메뉴 건너뛰기




Volumn 48, Issue 2, 1999, Pages 241-253

Islet amyloid: A long-recognized but underappreciated pathological feature of type 2 diabetes

Author keywords

[No Author keywords available]

Indexed keywords

AMYLIN; AMYLOID;

EID: 0032969276     PISSN: 00121797     EISSN: None     Source Type: Journal    
DOI: 10.2337/diabetes.48.2.241     Document Type: Review
Times cited : (444)

References (119)
  • 1
    • 85025386842 scopus 로고
    • The relation of diabetes mellitus to lesions of the pancreas: Hyaline degeneration of the islets of Langerhans
    • Opie E: The relation of diabetes mellitus to lesions of the pancreas: hyaline degeneration of the islets of Langerhans. J Exp Med 5:527-540, 1901
    • (1901) J Exp Med , vol.5 , pp. 527-540
    • Opie, E.1
  • 2
    • 0000611472 scopus 로고
    • Hyalinization of the islets of Langerhans in nondiabetic individuals
    • Bell ET: Hyalinization of the islets of Langerhans in nondiabetic individuals. Am J Pathol 35:801-805, 1959
    • (1959) Am J Pathol , vol.35 , pp. 801-805
    • Bell, E.T.1
  • 3
    • 0015277207 scopus 로고
    • Quantitative studies on amyloid in the islets of Langerhans
    • Westermark P: Quantitative studies on amyloid in the islets of Langerhans. Ups J Med Sci 77:91-94, 1972
    • (1972) Ups J Med Sci , vol.77 , pp. 91-94
    • Westermark, P.1
  • 5
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidosis: The beta-fibrilloses
    • Glenner GG: Amyloid deposits and amyloidosis: the beta-fibrilloses. N Engl J Med 302:1283-1292, 1333-1343, 1980
    • (1980) N Engl J Med , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 7
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW: Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 120:885-890, 1984
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 8
    • 0027458857 scopus 로고
    • Nomenclature of amyloid and amyloidosis
    • WHO-IUIS Nomenclature Sub-Committee: Nomenclature of amyloid and amyloidosis. Bull World Health Organ 71:105-112, 1993
    • (1993) Bull World Health Organ , vol.71 , pp. 105-112
  • 9
    • 0030684085 scopus 로고    scopus 로고
    • Aβ amyloidogenesis: Unique, or variation on a systemic theme?
    • Kisilevsky R, Fraser PE: Aβ amyloidogenesis: unique, or variation on a systemic theme? Crit Rev Biochem Mol Biol 32:361-104, 1997
    • (1997) Crit Rev Biochem Mol Biol , vol.32 , pp. 361-1104
    • Kisilevsky, R.1    Fraser, P.E.2
  • 10
    • 0014258458 scopus 로고
    • Fine structure of two amyloid-forming medullary carcinomas of thyroid
    • Meyer JS: Fine structure of two amyloid-forming medullary carcinomas of thyroid. Cancer 21:406-425, 1968
    • (1968) Cancer , vol.21 , pp. 406-425
    • Meyer, J.S.1
  • 12
    • 0023818388 scopus 로고
    • Calcitonin-like immunoreactivity of amyloid fibrils in medullary thyroid carcinomas: An immunoelectron microscope study
    • Berger G, Berger N, Guillaud MH, Trouillas J, Vauzelle JL: Calcitonin-like immunoreactivity of amyloid fibrils in medullary thyroid carcinomas: an immunoelectron microscope study. Virchows Arch A Pathol Anat Histopathol 412:543-551, 1988
    • (1988) Virchows Arch A Pathol Anat Histopathol , vol.412 , pp. 543-551
    • Berger, G.1    Berger, N.2    Guillaud, M.H.3    Trouillas, J.4    Vauzelle, J.L.5
  • 13
    • 0023222388 scopus 로고
    • Islet amyloid in type 2 human diabetes mellitus and adult diabetic cats contains a novel putative polypeptide hormone
    • Westermark P, Wernstedt C, O'Brien TD, Hayden DW, Johnson KH: Islet amyloid in type 2 human diabetes mellitus and adult diabetic cats contains a novel putative polypeptide hormone. Am J Pathol 127:414-417, 1987
    • (1987) Am J Pathol , vol.127 , pp. 414-417
    • Westermark, P.1    Wernstedt, C.2    O'Brien, T.D.3    Hayden, D.W.4    Johnson, K.H.5
  • 14
    • 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 islets
    • Westermark P, Wernstedt C, Wilander E, Hayden DW, O'Brien TD, Johnson KH: Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islets. Proc Natl Acad Sci U S A 84:3881-3885, 1987
    • (1987) Proc Natl Acad Sci 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
  • 15
    • 0023579739 scopus 로고
    • Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients
    • Cooper GJS, Willis AC, Clark A, Turner RC, Sim RB, Reid KBM: Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc Natl Acad Sci U S A 184:8628-8632, 1987
    • (1987) Proc Natl Acad Sci USA , vol.184 , pp. 8628-8632
    • Cooper, G.J.S.1    Willis, A.C.2    Clark, A.3    Turner, R.C.4    Sim, R.B.5    Reid, K.B.M.6
  • 16
    • 0023899417 scopus 로고
    • Isolation and characterization of amyloid P component from Alzheimer's disease and other types of cerebral amyloidosis
    • Coria F, Castano E, Prelli F, Larrondo-Lillo M, van Duinen S, Shelanski ML, Frangione B: Isolation and characterization of amyloid P component from Alzheimer's disease and other types of cerebral amyloidosis. Lab Invest 58:454-458, 1988
    • (1988) Lab Invest , vol.58 , pp. 454-458
    • Coria, F.1    Castano, E.2    Prelli, F.3    Larrondo-Lillo, M.4    Van Duinen, S.5    Shelanski, M.L.6    Frangione, B.7
  • 18
    • 0026542786 scopus 로고
    • Apolipoprotein E: A pathological chaperone protein in patients with cerebral and systemic amyloid
    • Wisniewski T, Frangione B: Apolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amyloid. Neurosci Lett 135:235-238, 1992
    • (1992) Neurosci Lett , vol.135 , pp. 235-238
    • Wisniewski, T.1    Frangione, B.2
  • 19
    • 0024387388 scopus 로고
    • Proteoglycans in the pathogenesis of Alzheimer's disease and other amyloidoses
    • Snow AD, Wight TN: Proteoglycans in the pathogenesis of Alzheimer's disease and other amyloidoses. Neurobiol Aging 10:481-497, 1989
    • (1989) Neurobiol Aging , vol.10 , pp. 481-497
    • Snow, A.D.1    Wight, T.N.2
  • 20
    • 0028082136 scopus 로고
    • An important role of heparan sulfate proteoglycan (perlecan) in a model system for the deposition and persistence of fibrillar a beta-amyloid in rat brain
    • Snow AD, Sekiguchi R, Nochlin D, Fraser P, Kimata K, Mizutani A, Arai M, Schreier WA, Morgan DG: An important role of heparan sulfate proteoglycan (perlecan) in a model system for the deposition and persistence of fibrillar A beta-amyloid in rat brain. Neuron 12:219-234, 1994
    • (1994) Neuron , vol.12 , pp. 219-234
    • Snow, A.D.1    Sekiguchi, R.2    Nochlin, D.3    Fraser, P.4    Kimata, K.5    Mizutani, A.6    Arai, M.7    Schreier, W.A.8    Morgan, D.G.9
  • 21
    • 84907135505 scopus 로고
    • Amyloid and polypeptide hormones: What is their relatioaship?
    • Westermark P: Amyloid and polypeptide hormones: what is their relatioaship? Amyloid Int J Exp Clin Invest 1:47-60, 1994
    • (1994) Amyloid Int J Exp Clin Invest , vol.1 , pp. 47-60
    • Westermark, P.1
  • 22
    • 0018750259 scopus 로고
    • The effect of aging on carbohydrate metabolism: A review of the English literature and a practical approach to the diagnosis of diabetes mellitus in the elderly
    • Davidson MB: The effect of aging on carbohydrate metabolism: a review of the English literature and a practical approach to the diagnosis of diabetes mellitus in the elderly. Metabolism 28:687-705, 1979
    • (1979) Metabolism , vol.28 , pp. 687-705
    • Davidson, M.B.1
  • 24
    • 0024463227 scopus 로고
    • Hyperproinsulinemia and amyloid in NIDDM: Clues to etiology of islet β-cell dysfunction?
    • Porte D Jr, Kahn SE: Hyperproinsulinemia and amyloid in NIDDM: clues to etiology of islet β-cell dysfunction? Diabetes 38:1333-1336, 1989
    • (1989) Diabetes , vol.38 , pp. 1333-1336
    • Porte D., Jr.1    Kahn, S.E.2
  • 32
    • 0023692891 scopus 로고
    • Pancreatic amylin and calcitonin gene-related peptide cause resistance to insulin in skeletal muscle in vitro
    • Leighton B, Cooper GJ: Pancreatic amylin and calcitonin gene-related peptide cause resistance to insulin in skeletal muscle in vitro. Nature 335:632-635, 1988
    • (1988) Nature , vol.335 , pp. 632-635
    • Leighton, B.1    Cooper, G.J.2
  • 33
    • 0025054691 scopus 로고
    • Inhibitory effect of rat amylin on the insulin responses to glucose and arginine in the perfused rat pancreas
    • Silvestre RA, Peiro' E, De'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 31:23-31, 1990
    • (1990) Regul Pept , vol.31 , pp. 23-31
    • Silvestre, R.A.1    Peiro', E.2    De'gano, P.3    Miralles, P.4    Marco, J.5
  • 34
    • 0028354142 scopus 로고
    • Amylin compared with calcitonin gene-related peptide: Structure, biology, and relevance to metabolic disease
    • Cooper GJS: Amylin compared with calcitonin gene-related peptide: structure, biology, and relevance to metabolic disease. Endocr Rev 15:163-201, 1994
    • (1994) Endocr Rev , vol.15 , pp. 163-201
    • Cooper, G.J.S.1
  • 35
    • 0029913870 scopus 로고    scopus 로고
    • Dose-responses for the slowing of gastric emptying in a rodent model by glucagon-like peptide (7-36) NH2, amylin, cholecystokinin, and other possible regulators of nutrient uptake
    • Young AA, Gedulin BR, Rink TJ: Dose-responses for the slowing of gastric emptying in a rodent model by glucagon-like peptide (7-36) NH2, amylin, cholecystokinin, and other possible regulators of nutrient uptake. Metabolism 45:1-3, 1996
    • (1996) Metabolism , vol.45 , pp. 1-3
    • Young, A.A.1    Gedulin, B.R.2    Rink, T.J.3
  • 38
    • 0028303844 scopus 로고
    • Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus
    • Lorenzo A, Razzaboni B, Weir GC, Yankner BA: Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus. Nature 368:756-760, 1994
    • (1994) Nature , vol.368 , pp. 756-760
    • Lorenzo, A.1    Razzaboni, B.2    Weir, G.C.3    Yankner, B.A.4
  • 39
    • 84920306449 scopus 로고    scopus 로고
    • Human islet amyloid polypeptide (hIAPP) cytotoxicity is caused by membrane damage
    • Janson J, Ashley R, Butler P: Human islet amyloid polypeptide (hIAPP) cytotoxicity is caused by membrane damage (Abstract). Diabetes 47 (Suppl. 1):A250, 1998
    • (1998) Diabetes , vol.47 , Issue.1 SUPPL.
    • Janson, J.1    Ashley, R.2    Butler, P.3
  • 45
    • 0029978228 scopus 로고    scopus 로고
    • Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic beta cell expression of human islet amyloid polypeptide
    • Verchere CB, D'Alessio DA, Palmiter RD, Weir GC, Bonner-Weir S, Baskin DG, Kahn SE: Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic beta cell expression of human islet amyloid polypeptide. Proc Natl Acad Sci U S A 93:3492-3496, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3492-3496
    • Verchere, C.B.1    D'Alessio, D.A.2    Palmiter, R.D.3    Weir, G.C.4    Bonner-Weir, S.5    Baskin, D.G.6    Kahn, S.E.7
  • 46
    • 0016753186 scopus 로고
    • Apoprotein composition of very low density lipoproteins of human serum
    • Kane JP, Sata T, Hamilton RL, Havel RJ: Apoprotein composition of very low density lipoproteins of human serum. J Clin Invest 56:1622-1634, 1975
    • (1975) J Clin Invest , vol.56 , pp. 1622-1634
    • Kane, J.P.1    Sata, T.2    Hamilton, R.L.3    Havel, R.J.4
  • 47
    • 0020972414 scopus 로고
    • Lipoprotein metabolism in the macrophage: Implications for cholesterol deposition in atherosclerosis
    • Brown MS, Goldstein JL: Lipoprotein metabolism in the macrophage: implications for cholesterol deposition in atherosclerosis. Annu Rev Biochem 52:223-261, 1983
    • (1983) Annu Rev Biochem , vol.52 , pp. 223-261
    • Brown, M.S.1    Goldstein, J.L.2
  • 48
  • 51
    • 0028080483 scopus 로고
    • Presence of apolipoprotein E on extracellular neurofibrillary tangles and on meningeal blood vessels precedes the Alzheimer beta-amyloid deposition
    • Yamaguchi H, Ishiguro K, Sugihara S, Nakazato Y, Kawarabayashi T, Sun X, Hirai S: Presence of apolipoprotein E on extracellular neurofibrillary tangles and on meningeal blood vessels precedes the Alzheimer beta-amyloid deposition. Acta Neuropathol 88:413-419, 1994
    • (1994) Acta Neuropathol , vol.88 , pp. 413-419
    • Yamaguchi, H.1    Ishiguro, K.2    Sugihara, S.3    Nakazato, Y.4    Kawarabayashi, T.5    Sun, X.6    Hirai, S.7
  • 52
    • 0029839914 scopus 로고    scopus 로고
    • Apolipoprotein E is associated with islet amyloid and other amyloidoses: Implications for Alzheimer's disease
    • Charge SB, Esiri MM, Bethune CA, Hansen BC, Clark A: Apolipoprotein E is associated with islet amyloid and other amyloidoses: implications for Alzheimer's disease. J Pathol 179:443-447, 1996
    • (1996) J Pathol , vol.179 , pp. 443-447
    • Charge, S.B.1    Esiri, M.M.2    Bethune, C.A.3    Hansen, B.C.4    Clark, A.5
  • 53
    • 0344749100 scopus 로고    scopus 로고
    • Role of apolipoprotein E and perlecan in islet amyloid formation in transgenic mice expressing human islet amyloid polypeptide
    • Verchere CB, Andrikopoulos S, D'Alessio DA, O'Brien KD, Wight TN, Snow AD, Olin KL, Kahn SE: Role of apolipoprotein E and perlecan in islet amyloid formation in transgenic mice expressing human islet amyloid polypeptide. Diabetes 47 (Suppl. 1):A30, 1998
    • (1998) Diabetes , vol.47 , Issue.1 SUPPL.
    • Verchere, C.B.1    Andrikopoulos, S.2    D'Alessio, D.A.3    O'Brien, K.D.4    Wight, T.N.5    Snow, A.D.6    Olin, K.L.7    Kahn, S.E.8
  • 54
    • 0023080585 scopus 로고
    • Astrocytes synthesize apolipoprotein E and metabolize apolipoprotein E-containing lipoproteins
    • Pitas RE, Boyles JK, Lee SH, Foss D, Mahley RW: Astrocytes synthesize apolipoprotein E and metabolize apolipoprotein E-containing lipoproteins. Biochim Biophys Acta 917:148-161, 1987
    • (1987) Biochim Biophys Acta , vol.917 , pp. 148-161
    • Pitas, R.E.1    Boyles, J.K.2    Lee, S.H.3    Foss, D.4    Mahley, R.W.5
  • 55
    • 0020426701 scopus 로고
    • Biochemical and genetic studies of the apoprotein E secreted by mouse macrophages and human monocytes
    • Basu SK, Ho YK, Brown MS, Bilheimer DW, Anderson RG, Goldstein JL: Biochemical and genetic studies of the apoprotein E secreted by mouse macrophages and human monocytes. J Biol Chem 257:9788-9795, 1982
    • (1982) J Biol Chem , vol.257 , pp. 9788-9795
    • Basu, S.K.1    Ho, Y.K.2    Brown, M.S.3    Bilheimer, D.W.4    Anderson, R.G.5    Goldstein, J.L.6
  • 56
    • 0028173205 scopus 로고
    • Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments
    • Ma J, Yee A, Brewer HB Jr, Das S, Potter H: Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments. Nature 372:92-94, 1994
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.1    Yee, A.2    Brewer H.B., Jr.3    Das, S.4    Potter, H.5
  • 57
    • 0027970307 scopus 로고
    • Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro
    • Wisniewski T, Castano EM, Golabek A, Vogel T, Frangione B: Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro. Am J Pathol 145:1030-1035, 1994
    • (1994) Am J Pathol , vol.145 , pp. 1030-1035
    • Wisniewski, T.1    Castano, E.M.2    Golabek, A.3    Vogel, T.4    Frangione, B.5
  • 60
    • 0026688125 scopus 로고
    • Localization of the basement membrane heparan sulfate proteoglycan in islet amyloid deposits in type II diabetes mellitus
    • Young ID, Ailles L, Narindrasorasak S, Tan R, Kisilevsky R: Localization of the basement membrane heparan sulfate proteoglycan in islet amyloid deposits in type II diabetes mellitus. Arch Pathol Lab Med 116:951-954, 1992
    • (1992) Arch Pathol Lab Med , vol.116 , pp. 951-954
    • Young, I.D.1    Ailles, L.2    Narindrasorasak, S.3    Tan, R.4    Kisilevsky, R.5
  • 61
    • 0025875756 scopus 로고
    • Proteoglycans: Structures and interactions
    • Kjellen L, Lindahl U: Proteoglycans: structures and interactions. Annu Rev Biochem 60:443-475, 1991
    • (1991) Annu Rev Biochem , vol.60 , pp. 443-475
    • Kjellen, L.1    Lindahl, U.2
  • 62
    • 0028102255 scopus 로고
    • The biology of perlecan: The multifaceted heparan sulphate proteoglycan of basement membranes and pericellular matrices
    • Iozzo RV, Cohen IR, Grassel S, Murdoch AD: The biology of perlecan: the multifaceted heparan sulphate proteoglycan of basement membranes and pericellular matrices. Biochem J 302:625-639, 1994
    • (1994) Biochem J , vol.302 , pp. 625-639
    • Iozzo, R.V.1    Cohen, I.R.2    Grassel, S.3    Murdoch, A.D.4
  • 63
    • 0026673537 scopus 로고
    • Effects of sulfate ions on Alzheimer beta/A4 peptide assemblies: Implications for amyloid fibril-proteoglycan interactions
    • Fraser PE, Nguyen JT, Chin DT, Kirschner DA: Effects of sulfate ions on Alzheimer beta/A4 peptide assemblies: implications for amyloid fibril-proteoglycan interactions. J Neurochem 59:1531-1540, 1992
    • (1992) J Neurochem , vol.59 , pp. 1531-1540
    • Fraser, P.E.1    Nguyen, J.T.2    Chin, D.T.3    Kirschner, D.A.4
  • 64
    • 0028978227 scopus 로고
    • Proteoglycan-mediated inhibition of A beta proteolysis: A potential cause of senile plaque accumulation
    • Gupta-Bansal R, Frederickson RC, Brunden KR: Proteoglycan-mediated inhibition of A beta proteolysis: a potential cause of senile plaque accumulation. J Biol Chem 270:18666-18671, 1995
    • (1995) J Biol Chem , vol.270 , pp. 18666-18671
    • Gupta-Bansal, R.1    Frederickson, R.C.2    Brunden, K.R.3
  • 65
    • 0031895939 scopus 로고    scopus 로고
    • Sulfate content and specific glycosaminoglycan backbone of perlecan are critical for perlecan's enhancement of islet amyloid polypeptide (amylin) fibril formation
    • Castillo GM, Cummings JA, Yang W, Judge ME, Sheardown MJ, Rimvall K, Hansen JB, Snow AD: Sulfate content and specific glycosaminoglycan backbone of perlecan are critical for perlecan's enhancement of islet amyloid polypeptide (amylin) fibril formation. Diabetes 47:612-620, 1998
    • (1998) Diabetes , vol.47 , pp. 612-620
    • Castillo, G.M.1    Cummings, J.A.2    Yang, W.3    Judge, M.E.4    Sheardown, M.J.5    Rimvall, K.6    Hansen, J.B.7    Snow, A.D.8
  • 66
    • 0018130887 scopus 로고
    • Insular amyloidosis and diabetes mellitus in Macaca nigra
    • Howard CF Jr: Insular amyloidosis and diabetes mellitus in Macaca nigra. Diabetes 27:357-364, 1978
    • (1978) Diabetes , vol.27 , pp. 357-364
    • Howard C.F., Jr.1
  • 67
    • 0022496637 scopus 로고
    • Longitudinal studies on the development of diabetes in individual Macaca nigra
    • Howard CF Jr: Longitudinal studies on the development of diabetes in individual Macaca nigra. Diabetologia 29:301-306, 1986
    • (1986) Diabetologia , vol.29 , pp. 301-306
    • Howard C.F., Jr.1
  • 68
    • 0018146301 scopus 로고
    • The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus
    • Westermark P, Wilander E: The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus. Diabetologia 15:417-421, 1978
    • (1978) Diabetologia , vol.15 , pp. 417-421
    • Westermark, P.1    Wilander, E.2
  • 69
    • 0027151935 scopus 로고
    • Diabetes mellitus in Macaca mulatta monkeys is characterised by islet amyloidosis and reduction in beta-cell population
    • de Koning EJ, Bodkin NL, Hansen BC, Clark A: Diabetes mellitus in Macaca mulatta monkeys is characterised by islet amyloidosis and reduction in beta-cell population. Diabetologia 36:378-384, 1993
    • (1993) Diabetologia , vol.36 , pp. 378-384
    • De Koning, E.J.1    Bodkin, N.L.2    Hansen, B.C.3    Clark, A.4
  • 70
    • 0026110135 scopus 로고
    • β-Cells in type II diabetes mellitus
    • Porte D Jr: β-Cells in type II diabetes mellitus. Diabetes 40:166-180, 1991
    • (1991) Diabetes , vol.40 , pp. 166-180
    • Porte D., Jr.1
  • 72
    • 0025095979 scopus 로고
    • Islet amyloid polypeptide (amylin): No evidence of an abnormal precursor sequence in 25 type 2 (non-insulin-dependent) diabetic patients
    • Nishi M, Bell GI, Steiner DF: Islet amyloid polypeptide (amylin): no evidence of an abnormal precursor sequence in 25 type 2 (non-insulin-dependent) diabetic patients. Diabetologia 33:628-630, 1990
    • (1990) Diabetologia , vol.33 , pp. 628-630
    • Nishi, M.1    Bell, G.I.2    Steiner, D.F.3
  • 76
    • 0029330879 scopus 로고
    • Amyloid formation in response to beta cell stress in vitro, but not in vivo, in islets of transgenic mice expressing human islet amyloid polypeptide
    • Westermark G, Benig-Arora M, Fox N, Carroll R, Chan S-J, Westermark P, Steiner DF: Amyloid formation in response to beta cell stress in vitro, but not in vivo, in islets of transgenic mice expressing human islet amyloid polypeptide. Mol Med 1:542-553, 1995
    • (1995) Mol Med , vol.1 , pp. 542-553
    • Westermark, G.1    Benig-Arora, M.2    Fox, N.3    Carroll, R.4    Chan, S.-J.5    Westermark, P.6    Steiner, D.F.7
  • 78
    • 0029742232 scopus 로고    scopus 로고
    • Treatment with growth hormone and dexamethasone in mice transgenic for human islet amyloid polypeptide causes islet amyloidosis and B-cell dysfunction
    • Couce M, Kane LA, O'Brien TD, Charlesworth J, Soeller W, McNeish J, Kreutter D, Roche P, Butler PC: Treatment with growth hormone and dexamethasone in mice transgenic for human islet amyloid polypeptide causes islet amyloidosis and B-cell dysfunction. Diabetes 45:1094-1101, 1996
    • (1996) Diabetes , vol.45 , pp. 1094-1101
    • Couce, M.1    Kane, L.A.2    O'Brien, T.D.3    Charlesworth, J.4    Soeller, W.5    McNeish, J.6    Kreutter, D.7    Roche, P.8    Butler, P.C.9
  • 80
    • 84995868876 scopus 로고
    • Islet amyloidosis in a patient with chronic massive insulin resistance due to antiinsulin receptor antibodies
    • O'Brien TD, Rizza RA, Carney JA, Butler PC: Islet amyloidosis in a patient with chronic massive insulin resistance due to antiinsulin receptor antibodies. J Clin Endocrinol Metab 79:290-282, 1994
    • (1994) J Clin Endocrinol Metab , vol.79 , pp. 290-1282
    • O'Brien, T.D.1    Rizza, R.A.2    Carney, J.A.3    Butler, P.C.4
  • 81
    • 0029126786 scopus 로고
    • Human islet amyloid polypeptide expression in COS-1 cells: A model of intracellular amyloidogenesis
    • O'Brien TD, Butler PC, Kreutter DK, Kane LA, Eberhardt NL: Human islet amyloid polypeptide expression in COS-1 cells: a model of intracellular amyloidogenesis. Am J Pathol 147:609-616, 1995
    • (1995) Am J Pathol , vol.147 , pp. 609-616
    • O'Brien, T.D.1    Butler, P.C.2    Kreutter, D.K.3    Kane, L.A.4    Eberhardt, N.L.5
  • 84
    • 0024413349 scopus 로고
    • Localisation of islet amyloid peptide in lipofuscin bodies and secretory granules of human B-cells and in islets of type-2 diabetic subjects
    • Clark A, Edwards CA, Ostle LR, Sutton R, Rothbard JB, Morris JF, Turner RC: Localisation of islet amyloid peptide in lipofuscin bodies and secretory granules of human B-cells and in islets of type-2 diabetic subjects. Cell Tissue Res 257:179-185, 1989
    • (1989) Cell Tissue Res , vol.257 , pp. 179-185
    • Clark, A.1    Edwards, C.A.2    Ostle, L.R.3    Sutton, R.4    Rothbard, J.B.5    Morris, J.F.6    Turner, R.C.7
  • 86
    • 0030478641 scopus 로고    scopus 로고
    • Islet amyloid polypeptide and insulin gene expression are regulated in parallel by glucose in vivo in rats
    • Mulder H, Ahren B, Sundler F: Islet amyloid polypeptide and insulin gene expression are regulated in parallel by glucose in vivo in rats. Am J Physiol 271:E1008-E1014, 1996
    • (1996) Am J Physiol , vol.271
    • Mulder, H.1    Ahren, B.2    Sundler, F.3
  • 87
    • 0024464611 scopus 로고
    • Impaired glucose tolerance is associated with increased islet amyloid polypeptide (IAPP) immunoreactivity in pancreatic beta cells
    • Johnson KH, O'Brien TD, Jordan K, Westermark P: Impaired glucose tolerance is associated with increased islet amyloid polypeptide (IAPP) immunoreactivity in pancreatic beta cells. Am J Pathol 135:245-250, 1989
    • (1989) Am J Pathol , vol.135 , pp. 245-250
    • Johnson, K.H.1    O'Brien, T.D.2    Jordan, K.3    Westermark, P.4
  • 89
    • 0025775928 scopus 로고
    • Hypersecretion of islet amyloid polypeptide from pancreatic islets of ventromedial hypothalamic-lesioned rats and obese Zucker rats
    • Tokuyania Y, Kanatsuka A, Ohsawa H, Yamaguchi T, Makino H, Yoshida S, Nagase H, Inoue S: Hypersecretion of islet amyloid polypeptide from pancreatic islets of ventromedial hypothalamic-lesioned rats and obese Zucker rats. Endocrinology 128:2739-2744, 1991
    • (1991) Endocrinology , vol.128 , pp. 2739-2744
    • Tokuyania, Y.1    Kanatsuka, A.2    Ohsawa, H.3    Yamaguchi, T.4    Makino, H.5    Yoshida, S.6    Nagase, H.7    Inoue, S.8
  • 91
    • 0031735539 scopus 로고    scopus 로고
    • Changes in amylin and amylin-like peptide concentrations and β-cell function in response to sulfonylurea or insulin therapy in NIDDM
    • Rachman J, Payne MJ, Levy JC, Barrow BA, Holman RR, Turner RC: Changes in amylin and amylin-like peptide concentrations and β-cell function in response to sulfonylurea or insulin therapy in NIDDM. Diabetes Care 21:810-816, 1998
    • (1998) Diabetes Care , vol.21 , pp. 810-816
    • Rachman, J.1    Payne, M.J.2    Levy, J.C.3    Barrow, B.A.4    Holman, R.R.5    Turner, R.C.6
  • 92
    • 0028329930 scopus 로고
    • Sorting and processing of secretory proteins
    • Halban PA, Irminger JC: Sorting and processing of secretory proteins. Biochem J 299:1-18, 1994
    • (1994) Biochem J , vol.299 , pp. 1-18
    • Halban, P.A.1    Irminger, J.C.2
  • 93
    • 0026580076 scopus 로고
    • 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
    • Nagamatsu S, Nishi M, Steiner DF: 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. Diabetes Res Clin Pract 15:49-05, 1992
    • (1992) Diabetes Res Clin Pract , vol.15 , pp. 49-105
    • Nagamatsu, S.1    Nishi, M.2    Steiner, D.F.3
  • 94
    • 0027193752 scopus 로고
    • Evidence for selective release of rodent islet amyloid polypeptide through the constitutive secretory pathway
    • Kahn SE, Verchere CB, D'Alessio DA, Cook DL, Fujimoto WT: Evidence for selective release of rodent islet amyloid polypeptide through the constitutive secretory pathway. Diabetologia 36:570-573, 1993
    • (1993) Diabetologia , vol.36 , pp. 570-573
    • Kahn, S.E.1    Verchere, C.B.2    D'Alessio, D.A.3    Cook, D.L.4    Fujimoto, W.T.5
  • 95
    • 0030064237 scopus 로고    scopus 로고
    • Processing of pro-islet amyloid polypeptide (proIAPP) by the prohormone convertase PC2
    • Badman MK, Shennan H, Jermany JL, Docherty K, Clark A: Processing of pro-islet amyloid polypeptide (proIAPP) by the prohormone convertase PC2. FEBS Lett 378:227-231, 1996
    • (1996) FEBS Lett , vol.378 , pp. 227-231
    • Badman, M.K.1    Shennan, H.2    Jermany, J.L.3    Docherty, K.4    Clark, A.5
  • 96
    • 0023895049 scopus 로고
    • Intraorganellar calcium and pH control proinsulin cleavage in the pancreatic β-cell via two distinct site-specific endopeptidases
    • Davidson HW, Rhodes CJ, Hutton JC: Intraorganellar calcium and pH control proinsulin cleavage in the pancreatic β-cell via two distinct site-specific endopeptidases. Nature 333:93-96, 1988
    • (1988) Nature , vol.333 , pp. 93-96
    • Davidson, H.W.1    Rhodes, C.J.2    Hutton, J.C.3
  • 98
    • 0023634652 scopus 로고
    • Disproportionate elevation of immunoreactive proinsulin in type 2 (non-insulin-dependent) diabetes mellitus and experimental insulin resistance
    • Ward WK, LaCava EC, Paquette TL, Beard JC, Wallum BJ, Porte D Jr: Disproportionate elevation of immunoreactive proinsulin in type 2 (non-insulin-dependent) diabetes mellitus and experimental insulin resistance. Diabetologia 30:698-702, 1987
    • (1987) Diabetologia , vol.30 , pp. 698-702
    • Ward, W.K.1    LaCava, E.C.2    Paquette, T.L.3    Beard, J.C.4    Wallum, B.J.5    Porte D., Jr.6
  • 99
    • 0030662718 scopus 로고
    • Release of incompletely processed proinsulin is the cause of the disproportionate proinsulinemia of NIDDM
    • Kahn SE, Halban PA: Release of incompletely processed proinsulin is the cause of the disproportionate proinsulinemia of NIDDM. Diabetes 46:1723-1732, 1987
    • (1987) Diabetes , vol.46 , pp. 1723-1732
    • Kahn, S.E.1    Halban, P.A.2
  • 100
    • 0031790302 scopus 로고    scopus 로고
    • Human aging is associated with parallel reductions in insulin and amylin release
    • Dechenes CJ, Verchere CB, Andrikopoulos S, Kahn SE: Human aging is associated with parallel reductions in insulin and amylin release. Am J Physiol 275:E785-E791, 1998
    • (1998) Am J Physiol , vol.275
    • Dechenes, C.J.1    Verchere, C.B.2    Andrikopoulos, S.3    Kahn, S.E.4
  • 101
    • 0024822388 scopus 로고
    • Diagnostic interpretation of the intravenous tolbutamide test for insulinoma
    • McMahon MM, O'Brien PC, Service FJ: Diagnostic interpretation of the intravenous tolbutamide test for insulinoma. Mayo Clin Proc 64:1481-1488, 1989
    • (1989) Mayo Clin Proc , vol.64 , pp. 1481-1488
    • McMahon, M.M.1    O'Brien, P.C.2    Service, F.J.3
  • 102
    • 0026509651 scopus 로고
    • Altered glucose regulation of insulin biosynthesis in insulinoma cells: Mouse beta TC3 cells secrete insulin-related peptides predominantly via a constitutive pathway
    • Nagamatsu S, Steiner DF: Altered glucose regulation of insulin biosynthesis in insulinoma cells: mouse beta TC3 cells secrete insulin-related peptides predominantly via a constitutive pathway. Endocrinology 130:748-754, 1992
    • (1992) Endocrinology , vol.130 , pp. 748-754
    • Nagamatsu, S.1    Steiner, D.F.2
  • 103
    • 0025812905 scopus 로고
    • Biosynthesis of islet amyloid polypeptide. Elevated expression in mouse beta TC3 cells
    • Nagamatsu S, Nishi M, Steiner DF: Biosynthesis of islet amyloid polypeptide. Elevated expression in mouse beta TC3 cells. J Biol Chem 266:13737-13741, 1991
    • (1991) J Biol Chem , vol.266 , pp. 13737-13741
    • Nagamatsu, S.1    Nishi, M.2    Steiner, D.F.3
  • 104
    • 0026734721 scopus 로고
    • Islet amyloid polypeptide-producing pancreatic islet cell tumor a clinical and biochemical characterization
    • Stridsberg M, Wilander E, Oberg K, Lundqvist G, Eriksson B: Islet amyloid polypeptide-producing pancreatic islet cell tumor a clinical and biochemical characterization. Scand J Gastroenterol 27:381-387, 1992
    • (1992) Scand J Gastroenterol , vol.27 , pp. 381-387
    • Stridsberg, M.1    Wilander, E.2    Oberg, K.3    Lundqvist, G.4    Eriksson, B.5
  • 106
    • 0025063525 scopus 로고
    • Diet of second-generation Japanese-American men with and without non-insulin-dependent diabetes
    • Tsunehara CH, Leonetti DL, Fujimoto WY: Diet of second-generation Japanese-American men with and without non-insulin-dependent diabetes. Am J Clin Nutr 52:731-738, 1990
    • (1990) Am J Clin Nutr , vol.52 , pp. 731-738
    • Tsunehara, C.H.1    Leonetti, D.L.2    Fujimoto, W.Y.3
  • 108
    • 0029027767 scopus 로고
    • Defective glucose-stimulated insulin release from perifused islets of C57BL/6J mice
    • Lee SK, Opara EC, Surwit RS, Feinglos MN, Akwari OE: Defective glucose-stimulated insulin release from perifused islets of C57BL/6J mice. Pancreas 11:206-211, 1995
    • (1995) Pancreas , vol.11 , pp. 206-211
    • Lee, S.K.1    Opara, E.C.2    Surwit, R.S.3    Feinglos, M.N.4    Akwari, O.E.5
  • 109
    • 0029151863 scopus 로고
    • Lipotoxicity in the pathogenesis of obesity-dependent NIDDM: Genetic and clinical implications
    • Unger RH: Lipotoxicity in the pathogenesis of obesity-dependent NIDDM: genetic and clinical implications. Diabetes 44:863-870, 1985
    • (1985) Diabetes , vol.44 , pp. 863-870
    • Unger, R.H.1
  • 110
    • 0032478314 scopus 로고    scopus 로고
    • Fatty acid-induced beta cell apoptosis: A link between obesity and diabetes
    • Shimabukuro M, Zhou YT, Levi M, linger RH: Fatty acid-induced beta cell apoptosis: a link between obesity and diabetes. Proc Natl Acad Sci U S A 95:2498-2502, 1998
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2498-2502
    • Shimabukuro, M.1    Zhou, Y.T.2    Levi, M.3    Linger, R.H.4
  • 111
    • 0028268936 scopus 로고
    • Long-term exposure of rat pancreatic islets to fatty acids inhibits glucose-induced insulin secretion and biosynthesis through a glucose fatty acid cycle
    • Zhou YP, Grill VE: Long-term exposure of rat pancreatic islets to fatty acids inhibits glucose-induced insulin secretion and biosynthesis through a glucose fatty acid cycle. J Clin Invest. 93:870-876, 1994
    • (1994) J Clin Invest. , vol.93 , pp. 870-876
    • Zhou, Y.P.1    Grill, V.E.2
  • 112
    • 0345611200 scopus 로고    scopus 로고
    • Long term elevation of free fatty acids leads to delayed processing of proinsulin and prohormone convertases 2 and 3 in the pancreatic beta cell line MIN6
    • Furukawa H, Carroll R, Steiner DF: Long term elevation of free fatty acids leads to delayed processing of proinsulin and prohormone convertases 2 and 3 in the pancreatic beta cell line MIN6. Diabetes 47 (Suppl. 1):A262, 1998
    • (1998) Diabetes , vol.47 , Issue.1 SUPPL.
    • Furukawa, H.1    Carroll, R.2    Steiner, D.F.3
  • 113
    • 0030155860 scopus 로고    scopus 로고
    • Amyloid beta-peptide and oxidative cellular injury in Alzheimer's disease
    • Mark RJ, Blanc EM, Mattson MP: Amyloid beta-peptide and oxidative cellular injury in Alzheimer's disease. Mol Neurobiol 12:211-224, 1996
    • (1996) Mol Neurobiol , vol.12 , pp. 211-224
    • Mark, R.J.1    Blanc, E.M.2    Mattson, M.P.3
  • 114
    • 0032514165 scopus 로고    scopus 로고
    • Promotion of transition metal-induced reactive oxygen species formation by beta-amyloid
    • Bondy SC, Guo-Ross SX, Truong AT: Promotion of transition metal-induced reactive oxygen species formation by beta-amyloid. Brain Res 799:91-96, 1998
    • (1998) Brain Res , vol.799 , pp. 91-96
    • Bondy, S.C.1    Guo-Ross, S.X.2    Truong, A.T.3
  • 116
    • 0028981717 scopus 로고
    • The Alzheimer's A beta peptide indures neurodegeneration and apoptotic cell death in transgenic mice
    • LaFerla FM, Tinkle BT, Bieberich CJ, Haudenschild CC, Jay G: The Alzheimer's A beta peptide indures neurodegeneration and apoptotic cell death in transgenic mice. Nat Genet 9:21-30, 1995
    • (1995) Nat Genet , vol.9 , pp. 21-30
    • LaFerla, F.M.1    Tinkle, B.T.2    Bieberich, C.J.3    Haudenschild, C.C.4    Jay, G.5
  • 118
    • 85041093955 scopus 로고    scopus 로고
    • Regulation of the apolipoprotein E by dietary lipids occurs by transcriptional and post-transcriptional mechanisms
    • Srivastava RA: Regulation of the apolipoprotein E by dietary lipids occurs by transcriptional and post-transcriptional mechanisms. Mol Cell Biochem 155:153-162, 1996
    • (1996) Mol Cell Biochem , vol.155 , pp. 153-162
    • Srivastava, R.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.