메뉴 건너뛰기




Volumn 16, Issue 3, 2016, Pages 162-179

Apoptosis in pancreatic β-islet cells in Type 2 diabetes

Author keywords

Amyloid; Apoptosis; Caspase; Hyperglycemia; Insulin; Islets of langerhans; Knockout mouse; Pro apoptotic genes; Type 2 diabetes; cells

Indexed keywords

APOPTOSIS REGULATORY PROTEIN;

EID: 85013072367     PISSN: 15128601     EISSN: 18404812     Source Type: Journal    
DOI: 10.17305/BJBMS.2016.919     Document Type: Review
Times cited : (156)

References (107)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phe-nomenon with wide-ranging implications in tissue kinetics
    • Kerr JF, Wyllie AH, Currie AR. Apoptosis: A basic biological phe-nomenon with wide-ranging implications in tissue kinetics. Br J Cancer 1972; 26(4):239-57. http://dx.doi.org/10.1038/bjc.1972.33.
    • (1972) Br J Cancer , vol.26 , Issue.4 , pp. 239-257
    • Kerr, JF1    Wyllie, AH2    Currie, AR.3
  • 2
    • 0028987251 scopus 로고
    • Dynamics of beta-cell mass in the growing rat pancreas: Estimation with a simple mathematical model
    • Finegood DT, Scaglia L, Bonner-Weir S. Dynamics of beta-cell mass in the growing rat pancreas: Estimation with a simple mathematical model. Diabetes 1995; 44(3):249-56. http://dx.doi.org/10.2337/diab.44.3.249.
    • (1995) Diabetes , vol.44 , Issue.3 , pp. 249-256
    • Finegood, DT1    Scaglia, L2    Bonner-Weir, S.3
  • 3
    • 0030903840 scopus 로고    scopus 로고
    • Apoptosis partic-ipates in the remodeling of the endocrine pancreas in the neonatal rat
    • Scaglia L, Cahill CJ, Finegood DT, Bonner-Weir S. Apoptosis partic-ipates in the remodeling of the endocrine pancreas in the neonatal rat. Endocrinology 1997; 138(4):1736-41. http://dx.doi.org/10.1210/endo.138.4.5069.
    • (1997) Endocrinology , vol.138 , Issue.4 , pp. 1736-1741
    • Scaglia, L1    Cahill, CJ2    Finegood, DT3    Bonner-Weir, S.4
  • 4
    • 0035128723 scopus 로고    scopus 로고
    • beta-cell apoptosis: Stimuli and sig-naling
    • Suppl 1
    • Mandrup-Poulsen T. beta-cell apoptosis: Stimuli and sig-naling. Diabetes 2001; 50 Suppl 1:S58-63. http://dx.doi.org/10.2337/diabetes.50.2007.S58.
    • (2001) Diabetes , vol.50 , pp. S58-S63
    • Mandrup-Poulsen, T.1
  • 5
    • 33846195875 scopus 로고    scopus 로고
    • Apoptosis in the pathophysiology of diabetes mellitus
    • Lee SC, Pervaiz S. Apoptosis in the pathophysiology of diabetes mellitus. Int J Biochem Cell Biol 2007; 39(3):497-504. http://dx.doi.org/10.1016/j.biocel.2006.09.007.
    • (2007) Int J Biochem Cell Biol , vol.39 , Issue.3 , pp. 497-504
    • Lee, SC1    Pervaiz, S.2
  • 6
    • 33747038451 scopus 로고    scopus 로고
    • Interventional strategies to pre-vent beta-cell apoptosis in islet transplantation
    • Emamaullee JA, Shapiro AM. Interventional strategies to pre-vent beta-cell apoptosis in islet transplantation. Diabetes 2006; 55(7):1907-14. http://dx.doi.org/10.2337/db05-1254.
    • (2006) Diabetes , vol.55 , Issue.7 , pp. 1907-1914
    • Emamaullee, JA1    Shapiro, AM.2
  • 7
    • 3242761599 scopus 로고    scopus 로고
    • Caspase-3 inhibitor prevents apoptosis of human islets immediately after isolation and improves islet graft function
    • Nakano M, Matsumoto I, Sawada T, Ansite J, Oberbroeckling J, Zhang HJ, et al. Caspase-3 inhibitor prevents apoptosis of human islets immediately after isolation and improves islet graft function. Pancreas 2004; 29(2):104-9. http://dx.doi.org/10.1097/00006676-200408000-00004.
    • (2004) Pancreas , vol.29 , Issue.2 , pp. 104-109
    • Nakano, M1    Matsumoto, I2    Sawada, T3    Ansite, J4    Oberbroeckling, J5    Zhang, HJ6
  • 8
    • 33746777779 scopus 로고    scopus 로고
    • Porcine islet graft function is affected by pretreat-ment with a caspase-3 inhibitor
    • Brandhorst D, Kumarasamy V, Maatoui A, Alt A, Bretzel RG, Brandhorst H. Porcine islet graft function is affected by pretreat-ment with a caspase-3 inhibitor. Cell Transplant 2006; 15(4):311-7. http://dx.doi.org/10.3727/000000006783981936.
    • (2006) Cell Transplant , vol.15 , Issue.4 , pp. 311-317
    • Brandhorst, D1    Kumarasamy, V2    Maatoui, A3    Alt, A4    Bretzel, RG5    Brandhorst, H.6
  • 9
    • 64649100459 scopus 로고    scopus 로고
    • Caspase-3 gene silencing for inhibiting apoptosis in insulinoma cells and human islets
    • Cheng G, Zhu L, Mahato RI. Caspase-3 gene silencing for inhibiting apoptosis in insulinoma cells and human islets. Mol Pharm 2008; 5(6):1093-102. http://dx.doi.org/10.1021/mp800093f.
    • (2008) Mol Pharm , vol.5 , Issue.6 , pp. 1093-1102
    • Cheng, G1    Zhu, L2    Mahato, RI.3
  • 10
    • 0030814675 scopus 로고    scopus 로고
    • Caspases: Killer proteases
    • Nicholson DW, Thornberry NA. Caspases: Killer proteases. Trends Biochem Sci 1997; 22(8):299-306. http://dx.doi.org/10.1016/S0968-0004(97)01085-2.
    • (1997) Trends Biochem Sci , vol.22 , Issue.8 , pp. 299-306
    • Nicholson, DW1    Thornberry, NA.2
  • 11
    • 0035128535 scopus 로고    scopus 로고
    • Role of apoptosis in pancreatic beta-cell death in diabetes
    • Suppl 1
    • Chandra J, Zhivotovsky B, Zaitsev S, Juntti-Berggren L, Berggren PO, Orrenius S. Role of apoptosis in pancreatic beta-cell death in diabetes. Diabetes 2001; 50 Suppl 1:S44-7. http://dx.doi.org/10.2337/diabetes.50.2007.S44.
    • (2001) Diabetes , vol.50 , pp. S44-S47
    • Chandra, J1    Zhivotovsky, B2    Zaitsev, S3    Juntti-Berggren, L4    Berggren, PO5    Orrenius, S.6
  • 12
    • 0031754828 scopus 로고    scopus 로고
    • Mechanisms of CD95 (APO-1/Fas)-mediated apoptosis
    • Peter ME, Krammer PH. Mechanisms of CD95 (APO-1/Fas)-mediated apoptosis. Curr Opin Immunol 1998; 10(5):545-51. http://dx.doi.org/10.1016/S0952-7915(98)80222-7.
    • (1998) Curr Opin Immunol , vol.10 , Issue.5 , pp. 545-551
    • Peter, ME1    Krammer, PH.2
  • 13
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • Sakahira H, Enari M, Nagata S. Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis. Nature 1998; 391(6662):96-9. http://dx.doi.org/10.1038/34214.
    • (1998) Nature , vol.391 , Issue.6662 , pp. 96-99
    • Sakahira, H1    Enari, M2    Nagata, S.3
  • 14
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross A, McDonnell JM, Korsmeyer SJ. BCL-2 family members and the mitochondria in apoptosis. Genes Dev 1999; 13(15):1899-911. http://dx.doi.org/10.1101/gad.13.15.1899.
    • (1999) Genes Dev , vol.13 , Issue.15 , pp. 1899-1911
    • Gross, A1    McDonnell, JM2    Korsmeyer, SJ.3
  • 15
    • 20444430478 scopus 로고    scopus 로고
    • Apoptotic pathways: Ten minutes to dead
    • Green DR. Apoptotic pathways: Ten minutes to dead. Cell 2005; 121(5):671-4. http://dx.doi.org/10.1016/j.cell.2005.05.019.
    • (2005) Cell , vol.121 , Issue.5 , pp. 671-674
    • Green, DR.1
  • 16
    • 0034982387 scopus 로고    scopus 로고
    • High glucose causes apoptosis in cultured human pancreatic islets of Langerhans: A potential role for regulation of specific Bcl family genes toward an apoptotic cell death program
    • Federici M, Hribal M, Perego L, Ranalli M, Caradonna Z, Perego C, et al. High glucose causes apoptosis in cultured human pancreatic islets of Langerhans: A potential role for regulation of specific Bcl family genes toward an apoptotic cell death program. Diabetes 2001; 50(6):1290-301. http://dx.doi.org/10.2337/diabetes.50.6.1290.
    • (2001) Diabetes , vol.50 , Issue.6 , pp. 1290-1301
    • Federici, M1    Hribal, M2    Perego, L3    Ranalli, M4    Caradonna, Z5    Perego, C6
  • 17
    • 0037204952 scopus 로고    scopus 로고
    • The Fas signaling pathway: More than a paradigm
    • Wajant H. The Fas signaling pathway: More than a paradigm. Science 2002; 296(5573):1635-6. http://dx.doi.org/10.1126/science.1071553.
    • (2002) Science , vol.296 , Issue.5573 , pp. 1635-1636
    • Wajant, H.1
  • 18
    • 0027145632 scopus 로고
    • Molecular cloning and expression of the Fas ligand, a novel member of the tumor necrosis factor family
    • Suda T, Takahashi T, Golstein P, Nagata S. Molecular cloning and expression of the Fas ligand, a novel member of the tumor necrosis factor family. Cell 1993; 75(6):1169-78. http://dx.doi.org/10.1016/0092-8674(93)90326-L.
    • (1993) Cell , vol.75 , Issue.6 , pp. 1169-1178
    • Suda, T1    Takahashi, T2    Golstein, P3    Nagata, S.4
  • 19
    • 21244498127 scopus 로고    scopus 로고
    • Transgenic expression of dominant-negative Fas-associated death domain protein in beta cells protects against Fas ligand-induced apopto-sis and reduces spontaneous diabetes in nonobese diabetic mice
    • Allison J, Thomas HE, Catterall T, Kay TW, Strasser A. Transgenic expression of dominant-negative Fas-associated death domain protein in beta cells protects against Fas ligand-induced apopto-sis and reduces spontaneous diabetes in nonobese diabetic mice. J Immunol 2005; 175(1):293-301. http://dx.doi.org/10.4049/jimmunol.175.1.293.
    • (2005) J Immunol , vol.175 , Issue.1 , pp. 293-301
    • Allison, J1    Thomas, HE2    Catterall, T3    Kay, TW4    Strasser, A.5
  • 20
    • 43549100675 scopus 로고    scopus 로고
    • Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis
    • Haataja L, Gurlo T, Huang CJ, Butler PC. Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis. Endocr Rev 2008; 29(3):303-16. http://dx.doi.org/10.1210/er.2007-0037.
    • (2008) Endocr Rev , vol.29 , Issue.3 , pp. 303-316
    • Haataja, L1    Gurlo, T2    Huang, CJ3    Butler, PC.4
  • 21
    • 0024160877 scopus 로고
    • Banting lecture 1988. Role of insulin resistance in human disease
    • Reaven GM. Banting lecture 1988. Role of insulin resistance in human disease. Diabetes 1988; 37(12):1595-607. http://dx.doi.org/10.2337/diab.37.12.1595.
    • (1988) Diabetes , vol.37 , Issue.12 , pp. 1595-1607
    • Reaven, GM.1
  • 22
    • 0037219411 scopus 로고    scopus 로고
    • Beta-cell deficit and increased beta-cell apoptosis in humans with type 2 diabetes
    • Butler AE, Janson J, Bonner-Weir S, Ritzel R, Rizza RA, Butler PC. Beta-cell deficit and increased beta-cell apoptosis in humans with type 2 diabetes. Diabetes 2003; 52(1):102-10. http://dx.doi.org/10.2337/diabetes.52.1.102.
    • (2003) Diabetes , vol.52 , Issue.1 , pp. 102-110
    • Butler, AE1    Janson, J2    Bonner-Weir, S3    Ritzel, R4    Rizza, RA5    Butler, PC.6
  • 23
    • 0034042959 scopus 로고    scopus 로고
    • Islet growth and development in the adult
    • Bonner-Weir S. Islet growth and development in the adult. J Mol Endocrinol 2000; 24(3):297-302. http://dx.doi.org/10.1677/jme.0.0240297.
    • (2000) J Mol Endocrinol , vol.24 , Issue.3 , pp. 297-302
    • Bonner-Weir, S.1
  • 24
    • 8744272467 scopus 로고    scopus 로고
    • Pancreatic islets from type 2 diabetic patients have functional defects and increased apoptosis that are ameliorated by metformin
    • Marchetti P, Del Guerra S, Marselli L, Lupi R, Masini M, Pollera M, et al. Pancreatic islets from type 2 diabetic patients have functional defects and increased apoptosis that are ameliorated by metformin. J Clin Endocrinol Metab 2004; 89(11):5535-41. http://dx.doi.org/10.1210/jc.2004-0150.
    • (2004) J Clin Endocrinol Metab , vol.89 , Issue.11 , pp. 5535-5541
    • Marchetti, P1    Del Guerra, S2    Marselli, L3    Lupi, R4    Masini, M5    Pollera, M6
  • 25
    • 0031040649 scopus 로고    scopus 로고
    • Gelatinases and inhibitors of gelatinases in pancreatic islets and islet cell tumors
    • Tomita T, Iwata K. Gelatinases and inhibitors of gelatinases in pancreatic islets and islet cell tumors. Modern Pathol 1997; 10(1):47-54.
    • (1997) Modern Pathol , vol.10 , Issue.1 , pp. 47-54
    • Tomita, T1    Iwata, K.2
  • 26
    • 14644396532 scopus 로고    scopus 로고
    • Matrix metalloproteinases 2 and 9 are dispensable for pancreatic islet formation and function in vivo
    • 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(3):694-701. http://dx.doi.org/10.2337/diabetes.54.3.694.
    • (2005) Diabetes , vol.54 , Issue.3 , pp. 694-701
    • Perez, SE1    Cano, DA2    Dao-Pick, T3    Rougier, JP4    Werb, Z5    Hebrok, M.6
  • 27
    • 0032536519 scopus 로고    scopus 로고
    • Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis
    • 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(4):587-600. http://dx.doi.org/10.1084/jem.187.4.587.
    • (1998) J Exp Med , vol.187 , Issue.4 , pp. 587-600
    • Hirata, H1    Takahashi, A2    Kobayashi, S3    Yonehara, S4    Sawai, H5    Okazaki, T6
  • 28
    • 0028990125 scopus 로고
    • Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari M, Quan LT, O’Rourke K, Desnoyers S, Zeng Z, Beidler DR, et al. Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 1995; 81(5):801-9. http://dx.doi.org/10.1016/0092-8674(95)90541-3.
    • (1995) Cell , vol.81 , Issue.5 , pp. 801-809
    • Tewari, M1    Quan, LT2    O’Rourke, K3    Desnoyers, S4    Zeng, Z5    Beidler, DR6
  • 29
    • 0036199634 scopus 로고    scopus 로고
    • Improved detection of apoptotic cells in archival paraffin sections: Immunohistochemistry using antibod-ies to cleaved caspase 3
    • Gown AM, Willingham MC. Improved detection of apoptotic cells in archival paraffin sections: Immunohistochemistry using antibod-ies to cleaved caspase 3. J Histochem Cytochem 2002;50(4):449-54. http://dx.doi.org/10.1177/002215540205000401.
    • (2002) J Histochem Cytochem , vol.50 , Issue.4 , pp. 449-454
    • Gown, AM1    Willingham, MC.2
  • 30
    • 0029125701 scopus 로고
    • Protease activation during apoptosis: Death by a thousand cuts?
    • Martin SJ, Green DR. Protease activation during apoptosis: Death by a thousand cuts? Cell 1995; 82(3):349-52. http://dx.doi.org/10.1016/0092-8674(95)90422-0.
    • (1995) Cell , vol.82 , Issue.3 , pp. 349-352
    • Martin, SJ1    Green, DR.2
  • 31
    • 77954791270 scopus 로고    scopus 로고
    • Immunocytochemical localisation of caspase-3 in pancreatic islets from type 2 diabetic subjects
    • Tomita T. Immunocytochemical localisation of caspase-3 in pancreatic islets from type 2 diabetic subjects. Pathology 2010; 42(5):432-7. http://dx.doi.org/10.3109/00313025.2010.493863.
    • (2010) Pathology , vol.42 , Issue.5 , pp. 432-437
    • Tomita, T.1
  • 32
    • 0033770540 scopus 로고    scopus 로고
    • Life and death of the pancreatic beta cells
    • Bonner-Weir S. Life and death of the pancreatic beta cells. Trends Endocrinol Metab 2000; 11(9):375-8. http://dx.doi.org/10.1016/S1043-2760(00)00305-2.
    • (2000) Trends Endocrinol Metab , vol.11 , Issue.9 , pp. 375-378
    • Bonner-Weir, S.1
  • 33
    • 58149337276 scopus 로고    scopus 로고
    • Islets in type 2 diabetes: In honor of Dr. Robert C. Turner
    • Bonner-Weir S, O’Brien TD. Islets in type 2 diabetes: In honor of Dr. Robert C. Turner. Diabetes 2008; 57(11):2899-904. http://dx.doi.org/10.2337/db07-1842.
    • (2008) Diabetes , vol.57 , Issue.11 , pp. 2899-2904
    • Bonner-Weir, S1    O’Brien, TD.2
  • 34
    • 12344323484 scopus 로고    scopus 로고
    • Type 2 diabetes-a matter of beta-cell life and death?
    • Rhodes CJ. Type 2 diabetes-a matter of beta-cell life and death? Science 2005; 307(5708):380-4. http://dx.doi.org/10.1126/science.1104345.
    • (2005) Science , vol.307 , Issue.5708 , pp. 380-384
    • Rhodes, CJ.1
  • 35
    • 85046915669 scopus 로고    scopus 로고
    • Immunocytochemical localization of cleaved caspase-3 in pancreatic islets from type 1 diabetic subjects
    • Tomita T. Immunocytochemical localization of cleaved caspase-3 in pancreatic islets from type 1 diabetic subjects. Islets 2010; 2(1):24-9. http://dx.doi.org/10.4161/isl.2.1.10041.
    • (2010) Islets , vol.2 , Issue.1 , pp. 24-29
    • Tomita, T.1
  • 36
    • 0031905990 scopus 로고    scopus 로고
    • TUNEL apoptotic cell detection in tissue sections: Critical evaluation and improvement
    • Labat-Moleur F, Guillermet C, Lorimier P, Robert C, Lantuejoul S, Brambilla E, et al. TUNEL apoptotic cell detection in tissue sections: Critical evaluation and improvement. J Histochem Cytochem 1998; 46(3):327-34. http://dx.doi.org/10.1177/002215549804600306.
    • (1998) J Histochem Cytochem , vol.46 , Issue.3 , pp. 327-334
    • Labat-Moleur, F1    Guillermet, C2    Lorimier, P3    Robert, C4    Lantuejoul, S5    Brambilla, E6
  • 37
    • 0037314551 scopus 로고    scopus 로고
    • Comparison of immunohistochemistry for activated caspase-3 and cleaved cytokeratin 18 with the TUNEL method for quantification of apoptosis in histological sections of PC-3 subcuta-neous xenografts
    • Duan WR, Garner DS, Williams SD, Funckes-Shippy CL, Spath IS, Blomme EA. Comparison of immunohistochemistry for activated caspase-3 and cleaved cytokeratin 18 with the TUNEL method for quantification of apoptosis in histological sections of PC-3 subcuta-neous xenografts. J Pathol 2003; 199(2):221-8. http://dx.doi.org/10.1002/path.1289.
    • (2003) J Pathol , vol.199 , Issue.2 , pp. 221-228
    • Duan, WR1    Garner, DS2    Williams, SD3    Funckes-Shippy, CL4    Spath, IS5    Blomme, EA.6
  • 38
    • 85046915675 scopus 로고    scopus 로고
    • Cleaved caspase-3 immunocytochemical staining for pancreatic islets and pancreatic endocrine tumors: A potential marker for biological malignancy
    • Tomita T. Cleaved caspase-3 immunocytochemical staining for pancreatic islets and pancreatic endocrine tumors: A potential marker for biological malignancy. Islets 2010; 2(2):82-8. http://dx.doi.org/10.4161/isl.2.2.10807.
    • (2010) Islets , vol.2 , Issue.2 , pp. 82-88
    • Tomita, T.1
  • 39
    • 72949142071 scopus 로고
    • Amyloidosis of the islets of Langerhans. A restudy of islet hyalin in diabetic and non-diabetic individuals
    • 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(1):49-59.
    • (1961) Am J Pathol , vol.38 , Issue.1 , pp. 49-59
    • Ehrlich, JC1    Ratner, IM.2
  • 40
    • 0034632806 scopus 로고    scopus 로고
    • Islet amyloid and type 2 diabetes mellitus
    • Höppener JW, Ahrén B, Lips CJ. Islet amyloid and type 2 diabetes mellitus. N Engl J Med 2000; 343(9):411-9.
    • (2000) N Engl J Med , vol.343 , Issue.9 , pp. 411-419
    • Höppener, JW1    Ahrén, B2    Lips, CJ.3
  • 41
    • 4043171124 scopus 로고    scopus 로고
    • Islet amy-loid: A critical entity in the pathogenesis of type 2 diabetes
    • Hull RL, Westermark GT, Westermark P, Kahn SE. Islet amy-loid: A critical entity in the pathogenesis of type 2 diabetes. J Clin Endocrinol Metab 2004; 89(8):3629-43. http://dx.doi.org/10.1210/jc.2004-0405.
    • (2004) J Clin Endocrinol Metab , vol.89 , Issue.8 , pp. 3629-3643
    • Hull, RL1    Westermark, GT2    Westermark, P3    Kahn, SE.4
  • 42
    • 0042822112 scopus 로고    scopus 로고
    • Increased beta-cell apop-tosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: Evidence for role of islet amyloid formation rather than direct action of amyloid
    • Butler AE, Janson J, Soeller WC, Butler PC. Increased beta-cell apop-tosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: Evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 2003; 52(9):2304-14. http://dx.doi.org/10.2337/diabetes.52.9.2304.
    • (2003) Diabetes , vol.52 , Issue.9 , pp. 2304-2314
    • Butler, AE1    Janson, J2    Soeller, WC3    Butler, PC.4
  • 43
    • 0023579739 scopus 로고
    • Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients
    • Cooper GJ, Willis AC, Clark A, Turner RC, Sim RB, Reid KB. Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc Natl Acad Sci U S A 1987; 84(23):8628-32. http://dx.doi.org/10.1073/pnas.84.23.8628.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , Issue.23 , pp. 8628-8632
    • Cooper, GJ1    Willis, AC2    Clark, A3    Turner, RC4    Sim, RB5    Reid, KB.6
  • 44
    • 0023025399 scopus 로고
    • A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas
    • 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(3):827-31. http://dx.doi.org/10.1016/0006-291X(86)90708-4.
    • (1986) Biochem Biophys Res Commun , vol.140 , Issue.3 , pp. 827-831
    • Westermark, P1    Wernstedt, C2    Wilander, E3    Sletten, K.4
  • 45
    • 0032969276 scopus 로고    scopus 로고
    • Islet amyloid: A long-rec-ognized but underappreciated pathological feature of type 2 diabe-tes
    • Kahn SE, Andrikopoulos S, Verchere CB. Islet amyloid: A long-rec-ognized but underappreciated pathological feature of type 2 diabe-tes. Diabetes 1999; 48(2):241-53. http://dx.doi.org/10.2337/diabetes.48.2.241.
    • (1999) Diabetes , vol.48 , Issue.2 , pp. 241-253
    • Kahn, SE1    Andrikopoulos, S2    Verchere, CB.3
  • 46
    • 0037800669 scopus 로고    scopus 로고
    • Amylin replacement with Pramlintide in type 1 and type 2 diabetes: A physiological approach to overcome a barrier with insulin therapy
    • Buse JB, Weyer C, Maggs DC. Amylin replacement with Pramlintide in type 1 and type 2 diabetes: A physiological approach to overcome a barrier with insulin therapy. Clin Diabetes 2002; 20(3):137-44. http://dx.doi.org/10.2337/diaclin.20.3.137.
    • (2002) Clin Diabetes , vol.20 , Issue.3 , pp. 137-144
    • Buse, JB1    Weyer, C2    Maggs, DC.3
  • 47
    • 0036751254 scopus 로고    scopus 로고
    • The human amylin analog, pramlintide, reduces postprandial hyperglu-cagonemia in patients with type 2 diabetes mellitus
    • Fineman M, Weyer C, Maggs DG, Strobel S, Kolterman OG. The human amylin analog, pramlintide, reduces postprandial hyperglu-cagonemia in patients with type 2 diabetes mellitus. Horm Metab Res 2002; 34(9):504-8. http://dx.doi.org/10.1055/s-2002-34790.
    • (2002) Horm Metab Res , vol.34 , Issue.9 , pp. 504-508
    • Fineman, M1    Weyer, C2    Maggs, DG3    Strobel, S4    Kolterman, OG.5
  • 48
    • 0033130649 scopus 로고    scopus 로고
    • Clinical implications of amylin and amylin deficiency
    • Kruger DF, Gatcomb PM, Owen SK. Clinical implications of amylin and amylin deficiency. Diabetes Educ 1999; 25(3):389-97. http://dx.doi.org/10.1177/014572179902500310.
    • (1999) Diabetes Educ , vol.25 , Issue.3 , pp. 389-397
    • Kruger, DF1    Gatcomb, PM2    Owen, SK.3
  • 49
    • 0034850444 scopus 로고    scopus 로고
    • 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
    • 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(14):1353-73. http://dx.doi.org/10.2174/1381612013397357.
    • (2001) Curr Pharm Des , vol.7 , Issue.14 , pp. 1353-1373
    • Weyer, C1    Maggs, DG2    Young, AA3    Kolterman, OG.4
  • 50
    • 84864400342 scopus 로고    scopus 로고
    • Islet amyloid polypeptide in pancreatic islets from type 2 diabetic subjects
    • Tomita T. Islet amyloid polypeptide in pancreatic islets from type 2 diabetic subjects. Islets 2012; 4(3):223-32. http://dx.doi.org/10.4161/isl.20477.
    • (2012) Islets , vol.4 , Issue.3 , pp. 223-232
    • Tomita, T.1
  • 51
    • 1542375103 scopus 로고    scopus 로고
    • Islet amyloid: A complication of islet dysfunction or an aetiological factor in Type 2 diabetes?
    • Clark A, Nilsson MR. Islet amyloid: A complication of islet dysfunction or an aetiological factor in Type 2 diabetes? Diabetologia 2004; 47(2):157-69. http://dx.doi.org/10.1007/s00125-003-1304-4.
    • (2004) Diabetologia , vol.47 , Issue.2 , pp. 157-169
    • Clark, A1    Nilsson, MR.2
  • 52
    • 0024213009 scopus 로고
    • Islet amyloid, increased A-cells, reduced B-cells and exocrine fibrosis quantitative changes in the pancreas in type 2 diabetes
    • 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(4):151-9.
    • (1988) Diabetes Res , vol.9 , Issue.4 , pp. 151-159
    • Clark, A1    Wells, CA2    Buley, ID3    Cruickshank, JK4    Vanhegan, RI5    Matthews, DR6
  • 53
    • 79954543511 scopus 로고    scopus 로고
    • ß-cell loss and ß-cell apoptosis in human type 2 diabetes are related to islet amyloid deposition
    • Jurgens CA, Toukatly MN, Fligner CL, Udayasankar J, Subramanian SL, Zraika S, et al. ß-cell loss and ß-cell apoptosis in human type 2 diabetes are related to islet amyloid deposition. Am J Pathol 2011; 178(6):2632-40. http://dx.doi.org/10.1016/j.ajpath.2011.02.036.
    • (2011) Am J Pathol , vol.178 , Issue.6 , pp. 2632-2640
    • Jurgens, CA1    Toukatly, MN2    Fligner, CL3    Udayasankar, J4    Subramanian, SL5    Zraika, S6
  • 54
    • 0030044018 scopus 로고    scopus 로고
    • Pore formation by the cytotoxic islet amyloid peptide amylin
    • Mirzabekov TA, Lin MC, Kagan BL. Pore formation by the cytotoxic islet amyloid peptide amylin. J Biol Chem 1996; 271(4):1988-92. http://dx.doi.org/10.1074/jbc.271.4.1988.
    • (1996) J Biol Chem , vol.271 , Issue.4 , pp. 1988-1992
    • Mirzabekov, TA1    Lin, MC2    Kagan, BL.3
  • 55
    • 76149102617 scopus 로고    scopus 로고
    • Evidence for proteotoxic-ity in beta cells in type 2 diabetes: Toxic islet amyloid oligomers from intracellularly in the secretory pathway
    • O’Brien TD, Glabe CG, Butler PC. Evidence for proteotoxic-ity in beta cells in type 2 diabetes: Toxic islet amyloid oligomers from intracellularly in the secretory pathway. Am J Pathol 2010; 176(2):861-9.
    • (2010) Am J Pathol , vol.176 , Issue.2 , pp. 861-869
    • O’Brien, TD1    Glabe, CG2    Butler, PC.3
  • 56
    • 0037167613 scopus 로고    scopus 로고
    • Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes
    • 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(38):11338-43. http://dx.doi.org/10.1021/bi020314u.
    • (2002) Biochemistry , vol.41 , Issue.38 , pp. 11338-11343
    • Anguiano, M1    Nowak, RJ2    Lansbury, PT3
  • 57
    • 43149118349 scopus 로고    scopus 로고
    • Membrane damage by human islet amyloid poly-peptide through fibril growth at the membrane
    • Engel MF, Khemtémourian L, Kleijer CC, Meeldijk HJ, Jacobs J, Verkleij AJ, et al. Membrane damage by human islet amyloid poly-peptide through fibril growth at the membrane. Proc Natl Acad Sci U S A 2008; 105(16):6033-8. http://dx.doi.org/10.1073/pnas.0708354105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.16 , pp. 6033-6038
    • Engel, MF1    Khemtémourian, L2    Kleijer, CC3    Meeldijk, HJ4    Jacobs, J5    Verkleij, AJ6
  • 58
    • 0028960483 scopus 로고
    • Defective maturation and function of antigen-presenting cells in type 1 diabetes
    • Jansen A, van Hagen M, Drexhage HA. Defective maturation and function of antigen-presenting cells in type 1 diabetes. Lancet 1995; 345(8948):491-2. http://dx.doi.org/10.1016/S0140-6736(95)90586-3.
    • (1995) Lancet , vol.345 , Issue.8948 , pp. 491-492
    • Jansen, A1    van Hagen, M2    Drexhage, HA.3
  • 59
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • 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(5618):486-9. http://dx.doi.org/10.1126/science.1079469.
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R1    Head, E2    Thompson, JL3    McIntire, TM4    Milton, SC5    Cotman, CW6
  • 60
    • 0038015599 scopus 로고    scopus 로고
    • Replication increases beta-cell vulnerability to human islet amyloid polypeptide-induced apoptosis
    • Ritzel RA, Butler PC. Replication increases beta-cell vulnerability to human islet amyloid polypeptide-induced apoptosis. Diabetes 2003; 52:1701-8. http://dx.doi.org/10.2337/diabetes.52.7.1701.
    • (2003) Diabetes , vol.52 , pp. 1701-1708
    • Ritzel, RA1    Butler, PC.2
  • 61
    • 0037300155 scopus 로고    scopus 로고
    • Amylin in human adult pancreatic islets
    • http://dx.doi.org/10.1080/0031302021000062299
    • Tomita T. Amylin in human adult pancreatic islets. Pathology 2003; 35(1):34-6. http://dx.doi.org/10.1097/01268031-200335010-00005, http://dx.doi.org/10.1080/0031302021000062299.
    • (2003) Pathology , vol.35 , Issue.1 , pp. 34-36
    • Tomita, T.1
  • 62
    • 0016227560 scopus 로고
    • Effect of alloxan on insulin secretion in isolated rat islets perifused in vitro
    • Tomita T, Lacy PE, Matschinsky FM, McDaniel ML. Effect of alloxan on insulin secretion in isolated rat islets perifused in vitro. Diabetes 1974; 23(6):517-24. http://dx.doi.org/10.2337/diab.23.6.517.
    • (1974) Diabetes , vol.23 , Issue.6 , pp. 517-524
    • Tomita, T1    Lacy, PE2    Matschinsky, FM3    McDaniel, ML.4
  • 63
    • 0017711712 scopus 로고
    • Interaction of cyclic AMP and alloxan on insulin secretion in isolated rat islets perifused in vitro
    • Tomita T, Scarpelli DG. Interaction of cyclic AMP and alloxan on insulin secretion in isolated rat islets perifused in vitro. Endocrinology 1977; 100(5):1327-33. http://dx.doi.org/10.1210/endo-100-5-1327.
    • (1977) Endocrinology , vol.100 , Issue.5 , pp. 1327-1333
    • Tomita, T1    Scarpelli, DG.2
  • 64
    • 33644749322 scopus 로고    scopus 로고
    • Mechanisms of pancreatic beta-cell death in type 1 and type 2 diabetes: Many differences, few similarities
    • Suppl 2
    • Cnop M, Welsh N, Jonas JC, Jörns A, Lenzen S, Eizirik DL. Mechanisms of pancreatic beta-cell death in type 1 and type 2 diabetes: Many differences, few similarities. Diabetes 2005; 54 Suppl 2:S97-107. http://dx.doi.org/10.2337/diabetes.54.suppl_2.S97.
    • (2005) Diabetes , vol.54 , pp. S97-107
    • Cnop, M1    Welsh, N2    Jonas, JC3    Jörns, A4    Lenzen, S5    Eizirik, DL.6
  • 65
    • 33644747390 scopus 로고    scopus 로고
    • Mechanisms of beta-cell death in type 2 diabetes
    • Suppl 2
    • Donath MY, Ehses JA, Maedler K, Schumann DM, Ellingsgaard H, Eppler E, et al. Mechanisms of beta-cell death in type 2 diabetes. Diabetes 2005; 54 Suppl 2:S108-13. http://dx.doi.org/10.2337/diabetes.54.suppl_2.S108.
    • (2005) Diabetes , vol.54 , pp. S108-S113
    • Donath, MY1    Ehses, JA2    Maedler, K3    Schumann, DM4    Ellingsgaard, H5    Eppler, E6
  • 66
    • 0022975389 scopus 로고
    • Differential regulation of glucokinase activity in pancreatic islets and liver of the rat
    • Bedoya FJ, Matschinsky FM, Shimizu T, O’Neil JJ, Appel MC. Differential regulation of glucokinase activity in pancreatic islets and liver of the rat. J Biol Chem 1986; 261(23):10760-4.
    • (1986) J Biol Chem , vol.261 , Issue.23 , pp. 10760-10764
    • Bedoya, FJ1    Matschinsky, FM2    Shimizu, T3    O’Neil, JJ4    Appel, MC.5
  • 67
    • 0025334163 scopus 로고
    • Glucokinase as glucose sensor and metabolic signal generator in pancreatic beta-cells and hepatocytes
    • http://dx.doi.org/10.2337/diabetes.39.6.647
    • Matschinsky FM. Glucokinase as glucose sensor and metabolic signal generator in pancreatic beta-cells and hepatocytes. Diabetes 1990; 39(6):647-52. http://dx.doi.org/10.2337/diab.39.6.647, http://dx.doi.org/10.2337/diabetes.39.6.647.
    • (1990) Diabetes , vol.39 , Issue.6 , pp. 647-652
    • Matschinsky, FM.1
  • 68
    • 0027358380 scopus 로고
    • Glucokinase as pancreatic beta cell glucose sensor and diabetes gene
    • Matschinsky F, Liang Y, Kesavan P, Wang L, Froguel P, Velho G, et al. Glucokinase as pancreatic beta cell glucose sensor and diabetes gene. J Clin Invest 1993; 92(5):2092-8. http://dx.doi.org/10.1172/JCI116809.
    • (1993) J Clin Invest , vol.92 , Issue.5 , pp. 2092-2098
    • Matschinsky, F1    Liang, Y2    Kesavan, P3    Wang, L4    Froguel, P5    Velho, G6
  • 69
    • 0023932670 scopus 로고
    • Control of glucose phos-phorylation and glucose usage in clonal insulinoma cells
    • Shimizu T, Knowles BB, Matschinsky FM. Control of glucose phos-phorylation and glucose usage in clonal insulinoma cells. Diabetes 1988; 37(5):563-8. http://dx.doi.org/10.2337/diab.37.5.563.
    • (1988) Diabetes , vol.37 , Issue.5 , pp. 563-568
    • Shimizu, T1    Knowles, BB2    Matschinsky, FM.3
  • 70
    • 33244466564 scopus 로고    scopus 로고
    • Glucose-sensing mechanisms in pancreatic beta-cells
    • MacDonald PE, Joseph JW, Rorsman P. Glucose-sensing mechanisms in pancreatic beta-cells. Philos Trans R Soc Lond B Biol Sci 2005; 360(1464):2211-25. http://dx.doi.org/10.1098/rstb.2005.1762.
    • (2005) Philos Trans R Soc Lond B Biol Sci , vol.360 , Issue.1464 , pp. 2211-2225
    • MacDonald, PE1    Joseph, JW2    Rorsman, P.3
  • 71
    • 0028859374 scopus 로고
    • Human and rat beta cells differ in glucose trans-porter but not in glucokinase gene expression
    • De Vos A, Heimberg H, Quartier E, Huypens P, Bouwens L, Pipeleers D, et al. Human and rat beta cells differ in glucose trans-porter but not in glucokinase gene expression. J Clin Invest 1995; 96(5):2489-95. http://dx.doi.org/10.1172/JCI118308.
    • (1995) J Clin Invest , vol.96 , Issue.5 , pp. 2489-2495
    • De Vos, A1    Heimberg, H2    Quartier, E3    Huypens, P4    Bouwens, L5    Pipeleers, D6
  • 72
    • 0027186032 scopus 로고
    • Mammalian glucokinase and its gene
    • Iynedjian PB. Mammalian glucokinase and its gene. Biochem J 1993; 293:1-13. http://dx.doi.org/10.1042/bj2930001.
    • (1993) Biochem J , vol.293 , pp. 1-13
    • Iynedjian, PB.1
  • 73
    • 0029071517 scopus 로고
    • Metabolic coupling factors in pancreatic beta-cell signal transduction
    • Newgard CB, McGarry JD. Metabolic coupling factors in pancreatic beta-cell signal transduction. Annu Rev Biochem 1995; 64:689-719. http://dx.doi.org/10.1146/annurev.bi.64.070195.003353.
    • (1995) Annu Rev Biochem , vol.64 , pp. 689-719
    • Newgard, CB1    McGarry, JD.2
  • 74
    • 77952539966 scopus 로고    scopus 로고
    • Glucose sensing in the pancreatic beta cells: A computational systems analysis
    • Fridlyand L, Philson LH. Glucose sensing in the pancreatic beta cells: A computational systems analysis. Theor Biol Med Model 2010; 7(15):1-44. http://dx.doi.org/10.1186/1742-4682-7-15.
    • (2010) Theor Biol Med Model , vol.7 , Issue.15 , pp. 1-44
    • Fridlyand, L1    Philson, LH.2
  • 75
    • 0026608764 scopus 로고
    • Close linkage of glucokinase locus on chromosome 7p to ear-ly-onset non-insulin-dependent diabetes mellitus
    • Froguel P, Vaxillaire M, Sun F, Velho G, Zouali H, Butel MO, et al. Close linkage of glucokinase locus on chromosome 7p to ear-ly-onset non-insulin-dependent diabetes mellitus. Nature 1992; 356(6365):162-4. http://dx.doi.org/10.1038/356162a0.
    • (1992) Nature , vol.356 , Issue.6365 , pp. 162-164
    • Froguel, P1    Vaxillaire, M2    Sun, F3    Velho, G4    Zouali, H5    Butel, MO6
  • 76
    • 27844525503 scopus 로고    scopus 로고
    • Monogenic syndromes of abnormal glucose homeostasis: Clinical review and relevance to the understanding of the pathology of insulin resistance and beta cell failure
    • Porter JR, Barrett TG. Monogenic syndromes of abnormal glucose homeostasis: Clinical review and relevance to the understanding of the pathology of insulin resistance and beta cell failure. J Med Genet 2005; 42(12):893-902. http://dx.doi.org/10.1136/jmg.2005.030791.
    • (2005) J Med Genet , vol.42 , Issue.12 , pp. 893-902
    • Porter, JR1    Barrett, TG.2
  • 77
    • 0031892442 scopus 로고    scopus 로고
    • Maturity-onset diabetes of the young: A clinical history
    • Tattersall R. Maturity-onset diabetes of the young: A clinical history. Diabet Med 1998; 15(1):11-4. http://dx.doi.org/10.1002/(SICI)1096-9136(199801)15:1 <11:AID-DIA561>3.0.CO;2-0.
    • (1998) Diabet Med , vol.15 , Issue.1 , pp. 11-14
    • Tattersall, R.1
  • 79
    • 0026511753 scopus 로고
    • Beta-cell dysfunction induced by chronic hyperglycemia. Current ideas on mechanism of impaired glucose-induced insulin secretion
    • Leahy JL, Bonner-Weir S, Weir GC. Beta-cell dysfunction induced by chronic hyperglycemia. Current ideas on mechanism of impaired glucose-induced insulin secretion. Diabetes Care 1992; 15(3):442-55. http://dx.doi.org/10.2337/diacare.15.3.442.
    • (1992) Diabetes Care , vol.15 , Issue.3 , pp. 442-455
    • Leahy, JL1    Bonner-Weir, S2    Weir, GC.3
  • 80
    • 24144490962 scopus 로고    scopus 로고
    • Exposure to chronic high glucose induces beta-cell apoptosis through decreased interaction of glucokinase with mitochondria: Downregulation of glucokinase in pancreatic beta-cells
    • Kim WH, Lee JW, Suh YH, Hong SH, Choi JS, Lim JH, et al. Exposure to chronic high glucose induces beta-cell apoptosis through decreased interaction of glucokinase with mitochondria: Downregulation of glucokinase in pancreatic beta-cells. Diabetes 2005; 54(9):2602-11. http://dx.doi.org/10.2337/diabetes.54.9.2602.
    • (2005) Diabetes , vol.54 , Issue.9 , pp. 2602-2611
    • Kim, WH1    Lee, JW2    Suh, YH3    Hong, SH4    Choi, JS5    Lim, JH6
  • 81
    • 1542616703 scopus 로고    scopus 로고
    • Proteins of the bcl-2 family in apoptosis signalling: From mechanistic insights to therapeutic opportunities
    • Chan SL, Yu VC. Proteins of the bcl-2 family in apoptosis signalling: From mechanistic insights to therapeutic opportunities. Clin Exp Pharmacol Physiol 2004; 31(3):119-28. http://dx.doi.org/10.1111/j.1440-1681.2004.03975.x.
    • (2004) Clin Exp Pharmacol Physiol , vol.31 , Issue.3 , pp. 119-128
    • Chan, SL1    Yu, VC.2
  • 82
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner MO. The biochemistry of apoptosis. Nature 2000; 407(6805):770-6. http://dx.doi.org/10.1038/35037710.
    • (2000) Nature , vol.407 , Issue.6805 , pp. 770-776
    • Hengartner, MO.1
  • 83
    • 15444380436 scopus 로고    scopus 로고
    • Synergetic inhibition of tumor necrosis factor-related apoptosis-in-ducing ligand-induced apoptosis in human pancreatic beta cells by Bcl-2 and X-linked inhibitor of apoptosis
    • Ou D, Wang X, Metzger DL, James RF, Pozzilli P, Plesner A, et al. Synergetic inhibition of tumor necrosis factor-related apoptosis-in-ducing ligand-induced apoptosis in human pancreatic beta cells by Bcl-2 and X-linked inhibitor of apoptosis. Hum Immunol 2005; 66(3):274-84. http://dx.doi.org/10.1016/j.humimm.2004.12.002.
    • (2005) Hum Immunol , vol.66 , Issue.3 , pp. 274-284
    • Ou, D1    Wang, X2    Metzger, DL3    James, RF4    Pozzilli, P5    Plesner, A6
  • 84
    • 0034456628 scopus 로고    scopus 로고
    • Cytokines induce both necrosis and apoptosis via a common Bcl-2-inhibitable pathway in rat insulin-producing cells
    • Saldeen J. Cytokines induce both necrosis and apoptosis via a common Bcl-2-inhibitable pathway in rat insulin-producing cells. Endocrinology 2000; 141(6):2003-10. http://dx.doi.org/10.1210/endo.141.6.7523.
    • (2000) Endocrinology , vol.141 , Issue.6 , pp. 2003-2010
    • Saldeen, J.1
  • 85
    • 0344309002 scopus 로고    scopus 로고
    • Mechanisms of caspase activa-tion
    • Boatright KM, Salvesen GS. Mechanisms of caspase activa-tion. Curr Opin Cell Biol 2003; 15(6):725-31. http://dx.doi.org/10.1016/j.ceb.2003.10.009.
    • (2003) Curr Opin Cell Biol , vol.15 , Issue.6 , pp. 725-731
    • Boatright, KM1    Salvesen, GS.2
  • 86
    • 3042771527 scopus 로고    scopus 로고
    • Role of caspases in the regulation of apoptotic pancreatic islet beta-cells death
    • Hui H, Dotta F, Di Mario U, Perfetti R. Role of caspases in the regulation of apoptotic pancreatic islet beta-cells death. J Cell Physiol 2004; 200(2):177-200. http://dx.doi.org/10.1002/jcp.20021.
    • (2004) J Cell Physiol , vol.200 , Issue.2 , pp. 177-200
    • Hui, H1    Dotta, F2    Di Mario, U3    Perfetti, R.4
  • 87
    • 0041357164 scopus 로고    scopus 로고
    • BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis
    • Danial NN, Gramm CF, Scorrano L, Zhang CY, Krauss S, Ranger AM, et al. BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis. Nature 2003; 424(6951):952-6. http://dx.doi.org/10.1038/nature01825.
    • (2003) Nature , vol.424 , Issue.6951 , pp. 952-956
    • Danial, NN1    Gramm, CF2    Scorrano, L3    Zhang, CY4    Krauss, S5    Ranger, AM6
  • 88
    • 38949140180 scopus 로고    scopus 로고
    • Dual role of proapoptotic BAD in insulin secretion and beta cell survival
    • Danial NN, Walensky LD, Zhang CY, Choi CS, Fisher JK, Molina AJ, et al. Dual role of proapoptotic BAD in insulin secretion and beta cell survival. Nat Med 2008; 14(2):144-53. http://dx.doi.org/10.1038/nm1717.
    • (2008) Nat Med , vol.14 , Issue.2 , pp. 144-153
    • Danial, NN1    Walensky, LD2    Zhang, CY3    Choi, CS4    Fisher, JK5    Molina, AJ6
  • 89
    • 0037023692 scopus 로고    scopus 로고
    • Mitochondrial metabolism sets the maximal limit of fuel-stimu-lated insulin secretion in a model pancreatic beta cell: A survey of four fuel secretagogues
    • Antinozzi PA, Ishihara H, Newgard CB, Wollheim CB. Mitochondrial metabolism sets the maximal limit of fuel-stimu-lated insulin secretion in a model pancreatic beta cell: A survey of four fuel secretagogues. J Biol Chem 2002; 277(14):11746-55. http://dx.doi.org/10.1074/jbc.M108462200.
    • (2002) J Biol Chem , vol.277 , Issue.14 , pp. 11746-11755
    • Antinozzi, PA1    Ishihara, H2    Newgard, CB3    Wollheim, CB.4
  • 90
    • 0028182528 scopus 로고
    • + and pancreatic B-cell function
    • + and pancreatic B-cell function. Biochem Soc Trans 1994; 22(1):12-8. http://dx.doi.org/10.1042/bst0220012.
    • (1994) Biochem Soc Trans , vol.22 , Issue.1 , pp. 12-18
    • Berggren, PO1    Larsson, O.2
  • 91
    • 0029939626 scopus 로고    scopus 로고
    • Glucose metabolism and insulin release in mouse HC9 cells, as model of wild-type pancreatic beta cells
    • Liang Y, Bai N, Doliba C, Wang L, Barner DK, Matschinsky FM. Glucose metabolism and insulin release in mouse HC9 cells, as model of wild-type pancreatic beta cells. Am J Physiol 1996; 270:E846-57.
    • (1996) Am J Physiol , vol.270 , pp. E846-E857
    • Liang, Y1    Bai, N2    Doliba, C3    Wang, L4    Barner, DK5    Matschinsky, FM.6
  • 92
    • 84872032559 scopus 로고    scopus 로고
    • Bcl-2 and Bcl-xL suppress glucose signaling in pancreatic ß-cells
    • Luciani DS, White SA, Widenmaier SB, Saran VV, Taghizadeh F, Hu X, et al. Bcl-2 and Bcl-xL suppress glucose signaling in pancreatic ß-cells. Diabetes 2013; 62(1):170-82. http://dx.doi.org/10.2337/db11-1464.
    • (2013) Diabetes , vol.62 , Issue.1 , pp. 170-182
    • Luciani, DS1    White, SA2    Widenmaier, SB3    Saran, VV4    Taghizadeh, F5    Hu, X6
  • 93
    • 7444241537 scopus 로고    scopus 로고
    • Breast cancer cells can evade apoptosis-mediated selective killing by a novel small molecule inhibitor of Bcl-2
    • Real PJ, Cao Y, Wang R, Nikolovska-Coleska Z, Sanz-Ortiz J, Wang S, et al. Breast cancer cells can evade apoptosis-mediated selective killing by a novel small molecule inhibitor of Bcl-2. Cancer Res 2004; 64(21):7947-53. http://dx.doi.org/10.1158/0008-5472.CAN-04-0945.
    • (2004) Cancer Res , vol.64 , Issue.21 , pp. 7947-7953
    • Real, PJ1    Cao, Y2    Wang, R3    Nikolovska-Coleska, Z4    Sanz-Ortiz, J5    Wang, S6
  • 94
    • 80051970600 scopus 로고    scopus 로고
    • Metabolic regulation of protein N-alpha-acetylation by Bcl-xL pro-motes cell survival
    • Yi CH, Pan H, Seebacher J, Jang IH, Hyberts SG, Heffron GJ, et al. Metabolic regulation of protein N-alpha-acetylation by Bcl-xL pro-motes cell survival. Cell 2011; 146(4):607-20. http://dx.doi.org/10.1016/j.cell.2011.06.050.
    • (2011) Cell , vol.146 , Issue.4 , pp. 607-620
    • Yi, CH1    Pan, H2    Seebacher, J3    Jang, IH4    Hyberts, SG5    Heffron, GJ6
  • 95
    • 70149105706 scopus 로고    scopus 로고
    • The BH4 domain of Bcl-2 inhibits ER calcium release and apoptosis by binding the regulatory and coupling domain of the IP3 receptor
    • Rong YP, Bultynck G, Aromolaran AS, Zhong F, Parys JB, De Smedt H, et al. The BH4 domain of Bcl-2 inhibits ER calcium release and apoptosis by binding the regulatory and coupling domain of the IP3 receptor. Proc Natl Acad Sci U S A 2009; 106(34):14397-402. http://dx.doi.org/10.1073/pnas.0907555106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.34 , pp. 14397-14402
    • Rong, YP1    Bultynck, G2    Aromolaran, AS3    Zhong, F4    Parys, JB5    De Smedt, H6
  • 96
    • 0025327064 scopus 로고
    • Hyperinsulinemia and its sequelae
    • Simonson DC. Hyperinsulinemia and its sequelae. Horm Metab Res Suppl 1990; 22:17-25.
    • (1990) Horm Metab Res Suppl , vol.22 , pp. 17-25
    • Simonson, DC.1
  • 97
    • 39149104320 scopus 로고    scopus 로고
    • The role for endoplasmic reticu-lum stress in diabetes mellitus
    • Eizirik DL, Cardozo AK, Cnop M. The role for endoplasmic reticu-lum stress in diabetes mellitus. Endocr Rev 2008; 29(1):42-61. http://dx.doi.org/10.1210/er.2007-0015.
    • (2008) Endocr Rev , vol.29 , Issue.1 , pp. 42-61
    • Eizirik, DL1    Cardozo, AK2    Cnop, M.3
  • 98
    • 70449105119 scopus 로고    scopus 로고
    • Beta cell apoptosis in diabetes
    • Thomas HE, McKenzie MD, Angstetra E, Campbell PD, Kay TW. Beta cell apoptosis in diabetes. Apoptosis 2009; 14(12):1389-404. http://dx.doi.org/10.1007/s10495-009-0339-5.
    • (2009) Apoptosis , vol.14 , Issue.12 , pp. 1389-1404
    • Thomas, HE1    McKenzie, MD2    Angstetra, E3    Campbell, PD4    Kay, TW.5
  • 99
    • 16744368499 scopus 로고    scopus 로고
    • Overexpression of Bcl-xL in beta cells prevents cell death but impairs mitochondrial signal for insulin secretion
    • Zhou YP, Pena JC, Roe MW, Mittal A, Levesetti M, Baldwin AC, et al. Overexpression of Bcl-xL in beta cells prevents cell death but impairs mitochondrial signal for insulin secretion. Am J Physiol Endocrinol Metab 2000; 278(2):E340-51.
    • (2000) Am J Physiol Endocrinol Metab , vol.278 , Issue.2 , pp. E340-E351
    • Zhou, YP1    Pena, JC2    Roe, MW3    Mittal, A4    Levesetti, M5    Baldwin, AC6
  • 100
    • 12344305124 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and type 2 dia-betes
    • Lowell BB, Shulman GI. Mitochondrial dysfunction and type 2 dia-betes. Science 2005; 307(5708)384-7. http://dx.doi.org/10.1126/science.1104343.
    • (2005) Science , vol.307 , Issue.5708 , pp. 384-387
    • Lowell, BB1    Shulman, GI.2
  • 101
    • 0028913896 scopus 로고
    • Metformin. A review of its pharmacological properties and therapeutic use in non-insulin-dependent diabetes mellitus
    • Dunn CJ, Peters DH. Metformin. A review of its pharmacological properties and therapeutic use in non-insulin-dependent diabetes mellitus. Drugs 1995; 49(5):721-49.
    • (1995) Drugs , vol.49 , Issue.5 , pp. 721-749
    • Dunn, CJ1    Peters, DH.2
  • 102
    • 0041736553 scopus 로고    scopus 로고
    • Metformin: New understandings, new uses
    • Hundal RS, Inzucchi SE. Metformin: New understandings, new uses. Drugs 2003; 63(18):1879-94. http://dx.doi.org/10.2165/00003495-200363180-00001.
    • (2003) Drugs , vol.63 , Issue.18 , pp. 1879-1894
    • Hundal, RS1    Inzucchi, SE.2
  • 103
    • 0037341552 scopus 로고    scopus 로고
    • Metformin rap-idly increases insulin receptor activation in human liver and signals preferentially through insulin-receptor substrate-2 and increase glucose uptake via increased GLUT-2 translocation
    • Gunton JE, Delhanty PJ, Takahashi SI, Baxter RC. Metformin rap-idly increases insulin receptor activation in human liver and signals preferentially through insulin-receptor substrate-2 and increase glucose uptake via increased GLUT-2 translocation. J Clin Endocrinol Metab 2003; 88(3):323-32. http://dx.doi.org/10.1210/jc.2002-021394.
    • (2003) J Clin Endocrinol Metab , vol.88 , Issue.3 , pp. 323-332
    • Gunton, JE1    Delhanty, PJ2    Takahashi, SI3    Baxter, RC.4
  • 104
    • 0036894342 scopus 로고    scopus 로고
    • Sulfonylurea stimulation of insulin secretion
    • Suppl 3
    • Proks P, Reimann F, Green N, Gribble F, Ashcroft F. Sulfonylurea stimulation of insulin secretion. Diabetes 2002; 51 Suppl 3:S368-76. http://dx.doi.org/10.2337/diabetes.51.2007.S368.
    • (2002) Diabetes , vol.51 , pp. S368-S376
    • Proks, P1    Reimann, F2    Green, N3    Gribble, F4    Ashcroft, F.5
  • 105
    • 33644876504 scopus 로고    scopus 로고
    • Thiazolidinediones: The case for early use
    • Kendall DM. Thiazolidinediones: The case for early use. Diabetes Care 2006; 29(1):154-7. http://dx.doi.org/10.2337/diacare.29.01.06.dc05-0711.
    • (2006) Diabetes Care , vol.29 , Issue.1 , pp. 154-157
    • Kendall, DM.1
  • 106
    • 12244275009 scopus 로고    scopus 로고
    • GLP-1 receptor agonists and DPP-4 inhibitors in the treatment of type 2 diabetes
    • Ahrén B, Schmitz O. GLP-1 receptor agonists and DPP-4 inhibitors in the treatment of type 2 diabetes. Horm Metab Res 2004; 36(11-12):867-76. http://dx.doi.org/10.1055/s-2004-826178.
    • (2004) Horm Metab Res , vol.36 , Issue.11-12 , pp. 867-876
    • Ahrén, B1    Schmitz, O.2
  • 107
    • 80052362968 scopus 로고    scopus 로고
    • Role of sodium-glu-cose cotransporter 2 (SGLT-2) inhibitors in the treatment of type 2 diabetes
    • Abdul-Ghani MA, Norton L, DeFrenzo RA. Role of sodium-glu-cose cotransporter 2 (SGLT-2) inhibitors in the treatment of type 2 diabetes. Endocr Rev 2011; 32(4):515-31. http://dx.doi.org/10.1210/er.2010-0029.
    • (2011) Endocr Rev , vol.32 , Issue.4 , pp. 515-531
    • Abdul-Ghani, MA1    Norton, L2    DeFrenzo, RA.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.