메뉴 건너뛰기




Volumn 96, Issue 8, 2009, Pages 3331-3340

Bovine insulin filaments induced by reducing disulfide bonds show a different morphology, secondary structure, and cell toxicity from intact insulin amyloid fibrils

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; BOVINE INSULIN; PEPTIDE HORMONE; TRIS(2 CARBOXYETHYL)PHOSPHINE; CONGO RED; INSULIN; PHOSPHINE DERIVATIVE; THIAZOLE DERIVATIVE; THIOFLAVINE; TRIS(2-CARBOXYETHYL)PHOSPHINE;

EID: 67649397928     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2008.12.3957     Document Type: Article
Times cited : (110)

References (46)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M. 2003. Protein folding and misfolding. Nature. 426:884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C. A., and M. A. Poirier. 2004. Protein aggregation and neurodegenerative disease. Nat. Med. 10:S10-S17.
    • (2004) Nat. Med , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 3
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • Uversky, V. N., and A. L. Fink. 2004. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta. 1698:131-153.
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 4
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix
    • Blake, C., and L. Serpell. 1996. Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix. Structure. 4:989-998.
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.2
  • 5
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • Nilsson, M. R. 2004. Techniques to study amyloid fibril formation in vitro. Methods. 34:151-160.
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 7
    • 0023948509 scopus 로고
    • Insulin as an amyloid-fibril protein at sites of repeated insulin injections in a diabetic patient
    • Dische, F.E., C.Wernstedt, G. T. Westermark,P.Westermark,M. B. Pepys, et al. 1988. Insulin as an amyloid-fibril protein at sites of repeated insulin injections in a diabetic patient. Diabetologia. 31:158-161.
    • (1988) Diabetologia , vol.31 , pp. 158-161
    • Dische, F.E.1    Wernstedt, C.2    Westermark, G.T.3    Westermark, P.4    Pepys, M.B.5
  • 9
    • 30044446633 scopus 로고    scopus 로고
    • Early events in the fibrillation of monomeric insulin
    • Ahmad, A., V. N. Uversky, D. Hong, and A. L. Fink. 2005. Early events in the fibrillation of monomeric insulin. J. Biol. Chem. 280:42669-42675.
    • (2005) J. Biol. Chem , vol.280 , pp. 42669-42675
    • Ahmad, A.1    Uversky, V.N.2    Hong, D.3    Fink, A.L.4
  • 10
    • 0035902492 scopus 로고    scopus 로고
    • Probing the mechanism of insulin fibril formation with insulin mutants
    • Nielsen, L., S. Frokjaer, J. Brange, V. N. Uversky, and A. L. Fink. 2001. Probing the mechanism of insulin fibril formation with insulin mutants. Biochemistry. 40:8397-8409.
    • (2001) Biochemistry , vol.40 , pp. 8397-8409
    • Nielsen, L.1    Frokjaer, S.2    Brange, J.3    Uversky, V.N.4    Fink, A.L.5
  • 11
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
    • Nielsen, L., R. Khurana, A. Coats, S. Frokjaer, J. Brange, et al. 2001. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry. 40:6036-6046.
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5
  • 12
    • 33745285736 scopus 로고    scopus 로고
    • The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner
    • Devlin, G. L., T. P. Knowles, A. Squires, M. G. McCammon, S. L. Gras, et al. 2006. The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner. J. Mol. Biol. 360:497-509.
    • (2006) J. Mol. Biol , vol.360 , pp. 497-509
    • Devlin, G.L.1    Knowles, T.P.2    Squires, A.3    McCammon, M.G.4    Gras, S.L.5
  • 13
    • 29244479548 scopus 로고    scopus 로고
    • Independent heterologous fibrillation of insulin and its B-chain peptide
    • Hong, D. P., and A. L. Fink. 2005. Independent heterologous fibrillation of insulin and its B-chain peptide. Biochemistry. 44:16701-16709.
    • (2005) Biochemistry , vol.44 , pp. 16701-16709
    • Hong, D.P.1    Fink, A.L.2
  • 14
    • 0001153517 scopus 로고
    • Selective reduction of disulfides by Tris (2-carboxyethyl) phosphine
    • Burns, J. A., J. C. Butler, J. Moran, and G. M. Whitesides. 1991. Selective reduction of disulfides by Tris (2-carboxyethyl) phosphine. J. Org. Chem. 56:2648-2650.
    • (1991) J. Org. Chem , vol.56 , pp. 2648-2650
    • Burns, J.A.1    Butler, J.C.2    Moran, J.3    Whitesides, G.M.4
  • 15
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm, S., and J. Bandekar. 1986. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 38:181-364.
    • (1986) Adv. Protein Chem , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 16
    • 0025951780 scopus 로고
    • FTIR studies of secondary structures of bovine insulin and its derivatives
    • Wei, J. A., Y. Z. Lin, J. M. Zhou, and C. L. Tsou. 1991. FTIR studies of secondary structures of bovine insulin and its derivatives. Biochim. Biophys. Acta. 1080:29-33.
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 29-33
    • Wei, J.A.1    Lin, Y.Z.2    Zhou, J.M.3    Tsou, C.L.4
  • 17
    • 33748660053 scopus 로고    scopus 로고
    • Structure-specific effects of protein topology on cross-β assembly: Studies of insulin fibrillation
    • Huang, K., N. C. Maiti, N. B. Phillips, P. R. Carey, and M. A. Weiss. 2006. Structure-specific effects of protein topology on cross-β assembly: studies of insulin fibrillation. Biochemistry. 45:10278-10293.
    • (2006) Biochemistry , vol.45 , pp. 10278-10293
    • Huang, K.1    Maiti, N.C.2    Phillips, N.B.3    Carey, P.R.4    Weiss, M.A.5
  • 19
    • 11144222595 scopus 로고    scopus 로고
    • The binding of thioflavin-T to amyloid fibrils: Localisation and implications
    • Krebs, M. R., E. H. Bromley, and A. M. Donald. 2005. The binding of thioflavin-T to amyloid fibrils: localisation and implications. J. Struct. Biol. 149:30-37.
    • (2005) J. Struct. Biol , vol.149 , pp. 30-37
    • Krebs, M.R.1    Bromley, E.H.2    Donald, A.M.3
  • 20
    • 33644666997 scopus 로고    scopus 로고
    • Amyloid fibril formation of a-synuclein is accelerated by preformed amyloid seeds of other proteins: Implications for the mechanism of transmissible conformational diseases
    • Yagi, H., E. Kusaka, K. Hongo, T. Mizobata, and Y. Kawata. 2005. Amyloid fibril formation of a-synuclein is accelerated by preformed amyloid seeds of other proteins: implications for the mechanism of transmissible conformational diseases. J. Biol. Chem. 280:38609-38616.
    • (2005) J. Biol. Chem , vol.280 , pp. 38609-38616
    • Yagi, H.1    Kusaka, E.2    Hongo, K.3    Mizobata, T.4    Kawata, Y.5
  • 21
    • 0032831759 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy in analysis of protein deposits
    • Seshadri, S., R. Khurana, and A. L. Fink. 1999. Fourier transform infrared spectroscopy in analysis of protein deposits. Methods Enzymol. 309:559-576.
    • (1999) Methods Enzymol , vol.309 , pp. 559-576
    • Seshadri, S.1    Khurana, R.2    Fink, A.L.3
  • 22
    • 0026507761 scopus 로고
    • Amide modes and protein conformation
    • Bandekar, J. 1992. Amide modes and protein conformation. Biochim. Biophys. Acta. 1120:123-143.
    • (1992) Biochim. Biophys. Acta , vol.1120 , pp. 123-143
    • Bandekar, J.1
  • 23
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils
    • Zandomeneghi, G., M. R. Krebs, M. G. McCammon, and M. Fandrich. 2004. FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils. Protein Sci. 13:3314-3321.
    • (2004) Protein Sci , vol.13 , pp. 3314-3321
    • Zandomeneghi, G.1    Krebs, M.R.2    McCammon, M.G.3    Fandrich, M.4
  • 24
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson, M., and H. H. Mantsch. 1995. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30:95-120.
    • (1995) Crit. Rev. Biochem. Mol. Biol , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 25
    • 24644503134 scopus 로고    scopus 로고
    • Characteristic two-dimensional IR spectroscopic features of antiparallel and parallel β-sheet polypeptides: Simulation studies
    • Hahn, S., S. S. Kim, C. Lee, and M. Cho. 2005. Characteristic two-dimensional IR spectroscopic features of antiparallel and parallel β-sheet polypeptides: simulation studies. J. Chem. Phys. 123:084905.
    • (2005) J. Chem. Phys , vol.123 , pp. 084905
    • Hahn, S.1    Kim, S.S.2    Lee, C.3    Cho, M.4
  • 26
    • 55949096479 scopus 로고    scopus 로고
    • Formation of highly toxic soluble amyloid β oligomers by the molecular chaperone prefoldin
    • Sakono, M., T. Zako, H. Ueda, M. Yohda, and M. Maeda. 2008. Formation of highly toxic soluble amyloid β oligomers by the molecular chaperone prefoldin. FEBS J. 275:5982-5993.
    • (2008) FEBS J , vol.275 , pp. 5982-5993
    • Sakono, M.1    Zako, T.2    Ueda, H.3    Yohda, M.4    Maeda, M.5
  • 27
    • 0033855775 scopus 로고    scopus 로고
    • Review: Model peptides and the physicochemical approach to β-amyloids
    • Lynn, D. G., and S. C. Meredith. 2000. Review: model peptides and the physicochemical approach to β-amyloids. J. Struct. Biol. 130:153-173.
    • (2000) J. Struct. Biol , vol.130 , pp. 153-173
    • Lynn, D.G.1    Meredith, S.C.2
  • 28
    • 0036172742 scopus 로고    scopus 로고
    • The intrachain disulfide bond of β (2)-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH
    • Ohhashi, Y., Y. Hagihara, G. Kozhukh, M. Hoshino, K. Hasegawa, et al. 2002. The intrachain disulfide bond of β (2)-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH. J. Biochem. (Tokyo). 131:45-52.
    • (2002) J. Biochem. (Tokyo) , vol.131 , pp. 45-52
    • Ohhashi, Y.1    Hagihara, Y.2    Kozhukh, G.3    Hoshino, M.4    Hasegawa, K.5
  • 29
    • 35348907339 scopus 로고    scopus 로고
    • Nilsson, K. P., A. Aslund, I. Berg, S. Nystrom, P. Konradsson, et al. 2007. Imaging distinct conformational states of amyloid-β fibrils in Alzheimer's disease using novel luminescent probes. ACS Chem. Biol. 2:553-560.
    • Nilsson, K. P., A. Aslund, I. Berg, S. Nystrom, P. Konradsson, et al. 2007. Imaging distinct conformational states of amyloid-β fibrils in Alzheimer's disease using novel luminescent probes. ACS Chem. Biol. 2:553-560.
  • 30
    • 34447539588 scopus 로고    scopus 로고
    • Quantum efficiency and two-photon absorption cross-section of conjugated polyelectrolytes used for protein conformation measurements with applications on amyloid structures
    • Stabo-Eeg, F., M. Lindgren, K. P. Nilsson, O. Inganas, and P. Hammarstrom. 2007. Quantum efficiency and two-photon absorption cross-section of conjugated polyelectrolytes used for protein conformation measurements with applications on amyloid structures. Chem. Phys. 336:121-126.
    • (2007) Chem. Phys , vol.336 , pp. 121-126
    • Stabo-Eeg, F.1    Lindgren, M.2    Nilsson, K.P.3    Inganas, O.4    Hammarstrom, P.5
  • 31
    • 36849060218 scopus 로고    scopus 로고
    • Promotion of insulin aggregation by protein disulfide isomerase
    • Maeda, R., K. Ado, N. Takeda, and Y. Taniguchi. 2007. Promotion of insulin aggregation by protein disulfide isomerase. Biochim. Biophys. Acta. 1774:1619-1627.
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 1619-1627
    • Maeda, R.1    Ado, K.2    Takeda, N.3    Taniguchi, Y.4
  • 32
    • 0034649352 scopus 로고    scopus 로고
    • Amyloid fibril formation by A β 16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR
    • Balbach, J. J., Y. Ishii, O. N. Antzutkin, R. D. Leapman, N. W. Rizzo, et al. 2000. Amyloid fibril formation by A β 16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR. Biochemistry. 39:13748-13759.
    • (2000) Biochemistry , vol.39 , pp. 13748-13759
    • Balbach, J.J.1    Ishii, Y.2    Antzutkin, O.N.3    Leapman, R.D.4    Rizzo, N.W.5
  • 33
    • 0028804827 scopus 로고
    • Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide
    • Lansbury, Jr., P. T., P. R. Costa, J. M. Griffiths, E. J. Simon, M. Auger, et al. 1995. Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. Nat. Struct. Biol. 2:990-998.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 990-998
    • Lansbury Jr., P.T.1    Costa, P.R.2    Griffiths, J.M.3    Simon, E.J.4    Auger, M.5
  • 34
    • 0025275241 scopus 로고
    • Molecular determinants of amyloid deposition in Alzheimer's disease: Conformational studies of synthetic β-protein fragments
    • Halverson, K., P. E. Fraser, D. A. Kirschner, and P. T. Lansbury Jr. 1990. Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic β-protein fragments. Biochemistry. 29:2639-2644.
    • (1990) Biochemistry , vol.29 , pp. 2639-2644
    • Halverson, K.1    Fraser, P.E.2    Kirschner, D.A.3    Lansbury Jr., P.T.4
  • 35
    • 25844493690 scopus 로고    scopus 로고
    • Experimental evidence for the reorganization of β-strands within aggregates of the Aβ (16-22) peptide
    • Petty, S. A., and S. M. Decatur. 2005. Experimental evidence for the reorganization of β-strands within aggregates of the Aβ (16-22) peptide. J. Am. Chem. Soc. 127:13488-13489.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 13488-13489
    • Petty, S.A.1    Decatur, S.M.2
  • 36
    • 0032506114 scopus 로고    scopus 로고
    • Propagating structure of Alzheimer's β-amyloid (10-35) is parallel β-sheet with residues in exact register
    • Benzinger, T. L., D. M. Gregory, T. S. Burkoth, H. Miller-Auer, D. G. Lynn, et al. 1998. Propagating structure of Alzheimer's β-amyloid (10-35) is parallel β-sheet with residues in exact register. Proc. Natl. Acad. Sci. USA. 95:13407-13412.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13407-13412
    • Benzinger, T.L.1    Gregory, D.M.2    Burkoth, T.S.3    Miller-Auer, H.4    Lynn, D.G.5
  • 38
    • 0242580170 scopus 로고    scopus 로고
    • Neurotoxicity and physicochemical properties of Aβ mutant peptides from cerebral amyloid angiopathy: Implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease
    • Murakami, K., K. Irie, A. Morimoto, H. Ohigashi, M. Shindo, et al. 2003. Neurotoxicity and physicochemical properties of Aβ mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease. J. Biol. Chem. 278:46179-46187.
    • (2003) J. Biol. Chem , vol.278 , pp. 46179-46187
    • Murakami, K.1    Irie, K.2    Morimoto, A.3    Ohigashi, H.4    Shindo, M.5
  • 39
    • 17744395315 scopus 로고    scopus 로고
    • β-Sheet structure in amyloid β fibrils and vibrational dipolar coupling
    • Paul, C., and P. H. Axelsen. 2005. β-Sheet structure in amyloid β fibrils and vibrational dipolar coupling. J. Am. Chem. Soc. 127:5754-5755.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 5754-5755
    • Paul, C.1    Axelsen, P.H.2
  • 40
    • 0003100933 scopus 로고
    • Raman Spectroscopy of Proteins
    • Spectroscopy. J. R. Downey and G. J. Jans, editors. Heydon & Son, London
    • Frushour, B. G., and J. L. Koenig. 1975. Raman Spectroscopy of Proteins. In Advances in Infrared and Raman Spectroscopy. J. R. Downey and G. J. Jans, editors. Heydon & Son, London.
    • (1975) Advances in Infrared and Raman
    • Frushour, B.G.1    Koenig, J.L.2
  • 41
    • 0034846252 scopus 로고    scopus 로고
    • Role of the single disulphide bond of β(2)-microglobulin in amyloidosis in vitro
    • Smith, D. P., and S. E. Radford. 2001. Role of the single disulphide bond of β(2)-microglobulin in amyloidosis in vitro. Protein Sci. 10:1775-1784.
    • (2001) Protein Sci , vol.10 , pp. 1775-1784
    • Smith, D.P.1    Radford, S.E.2
  • 42
    • 33846562360 scopus 로고    scopus 로고
    • Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion
    • Mishra, R., K. Sorgjerd, S. Nystrom, A. Nordigarden, Y. C. Yu, et al. 2007. Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion. J. Mol. Biol. 366:1029-1044.
    • (2007) J. Mol. Biol , vol.366 , pp. 1029-1044
    • Mishra, R.1    Sorgjerd, K.2    Nystrom, S.3    Nordigarden, A.4    Yu, Y.C.5
  • 43
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., E. Head, J. L. Thompson, T. M. McIntire, S. C. Milton, et al. 2003. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science. 300:486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5
  • 44
    • 56349095198 scopus 로고    scopus 로고
    • Prefibrillar transthyretin oligomers and cold stored native tetrameric transthyretin are cytotoxic in cell culture
    • Sorgjerd, K., T. Klingstedt, M. Lindgren, K. Kagedal, and P. Hammarstrom. 2008. Prefibrillar transthyretin oligomers and cold stored native tetrameric transthyretin are cytotoxic in cell culture. Biochem. Biophys. Res. Commun. 377:1072-1078.
    • (2008) Biochem. Biophys. Res. Commun , vol.377 , pp. 1072-1078
    • Sorgjerd, K.1    Klingstedt, T.2    Lindgren, M.3    Kagedal, K.4    Hammarstrom, P.5
  • 45
    • 33846023647 scopus 로고    scopus 로고
    • Lysozyme amyloid oligomers and fibrils induce cellular death via different apoptotic/necrotic pathways
    • Gharibyan, A. L., V. Zamotin, K. Yanamandra, O. S. Moskaleva, B. A. Margulis, et al. 2007. Lysozyme amyloid oligomers and fibrils induce cellular death via different apoptotic/necrotic pathways. J. Mol. Biol. 365:1337-1349.
    • (2007) J. Mol. Biol , vol.365 , pp. 1337-1349
    • Gharibyan, A.L.1    Zamotin, V.2    Yanamandra, K.3    Moskaleva, O.S.4    Margulis, B.A.5
  • 46
    • 0037387147 scopus 로고    scopus 로고
    • A cell surface receptor complex for fibrillar β-amyloid mediates microglial activation
    • Bamberger, M. E., M. E. Harris, D. R. McDonald, J. Husemann, and G. E. Landreth. 2003. A cell surface receptor complex for fibrillar β-amyloid mediates microglial activation. J. Neurosci. 23:2665-2674.
    • (2003) J. Neurosci , vol.23 , pp. 2665-2674
    • Bamberger, M.E.1    Harris, M.E.2    McDonald, D.R.3    Husemann, J.4    Landreth, G.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.