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Volumn 377, Issue 3, 2004, Pages 709-716

Pancreatic β-cell granule peptides form heteromolecular complexes which inhibit islet amyloid polypeptide fibril formation

Author keywords

Amyloid fibril; Diabetes; Insulin; Islet amyloid polypeptide; Type 2 diabetes; sheet

Indexed keywords

CELLS; IMMUNOLOGY; INSULIN; POLYPEPTIDES; SURFACE PLASMON RESONANCE; TRANSMISSION ELECTRON MICROSCOPY;

EID: 1242292280     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/bj20030852     Document Type: Article
Times cited : (93)

References (34)
  • 1
    • 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
    • Westermark, P., Wernstedt, C., Wilander, E., Hayden, D. W., O'Brien, T. D, and Johnson, K. H. (1987) Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc. Natl. Acad. Sci. U.S.A. 84, 3881-3885
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 3881-3885
    • Westermark, P.1    Wernstedt, C.2    Wilander, E.3    Hayden, D.W.4    O'Brien, T.D.A.5    Johnson, K.H.6
  • 2
    • 0023189095 scopus 로고
    • Islet amyloid formed from diabetes-associated peptide may be pathogenic in type-2 diabetes
    • Clark, A., Cooper, G. J., Lewis, C. E., Morris, J. F., Willis, A. C., Reid, K. B. and Turner, R. C. (1987) Islet amyloid formed from diabetes-associated peptide may be pathogenic in type-2 diabetes. Lancet II, 231-234
    • (1987) Lancet , vol.2 , pp. 231-234
    • Clark, A.1    Cooper, G.J.2    Lewis, C.E.3    Morris, J.F.4    Willis, A.C.5    Reid, K.B.6    Turner, R.C.7
  • 3
    • 0024428356 scopus 로고
    • Islet amyloid polypeptide (IAPP): cDNA cloning and identification of an amyloidogenic region associated with the species-specific occurrence of age-related diabetes mellitus
    • Betsholtz, C., Svensson, V, Rorsman, F., Engstrom, U., Westermark, G. T., Wilander, E., Johnson, K. and Westermark, P. (1989) Islet amyloid polypeptide (IAPP): cDNA cloning and identification of an amyloidogenic region associated with the species-specific occurrence of age-related diabetes mellitus. Exp. Cell Res. 183, 484-493
    • (1989) Exp. Cell Res. , vol.183 , pp. 484-493
    • Betsholtz, C.1    Svensson, V.2    Rorsman, F.3    Engstrom, U.4    Westermark, G.T.5    Wilander, E.6    Johnson, K.7    Westermark, P.8
  • 4
    • 0025287442 scopus 로고
    • Effects of meal ingestion on plasma amylin concentration in NIDDM and nondiabetic humans
    • Butler, P. C., Chou, J., Carter, W. B., Wang, Y. N., Bu, B. H., Chang, D., Chang, J. K. and Rizza, R. A. (1990) Effects of meal ingestion on plasma amylin concentration in NIDDM and nondiabetic humans. Diabetes 39, 752-756
    • (1990) Diabetes , vol.39 , pp. 752-756
    • Butler, P.C.1    Chou, J.2    Carter, W.B.3    Wang, Y.N.4    Bu, B.H.5    Chang, D.6    Chang, J.K.7    Rizza, R.A.8
  • 5
    • 0025967810 scopus 로고
    • Plasma islet amyloid polypeptide (amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients
    • Sanke, T., Hanabusa, T., Nakano, Y., Oki, C., Okai, K., Nishimura, S., Kondo, M. and Nanjo, K. (1991) Plasma islet amyloid polypeptide (amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients. Diabetologia 34, 129-132
    • (1991) Diabetologia , vol.34 , pp. 129-132
    • Sanke, T.1    Hanabusa, T.2    Nakano, Y.3    Oki, C.4    Okai, K.5    Nishimura, S.6    Kondo, M.7    Nanjo, K.8
  • 6
    • 0030064237 scopus 로고    scopus 로고
    • Processing of pro-islet amyloid polypeptide (proIAPP) by the prohormone convertase PC2
    • Badman, M. K., Shennan, K. I., Jermany, J. L., Docherty, K. and Clark, A. (1996) Processing of pro-islet amyloid polypeptide (proIAPP) by the prohormone convertase PC2. FEBS Lett. 378, 227-231
    • (1996) FEBS Lett. , vol.378 , pp. 227-231
    • Badman, M.K.1    Shennan, K.I.2    Jermany, J.L.3    Docherty, K.4    Clark, A.5
  • 7
    • 0026313787 scopus 로고
    • Proprotein-processing endopeptidases of the insulin secretory granule
    • Bailyes, E. M., Bennett, D. L. and Hutton, J, C. (1991) Proprotein-processing endopeptidases of the insulin secretory granule. Enzyme 45, 301-313
    • (1991) Enzyme , vol.45 , pp. 301-313
    • Bailyes, E.M.1    Bennett, D.L.2    Hutton, J.C.3
  • 8
    • 0021699977 scopus 로고
    • Secretory granules
    • Hutton, J. C. (1984) Secretory granules. Experientia 40, 1091-1098
    • (1984) Experientia , vol.40 , pp. 1091-1098
    • Hutton, J.C.1
  • 10
    • 0028901314 scopus 로고
    • Amylin/islet amyloid polypeptide: Biochemistry, physiology, patho-physiology
    • Castillo, M. J., Scheen, A. J. and Lefebvre, P. J. (1995) Amylin/islet amyloid polypeptide: biochemistry, physiology, patho-physiology. Diabetes Metab. 21, 3-25
    • (1995) Diabetes Metab. , vol.21 , pp. 3-25
    • Castillo, M.J.1    Scheen, A.J.2    Lefebvre, P.J.3
  • 11
    • 0030025653 scopus 로고    scopus 로고
    • Effects of β-cell granule components on human islet amyloid polypeptide fibril formation
    • Westermark, P., Li, Z. C., Westermark, G. T., Leckstrom, A. and Steiner, D. F. (1996) Effects of β-cell granule components on human islet amyloid polypeptide fibril formation. FEBS Lett. 379, 203-206
    • (1996) FEBS Lett. , vol.379 , pp. 203-206
    • Westermark, P.1    Li, Z.C.2    Westermark, G.T.3    Leckstrom, A.4    Steiner, D.F.5
  • 12
    • 0032969276 scopus 로고    scopus 로고
    • Islet amyloid: A long-recognized but underappreciated pathological feature of type 2 diabetes
    • Kahn, S. E., Andrikopoulos, S. and Verchere, C. B. (1999) Islet amyloid: a long-recognized but underappreciated pathological feature of type 2 diabetes. Diabetes 48, 241-253
    • (1999) Diabetes , vol.48 , pp. 241-253
    • Kahn, S.E.1    Andrikopoulos, S.2    Verchere, C.B.3
  • 13
    • 0029978228 scopus 로고    scopus 로고
    • Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic β-cell expression of human islet amyloid polypeptide
    • Verchere, C. B., D'Alessio, D. A., Palmiter, R. D., Weir, G. C., Bonner Weir, S., Baskin, D. G. and Kahn, S. E. (1996) Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic β-cell expression of human islet amyloid polypeptide. Proc. Natl. Acad. Sci. U.S.A. 93, 3492-3496
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 14
    • 0029742232 scopus 로고    scopus 로고
    • Treatment with growth hormone and dexamethasone in mice transgenic for human islet amyloid polypeptide causes islet amyloidosis and β-cell dysfunction
    • Couce, M., Kane, L. A., O'Brien, T. D., Charlesworth, J., Soeller, W., McNeish, J., Kreutter, D., Roche, P. and Butler, P. C. (1996) Treatment with growth hormone and dexamethasone in mice transgenic for human islet amyloid polypeptide causes islet amyloidosis and β-cell dysfunction. Diabetes 45, 1094-1101
    • (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
  • 16
    • 0033997942 scopus 로고    scopus 로고
    • Transthyretin binds amyloid β peptides, Aβ1-A42 and Aβ1-A40 to form complex in the autopsied human kidney - Possible role of transthyretin for Aβ sequestration
    • Tsuzuki, K., Fukatsu, R., Yamaguchi, H., Tateno, M., Imai, K., Fujii, N. and Yamauchi, T. (2000) Transthyretin binds amyloid β peptides, Aβ1-A42 and Aβ1-A40 to form complex in the autopsied human kidney - possible role of transthyretin for Aβ sequestration. Neurosci. Lett. 281, 171-174
    • (2000) Neurosci. Lett. , vol.281 , pp. 171-174
    • Tsuzuki, K.1    Fukatsu, R.2    Yamaguchi, H.3    Tateno, M.4    Imai, K.5    Fujii, N.6    Yamauchi, T.7
  • 17
    • 0034677739 scopus 로고    scopus 로고
    • Preparation of synthetic human islet amyloid polypeptide (IAPP) in a stable conformation to enable study of conversion to amyloid-like fibrils
    • Higham, C. E., Jaikaran, E. T. A. S., Fraser, P. E., Gross, M. and Clark, A. (2000) Preparation of synthetic human islet amyloid polypeptide (IAPP) in a stable conformation to enable study of conversion to amyloid-like fibrils. FEBS Lett. 470, 55-60
    • (2000) FEBS Lett. , vol.470 , pp. 55-60
    • Higham, C.E.1    Jaikaran, E.T.A.S.2    Fraser, P.E.3    Gross, M.4    Clark, A.5
  • 19
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of β-sheet amyloid fibril structures with thioflavin T
    • LeVine, H. (1999) Quantification of β-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309, 274-284
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
    • Levine, H.1
  • 20
    • 0031591653 scopus 로고    scopus 로고
    • β-Cell granule peptides affect human islet amyloid polypeptide (IAPP) fibril formation in vitro
    • Janciauskiene, S., Eriksson, S., Carlemalm, E. and Ahrén, B. (1997) β-Cell granule peptides affect human islet amyloid polypeptide (IAPP) fibril formation in vitro. Biochem. Biophys. Res. Commun. 236, 580-585
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 580-585
    • Janciauskiene, S.1    Eriksson, S.2    Carlemalm, E.3    Ahrén, B.4
  • 21
    • 0027447093 scopus 로고
    • Influence of islet amyloid polypeptide and the 8-37 fragment of islet amyloid polypeptide on insulin release from perifused rat islets
    • Wang, Z. L., Bennet, W. M., Ghatei, M. A., Byfield, P. G., Smith, D. M. and Bloom, S. R. (1993) Influence of islet amyloid polypeptide and the 8-37 fragment of islet amyloid polypeptide on insulin release from perifused rat islets. Diabetes 42, 330-335
    • (1993) Diabetes , vol.42 , pp. 330-335
    • Wang, Z.L.1    Bennet, W.M.2    Ghatei, M.A.3    Byfield, P.G.4    Smith, D.M.5    Bloom, S.R.6
  • 22
    • 26544432461 scopus 로고    scopus 로고
    • Insulin and islet amyloid polypeptide 'amylin' form stable molecular complexes
    • Jaikaran, E. T. A. S., Robinson, C. V., Fraser, P. E. and Clark, A. (1998) Insulin and islet amyloid polypeptide 'amylin' form stable molecular complexes. Diabetic Med. 15 (Suppl. 2), S6
    • (1998) Diabetic Med. , vol.15 , Issue.2 SUPPL.
    • Jaikaran, E.T.A.S.1    Robinson, C.V.2    Fraser, P.E.3    Clark, A.4
  • 24
    • 0024307842 scopus 로고
    • Co-localization of islet amyloid polypeptide and insulin in the β-cell secretory granules of the human pancreatic islets
    • Lukinius, A., Wilander, E., Westermark, G. T., Engström, U. and Westermark, P. (1989) Co-localization of islet amyloid polypeptide and insulin in the β-cell secretory granules of the human pancreatic islets. Diabetologia 32, 240-244
    • (1989) Diabetologia , vol.32 , pp. 240-244
    • Lukinius, A.1    Wilander, E.2    Westermark, G.T.3    Engström, U.4    Westermark, P.5
  • 25
    • 0035804936 scopus 로고    scopus 로고
    • Identification of a novel human islet amyloid polypeptide β-sheet domain and factors influencing fibrillogenesis
    • Jaikaran, E. T. A. S., Higham, C. E., Serpell, L. C., Zurdo, J., Gross, M., Clark, A. and Fraser, P. E. (2001) Identification of a novel human islet amyloid polypeptide β-sheet domain and factors influencing fibrillogenesis. J. Mol. Biol. 308, 515-525
    • (2001) J. Mol. Biol. , vol.308 , pp. 515-525
    • Jaikaran, E.T.A.S.1    Higham, C.E.2    Serpell, L.C.3    Zurdo, J.4    Gross, M.5    Clark, A.6    Fraser, P.E.7
  • 28
    • 0021676541 scopus 로고
    • Non-uniform distribution of islet amyloid in the pancreas of 'maturity-onset' diabetic patients
    • Clark, A., Holman, R., Matthews, D., Hockaday, T. and Turner, R. (1984) Non-uniform distribution of islet amyloid in the pancreas of 'maturity-onset' diabetic patients. Diabetologia 27, 527-528
    • (1984) Diabetologia , vol.27 , pp. 527-528
    • Clark, A.1    Holman, R.2    Matthews, D.3    Hockaday, T.4    Turner, R.5
  • 29
    • 0020569676 scopus 로고
    • Islet amyloid in Type 2 (non-insulin-dependent) diabetes is related to insulin
    • Westermark, P. and Wilander, E. (1983) Islet amyloid in Type 2 (non-insulin-dependent) diabetes is related to insulin. Diabetologia 24, 342-346
    • (1983) Diabetologia , vol.24 , pp. 342-346
    • Westermark, P.1    Wilander, E.2
  • 30
    • 0030843572 scopus 로고    scopus 로고
    • Pramlintide: A human amylin analogue reduced postprandial plasma glucose, insulin, and C-peptide concentrations in patients with type 2 diabetes
    • Thompson, R. G., Gottlieb, A., Organ, K., Koda, J., Kisicki, J. and Kolterman, O. G. (1997) Pramlintide: a human amylin analogue reduced postprandial plasma glucose, insulin, and C-peptide concentrations in patients with type 2 diabetes. Diabetic Med. 14, 547-555
    • (1997) Diabetic Med. , vol.14 , pp. 547-555
    • Thompson, R.G.1    Gottlieb, A.2    Organ, K.3    Koda, J.4    Kisicki, J.5    Kolterman, O.G.6
  • 31
    • 0032800840 scopus 로고    scopus 로고
    • Isolation and identification of cyclic imide and deamidation products in heat stressed pramlintide injection drug product
    • Hekman, C. M., DeMond, W. S., Kelley, P. J., Mauch, S. F. and Williams, J. D. (1999) Isolation and identification of cyclic imide and deamidation products in heat stressed pramlintide injection drug product. J, Pharm. Biomed. Anal. 20, 763-772
    • (1999) J, Pharm. Biomed. Anal. , vol.20 , pp. 763-772
    • Hekman, C.M.1    Demond, W.S.2    Kelley, P.J.3    Mauch, S.F.4    Williams, J.D.5
  • 32
    • 0034570847 scopus 로고    scopus 로고
    • Islet amyloid development in a mouse strain lacking endogenous islet amyloid polypeptide (IAPP) but expressing human IAPP
    • Westermark, G. T., Gebre-Medhin, S., Steiner, D. F. and Westermark, P. (2000) Islet amyloid development in a mouse strain lacking endogenous islet amyloid polypeptide (IAPP) but expressing human IAPP. Mol. Med. 6, 998-1007
    • (2000) Mol. Med. , vol.6 , pp. 998-1007
    • Westermark, G.T.1    Gebre-Medhin, S.2    Steiner, D.F.3    Westermark, P.4
  • 33
    • 0035969513 scopus 로고    scopus 로고
    • Islet amyloid and type 2 diabetes: From molecular misfolding to islet pathophysiology
    • Jaikaran, E. T. A. S. and Clark, A. (2001) Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology. Biochim. Biophys. Acta 1537, 179-203
    • (2001) Biochim. Biophys. Acta , vol.1537 , pp. 179-203
    • Jaikaran, E.T.A.S.1    Clark, A.2
  • 34
    • 0030662718 scopus 로고    scopus 로고
    • Release of incompletely processed proinsulin is the cause of the disproportionate proinsulinaemia of NIDDM
    • Halban, P. A. and Kahn, S. E. (1997) Release of incompletely processed proinsulin is the cause of the disproportionate proinsulinaemia of NIDDM. Diabetes 46, 1725-1732
    • (1997) Diabetes , vol.46 , pp. 1725-1732
    • Halban, P.A.1    Kahn, S.E.2


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