4291
    • (2002) Chemistry , vol.8 , pp. 4285-4291
    • Rijkers, D.T.1    Höppener, J.W.M.2    Posthuma, G.3    Lips, C.J.M.4    Liskamp, R.M.5
  • 70
    • 5644248079 scopus 로고    scopus 로고
    • Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet beta cells in diabetes
    • R.P. Robertson Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet beta cells in diabetes Journal of Biological Chemistry 279 2004 42351 42354
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 42351-42354
    • Robertson, R.P.1
  • 71
    • 0036885616 scopus 로고    scopus 로고
    • Insulin: Discovery and controversy
    • L. Rosenfeld Insulin: Discovery and controversy Clinical Chemistry 48 2002 2270 2288
    • (2002) Clinical Chemistry , vol.48 , pp. 2270-2288
    • Rosenfeld, L.1
  • 73
    • 0242443338 scopus 로고    scopus 로고
    • Immunohistochemical localization of amylin in human pancreas, thyroid, pituitary and their tumors
    • F. Rotondo, S. Vidal, D. Bell, E. Horvath, K. Kovacs, and B.W. Scheithauer Immunohistochemical localization of amylin in human pancreas, thyroid, pituitary and their tumors Acta Histochemica 105 2003 303 307
    • (2003) Acta Histochemica , vol.105 , pp. 303-307
    • Rotondo, F.1    Vidal, S.2    Bell, D.3    Horvath, E.4    Kovacs, K.5    Scheithauer, B.W.6
  • 75
    • 0034516988 scopus 로고    scopus 로고
    • Towards a comprehensive theory for Alzheimer's disease. Hypothesis: Alzheimer's disease is caused by the cerebral accumulation and cytotoxicity of amyloid beta-protein
    • D.J. Selkoe Towards a comprehensive theory for Alzheimer's disease. Hypothesis: Alzheimer's disease is caused by the cerebral accumulation and cytotoxicity of amyloid beta-protein Annals of the New York Academy of Sciences 924 2000 17 25
    • (2000) Annals of the New York Academy of Sciences , vol.924 , pp. 17-25
    • Selkoe, D.J.1
  • 76
    • 0031920985 scopus 로고    scopus 로고
    • Islet amyloid-associated diabetes in obese A(vy)/a mice expressing human islet amyloid polypeptide
    • W.C. Soeller, J. Janson, S.E. Hart, J.C. Parker, M.D. Carty, and R.W. Stevenson Islet amyloid-associated diabetes in obese A(vy)/a mice expressing human islet amyloid polypeptide Diabetes 47 1998 743 750
    • (1998) Diabetes , vol.47 , pp. 743-750
    • Soeller, W.C.1    Janson, J.2    Hart, S.E.3    Parker, J.C.4    Carty, M.D.5    Stevenson, R.W.6
  • 77
    • 29544452318 scopus 로고    scopus 로고
    • The relation of fasting and 2-h postchallenge plasma glucose concentrations to mortality: Data from the Baltimore Longitudinal Study of Aging with a critical review of the literature
    • J.D. Sorkin, D.C. Muller, J.L. Fleg, and R. Andres The relation of fasting and 2-h postchallenge plasma glucose concentrations to mortality: Data from the Baltimore Longitudinal Study of Aging with a critical review of the literature Diabetes Care 28 2005 2626 2632
    • (2005) Diabetes Care , vol.28 , pp. 2626-2632
    • Sorkin, J.D.1    Muller, D.C.2    Fleg, J.L.3    Andres, R.4
  • 78
    • 17044386953 scopus 로고    scopus 로고
    • Type 2 diabetes: Principles of pathogenesis and therapy
    • M. Stumvoll, B.J. Goldstein, and T.W. Van Haeften Type 2 diabetes: Principles of pathogenesis and therapy Lancet 365 2005 1333 1346
    • (2005) Lancet , vol.365 , pp. 1333-1346
    • Stumvoll, M.1    Goldstein, B.J.2    Van Haeften, T.W.3
  • 79
    • 16644385273 scopus 로고    scopus 로고
    • An underdiagnosed type of diabetes: The MODY syndromes. Pathophysiology, clinical presentation and renal disease progression
    • D. Tsakiris, and K. Ioannou An underdiagnosed type of diabetes: The MODY syndromes. Pathophysiology, clinical presentation and renal disease progression Journal of Nephrology 17 2004 637 641
    • (2004) Journal of Nephrology , vol.17 , pp. 637-641
    • Tsakiris, D.1    Ioannou, K.2
  • 82
    • 34447595268 scopus 로고
    • Über eine im Gehirn und Rückenmark des Menschen aufgefundene Substanz mit der chemischen Reaction der Cellulose
    • R. Virchow Über eine im Gehirn und Rückenmark des Menschen aufgefundene Substanz mit der chemischen Reaction der Cellulose Archives of Pathological Anatomy and Physiology and Clinical Medicine 6 1854 135 138
    • (1854) Archives of Pathological Anatomy and Physiology and Clinical Medicine , vol.6 , pp. 135-138
    • Virchow, R.1
  • 83
    • 0035143161 scopus 로고    scopus 로고
    • Naturally occurring and experimental diabetes in cynomolgus monkeys: A comparison of carbohydrate and lipid metabolism and islet pathology
    • J.D. Wagner, J.M. Cline, M.K. Shadoan, B.C. Bullock, S.E. Rankin, and W.T. Cefalu Naturally occurring and experimental diabetes in cynomolgus monkeys: A comparison of carbohydrate and lipid metabolism and islet pathology Toxicologic Pathology 29 2001 142 148
    • (2001) Toxicologic Pathology , vol.29 , pp. 142-148
    • Wagner, J.D.1    Cline, J.M.2    Shadoan, M.K.3    Bullock, B.C.4    Rankin, S.E.5    Cefalu, W.T.6
  • 84
    • 12444281820 scopus 로고    scopus 로고
    • Potential role of oral thiazolidinedione therapy in preserving beta-cell function in type 2 diabetes mellitus
    • H. Walter, and G. Lubben Potential role of oral thiazolidinedione therapy in preserving beta-cell function in type 2 diabetes mellitus Drugs 65 2005 1 13
    • (2005) Drugs , vol.65 , pp. 1-13
    • Walter, H.1    Lubben, G.2
  • 85
    • 0035123349 scopus 로고    scopus 로고
    • The prohormone convertase enzyme 2 (PC2) is essential for processing pro-islet amyloid polypeptide at the NH2-terminal cleavage site
    • J. Wang, J. Xu, J. Finnerty, M. Furuta, D.F. Steiner, and C.B. Verchere The prohormone convertase enzyme 2 (PC2) is essential for processing pro-islet amyloid polypeptide at the NH2-terminal cleavage site Diabetes 50 2001 534 539
    • (2001) Diabetes , vol.50 , pp. 534-539
    • Wang, J.1    Xu, J.2    Finnerty, J.3    Furuta, M.4    Steiner, D.F.5    Verchere, C.B.6
  • 89
    • 0023192941 scopus 로고
    • 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
    • P. Westermark, C. Wernstedt, E. Wilander, D.W. Hayden, T.D. O'Brien, and K.H. Johnson 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 Proceedings of the National Academy of Sciences USA 84 1987 3881 3885
    • (1987) Proceedings of the National Academy of Sciences USA , vol.84 , pp. 3881-3885
    • Westermark, P.1    Wernstedt, C.2    Wilander, E.3    Hayden, D.W.4    O'Brien, T.D.5    Johnson, K.H.6
  • 90
    • 0023025399 scopus 로고
    • A novel peptide in the calcitonin gene related peptide family as an amyloid fibrilprotein in the endocrine pancreas
    • P. Westermark, C. Wernstedt, E. Wilander, and K. Sletten A novel peptide in the calcitonin gene related peptide family as an amyloid fibrilprotein in the endocrine pancreas Biochemical Biophysical Research Communications 140 1986 827 831
    • (1986) Biochemical Biophysical Research Communications , vol.140 , pp. 827-831
    • Westermark, P.1    Wernstedt, C.2    Wilander, E.3    Sletten, K.4
  • 92
    • 2342466734 scopus 로고    scopus 로고
    • Global prevalence of diabetes: Estimates for the year 2000 and projections for 2030
    • S. Wild, G. Roglic, A. Green, R. Sicree, and H. King Global prevalence of diabetes: Estimates for the year 2000 and projections for 2030 Diabetes Care 27 2004 1047 1053
    • (2004) Diabetes Care , vol.27 , pp. 1047-1053
    • Wild, S.1    Roglic, G.2    Green, A.3    Sicree, R.4    King, H.5
  • 93
    • 4944251744 scopus 로고    scopus 로고
    • Insulin resistance and obesity: Resistin, a hormone secreted by adipose tissue
    • G. Wolf Insulin resistance and obesity: Resistin, a hormone secreted by adipose tissue Nutrition Reviews 62 2004 389 394
    • (2004) Nutrition Reviews , vol.62 , pp. 389-394
    • Wolf, G.1
  • 94
    • 0346101742 scopus 로고    scopus 로고
    • Fibrillogenic amylin evokes islet beta-cell apoptosis through linked activation of a caspase cascade and JNK1
    • S. Zhang, J. Liu, M. Dragunow, and G.J.S. Cooper Fibrillogenic amylin evokes islet beta-cell apoptosis through linked activation of a caspase cascade and JNK1 Journal of Biological Chemistry 278 2003 52810 52819
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 52810-52819
    • Zhang, S.1    Liu, J.2    Dragunow, M.3    Cooper, G.J.S.4
  • 95
    • 0242332129 scopus 로고    scopus 로고
    • Prevalence and clinicopathological characteristics of islet amyloid in chinese patients with type 2 diabetes
    • H.L. Zhao, F.M. Lai, P.C. Tong, D.R. Zhong, D. Yang, and B. Tomlinson Prevalence and clinicopathological characteristics of islet amyloid in chinese patients with type 2 diabetes Diabetes 52 2003 2759 2766
    • (2003) Diabetes , vol.52 , pp. 2759-2766
    • Zhao, H.L.1    Lai, F.M.2    Tong, P.C.3    Zhong, D.R.4    Yang, D.5    Tomlinson, B.6
  • 96
    • 18144453071 scopus 로고    scopus 로고
    • The burden of type 2 diabetes: Are we doing enough?
    • P. Zimmet The burden of type 2 diabetes: Are we doing enough? Diabetes and Metabolism 29 2003 6S9 6S18
    • (2003) Diabetes and Metabolism , vol.29
    • Zimmet, P.1


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