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Volumn 273, Issue 18, 2006, Pages 4250-4263

High affinity copper binding by stefin B (cystatin B) and its role in the inhibition of amyloid fibrillation

Author keywords

Copper binding proteins; Cystatin; Inhibition of amyloid fibril formation; Oligomers; Protein aggregation; Stefin B

Indexed keywords

AMYLOID; COPPER; CYSTATIN B; CYSTEINE PROTEINASE INHIBITOR; STEFIN B;

EID: 33748304111     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2006.05426.x     Document Type: Article
Times cited : (28)

References (55)
  • 2
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson CM (1999) Protein misfolding, evolution and disease. Trends Biochem Sci 24, 329-332.
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 4
    • 18144374793 scopus 로고    scopus 로고
    • Metal ion-dependent effects of clioquinol on the fibril growth of an amyloid {beta} peptide
    • Raman B, Ban T, Yamaguchi K, Sakai M, Kawai T, Naiki H & Goto Y (2005) Metal ion-dependent effects of clioquinol on the fibril growth of an amyloid {beta} peptide. J Biol Chem 280, 16157-16162.
    • (2005) J Biol Chem , vol.280 , pp. 16157-16162
    • Raman, B.1    Ban, T.2    Yamaguchi, K.3    Sakai, M.4    Kawai, T.5    Naiki, H.6    Goto, Y.7
  • 6
    • 1842531945 scopus 로고    scopus 로고
    • Different propensity to form amyloid fibrils by two homologous proteins-Human stefins A and B: Searching for an explanation
    • Jenko S, Škarabot M, Kenig M, Gunčar G, Muševič I, Turk D & Žerovnik E (2004) Different propensity to form amyloid fibrils by two homologous proteins-Human stefins A and B: searching for an explanation. Proteins 55, 417-425.
    • (2004) Proteins , vol.55 , pp. 417-425
    • Jenko, S.1    Škarabot, M.2    Kenig, M.3    Gunčar, G.4    Muševič, I.5    Turk, D.6    Žerovnik, E.7
  • 7
    • 0036382240 scopus 로고    scopus 로고
    • Conformational changes preceding amyloid-fibril formation of amyloid-beta and stefin B; parallels in pH dependence
    • Matsunaga Y, Žerovnik E, Yamada T & Turk V (2002) Conformational changes preceding amyloid-fibril formation of amyloid-beta and stefin B; parallels in pH dependence. Curr Med Chem 9, 1717-1724.
    • (2002) Curr Med Chem , vol.9 , pp. 1717-1724
    • Matsunaga, Y.1    Žerovnik, E.2    Yamada, T.3    Turk, V.4
  • 10
    • 0025817602 scopus 로고
    • The cystatins: Protein inhibitors of cysteine proteinases
    • Turk V & Bode W (1991) The cystatins: protein inhibitors of cysteine proteinases. FEBS Lett 285, 213-219.
    • (1991) FEBS Lett , vol.285 , pp. 213-219
    • Turk, V.1    Bode, W.2
  • 11
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteinases: Facts and opportunities
    • Turk V, Turk B & Turk D (2001) Lysosomal cysteine proteinases: facts and opportunities. EMBO J 20, 4629-4633.
    • (2001) EMBO J , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 12
    • 0025301658 scopus 로고
    • The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: A novel type of proteinase inhibitor interaction
    • Stubbs MT, Laber B, Bode W, Huber R, Jerala R, Lenarčič B & Turk V (1990) The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. EMBO J 9, 1939-1947.
    • (1990) EMBO J , vol.9 , pp. 1939-1947
    • Stubbs, M.T.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5    Lenarčič, B.6    Turk, V.7
  • 13
    • 0037459045 scopus 로고    scopus 로고
    • Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases
    • Jenko S, Dolenc I, Gunčar G, Doberšek A, Podobnik M & Turk D (2003) Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases. J Mol Biol 326, 875-885.
    • (2003) J Mol Biol , vol.326 , pp. 875-885
    • Jenko, S.1    Dolenc, I.2    Gunčar, G.3    Doberšek, A.4    Podobnik, M.5    Turk, D.6
  • 15
    • 0033520512 scopus 로고    scopus 로고
    • Accessing the global minimum conformation of stefin A dimer by annealing under partially denaturing conditions
    • Jerala R & Žerovnik E (1999) Accessing the global minimum conformation of stefin A dimer by annealing under partially denaturing conditions. J Mol Biol 291, 1079-1089.
    • (1999) J Mol Biol , vol.291 , pp. 1079-1089
    • Jerala, R.1    Žerovnik, E.2
  • 16
    • 0035801540 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily
    • Staniforth RA, Giannini S, Higgins LD, Conroy MJ, Hounslow AM, Jerala R, Craven CJ & Waltho JP (2001) Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. EMBO J 20, 4774-4781.
    • (2001) EMBO J , vol.20 , pp. 4774-4781
    • Staniforth, R.A.1    Giannini, S.2    Higgins, L.D.3    Conroy, M.J.4    Hounslow, A.M.5    Jerala, R.6    Craven, C.J.7    Waltho, J.P.8
  • 18
    • 0036848257 scopus 로고    scopus 로고
    • New insights into the molecular basis of progressive myoclonus epilepsy: A multiprotein complex with cystatin B
    • Di Giamo R, Riccio M, Santi S, Galeotti C, Ambrosetti DC & Melli M (2002) New insights into the molecular basis of progressive myoclonus epilepsy: a multiprotein complex with cystatin B. Hum Mol Genet 11, 2941-2950.
    • (2002) Hum Mol Genet , vol.11 , pp. 2941-2950
    • Di Giamo, R.1    Riccio, M.2    Santi, S.3    Galeotti, C.4    Ambrosetti, D.C.5    Melli, M.6
  • 19
    • 0035862167 scopus 로고    scopus 로고
    • Nuclear localization of cystatin B, the cathepsin inhibitor implicated in myoclonus epilepsy (EPM1)
    • Riccio M, Di Giaimo R, Pianetti S, Palmieri PP, Melli M & Santi S (2001) Nuclear localization of cystatin B, the cathepsin inhibitor implicated in myoclonus epilepsy (EPM1). Exp Cell Res 262, 84-94.
    • (2001) Exp Cell Res , vol.262 , pp. 84-94
    • Riccio, M.1    Di Giaimo, R.2    Pianetti, S.3    Palmieri, P.P.4    Melli, M.5    Santi, S.6
  • 21
    • 0035446403 scopus 로고    scopus 로고
    • Cystatin B-deficient mice have increased expression of apoptosis and glial activation genes
    • Lieuallen K, Pennacchio LA, Park M, Myers RM & Lennon GG (2001) Cystatin B-deficient mice have increased expression of apoptosis and glial activation genes. Hum Mol Genet 10, 1867-1871.
    • (2001) Hum Mol Genet , vol.10 , pp. 1867-1871
    • Lieuallen, K.1    Pennacchio, L.A.2    Park, M.3    Myers, R.M.4    Lennon, G.G.5
  • 24
    • 0034116090 scopus 로고    scopus 로고
    • Seizures induce widespread upregulation of cystatin B, the gene mutated in progressive myoclonus epilepsy, in rat forebrain neurons
    • D'Amato E, Kokaia Z, Nanobashvili A, Reeben M, Lehesjoki AE, Saarma M & Lindvall O (2000) Seizures induce widespread upregulation of cystatin B, the gene mutated in progressive myoclonus epilepsy, in rat forebrain neurons. Eur J Neurosci 12, 1687-1695.
    • (2000) Eur J Neurosci , vol.12 , pp. 1687-1695
    • D'Amato, E.1    Kokaia, Z.2    Nanobashvili, A.3    Reeben, M.4    Lehesjoki, A.E.5    Saarma, M.6    Lindvall, O.7
  • 26
  • 27
    • 0027378622 scopus 로고
    • Abnormal distribution of cathepsin proteinases and endogenous inhibitors (cystatins) in the hippocampus of patients with Alzheimer's disease, parkinsonism-dementia complex on Guam, and senile dementia and in the aged
    • Ii K, Hidehumi I, Kominami E & Hirano A (1993) Abnormal distribution of cathepsin proteinases and endogenous inhibitors (cystatins) in the hippocampus of patients with Alzheimer's disease, parkinsonism-dementia complex on Guam, and senile dementia and in the aged. Virchows Arch a Pathol Anat Histopathol 423, 185-194.
    • (1993) Virchows Arch a Pathol Anat Histopathol , vol.423 , pp. 185-194
    • Ii, K.1    Hidehumi, I.2    Kominami, E.3    Hirano, A.4
  • 28
    • 0024464461 scopus 로고
    • Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor
    • Manning MC & Woody RW (1989) Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor. Biochemistry 28, 8609-8613.
    • (1989) Biochemistry , vol.28 , pp. 8609-8613
    • Manning, M.C.1    Woody, R.W.2
  • 29
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore L & Wallace BA (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res 32, W668-W673.
    • (2004) Nucleic Acids Res , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 30
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • Lobley A, Whitmore L & Wallace BA (2002) DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 18, 211-212.
    • (2002) Bioinformatics , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 31
    • 0026795168 scopus 로고
    • Intermediates in denaturation of a small globular protein, recombinant human stefin B
    • Žerovnik E, Jerala R, Kroon-Žitko L, Pain RH & Turk V (1992) Intermediates in denaturation of a small globular protein, recombinant human stefin B. J Biol Chem 267, 9041-9046.
    • (1992) J Biol Chem , vol.267 , pp. 9041-9046
    • Žerovnik, E.1    Jerala, R.2    Kroon-Žitko, L.3    Pain, R.H.4    Turk, V.5
  • 35
    • 0037255361 scopus 로고    scopus 로고
    • Assembly of amyloid protofibrils via critical oligomers - A novel pathway of amyloid formation
    • Modler AJ, Gast K, Lutsch G & Damaschun G (2003) Assembly of amyloid protofibrils via critical oligomers - a novel pathway of amyloid formation. J Mol Biol 325, 135-148.
    • (2003) J Mol Biol , vol.325 , pp. 135-148
    • Modler, A.J.1    Gast, K.2    Lutsch, G.3    Damaschun, G.4
  • 39
    • 25844466988 scopus 로고    scopus 로고
    • In vitro study of stability and amyloid-fibril formation of two mutants of human stefin B (cystatin B) occurring in patients with EPM1
    • Rabzelj S, Turk V & Žerovnik E (2005) In vitro study of stability and amyloid-fibril formation of two mutants of human stefin B (cystatin B) occurring in patients with EPM1. Protein Sci 14, 2713-2722.
    • (2005) Protein Sci , vol.14 , pp. 2713-2722
    • Rabzelj, S.1    Turk, V.2    Žerovnik, E.3
  • 41
    • 0034705438 scopus 로고    scopus 로고
    • Copper (II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation
    • Qin K, Yang DS, Yang Y, Chishti MA, Meng LJ, Kretzschmar HA, Yip CM, Fraser PE & Westaway D (2000) Copper (II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation. Biol Chem 275, 19121-19131.
    • (2000) Biol Chem , vol.275 , pp. 19121-19131
    • Qin, K.1    Yang, D.S.2    Yang, Y.3    Chisti, M.A.4    Meng, L.J.5    Kretzschmar, H.A.6    Yip, C.M.7    Fraser, P.E.8    Westaway, D.9
  • 43
    • 0034654304 scopus 로고    scopus 로고
    • Consequences of manganese replacement of copper for prion protein function and proteinase resistance
    • Brown DR, Hafiz F, Glasssmith LL, Wong B-S, Jones IM, Clive C & Haswell SJ (2000) Consequences of manganese replacement of copper for prion protein function and proteinase resistance. EMBO J 19, 1180-1186.
    • (2000) EMBO J , vol.19 , pp. 1180-1186
    • Brown, D.R.1    Hafiz, F.2    Glasssmith, L.L.3    Wong, B.-S.4    Jones, I.M.5    Clive, C.6    Haswell, S.J.7
  • 45
    • 0028177269 scopus 로고
    • The beta A4 amyloid precursor protein binding to copper
    • Hesse L, Beher D, Masters CL & Multhaup G (1994) The beta A4 amyloid precursor protein binding to copper. FEBS Lett 349, 109-116.
    • (1994) FEBS Lett , vol.349 , pp. 109-116
    • Hesse, L.1    Beher, D.2    Masters, C.L.3    Multhaup, G.4
  • 46
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of copper interactions with alzheimer amyloid beta peptides: Identification of an attomolar-affinity copper binding site on amyloid beta1-42
    • Atwood CS, Scarpa RC, Huang X, Moir RD, Jones WD, Fairlie DP, Tanzi RE & Bush AI (2000) Characterization of copper interactions with alzheimer amyloid beta peptides: identification of an attomolar-affinity copper binding site on amyloid beta1-42. J Neurochem 75, 1219-1233.
    • (2000) J Neurochem , vol.75 , pp. 1219-1233
    • Atwood, C.S.1    Scarpa, R.C.2    Huang, X.3    Moir, R.D.4    Jones, W.D.5    Fairlie, D.P.6    Tanzi, R.E.7    Bush, A.I.8
  • 47
    • 0033430087 scopus 로고    scopus 로고
    • Copper inhibits beta-amyloid production and stimulates the non-amyloidogenic pathway of amyloid-precursor-protein secretion
    • Borchardt T, Camakaris J, Cappai R, Masters CL, Beyreuther K & Multhaup G (1999) Copper inhibits beta-amyloid production and stimulates the non-amyloidogenic pathway of amyloid-precursor-protein secretion. Biochem J 344, 461-467.
    • (1999) Biochem J , vol.344 , pp. 461-467
    • Borchardt, T.1    Camakaris, J.2    Cappai, R.3    Masters, C.L.4    Beyreuther, K.5    Multhaup, G.6
  • 49
    • 33644813233 scopus 로고    scopus 로고
    • A native to amyloidogenic transition regulated by a backbone trigger
    • Eakin CM, Berman AJ & Miranker AD (2005) A native to amyloidogenic transition regulated by a backbone trigger. Nat Struct Biol 13, 202-208.
    • (2005) Nat Struct Biol , vol.13 , pp. 202-208
    • Eakin, C.M.1    Berman, A.J.2    Miranker, A.D.3
  • 50
    • 0043011297 scopus 로고    scopus 로고
    • Cathepsin B but not cathepsins L or S contributes to the pathogenesis of Unverricht-Lundborg progressive myoclonus epilepsy (EPM1)
    • Houseweart MK, Pennacchio LA, Vilaythong A, Peters C, Noebels JL & Myers RM (2003) Cathepsin B but not cathepsins L or S contributes to the pathogenesis of Unverricht-Lundborg progressive myoclonus epilepsy (EPM1). J Neurobiol 56, 315-327.
    • (2003) J Neurobiol , vol.56 , pp. 315-327
    • Houseweart, M.K.1    Pennacchio, L.A.2    Vilaythong, A.3    Peters, C.4    Noebels, J.L.5    Myers, R.M.6
  • 51
    • 0022407298 scopus 로고
    • Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human liver
    • Ritonja A, Machleidt W & Barrett AJ (1985) Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human liver. Biochem Biophys Res Commun 131, 1187-1192.
    • (1985) Biochem Biophys Res Commun , vol.131 , pp. 1187-1192
    • Ritonja, A.1    Machleidt, W.2    Barrett, A.J.3
  • 52
    • 0023733116 scopus 로고
    • Cloning a synthetic gene for human stefin B and its expression in E. coli
    • Jerala R, Trstenjak M, Lenarčič B & Turk V (1988) Cloning a synthetic gene for human stefin B and its expression in E. coli. FEBS Lett 239, 41-44.
    • (1988) FEBS Lett , vol.239 , pp. 41-44
    • Jerala, R.1    Trstenjak, M.2    Lenarčič, B.3    Turk, V.4
  • 53
    • 30044443305 scopus 로고    scopus 로고
    • High affinity binding between copper and full-length prion protein identified by two different techniques
    • Thompsett AR, Abdelraheim SR, Daniels M & Brown DR (2005) High affinity binding between copper and full-length prion protein identified by two different techniques. J Biol Chem 280, 42750-42758.
    • (2005) J Biol Chem , vol.280 , pp. 42750-42758
    • Thompsett, A.R.1    Abdelraheim, S.R.2    Daniels, M.3    Brown, D.R.4
  • 54
    • 0034631701 scopus 로고    scopus 로고
    • 2+ (II) binding to His, GlyGlyHis, HisGlyHis, and bovine serum albumin: A critical evaluation
    • 2+ (II) binding to His, GlyGlyHis, HisGlyHis, and bovine serum albumin: a critical evaluation. Inorg Chem 39, 3057-3064.
    • (2000) Inorg Chem , vol.39 , pp. 3057-3064
    • Zhang, Y.1    Akilesh, S.2    Wilcox, D.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.