메뉴 건너뛰기




Volumn 1783, Issue 2, 2008, Pages 312-322

Cystatin B and its EPM1 mutants are polymeric and aggregate prone in vivo

Author keywords

Cellular aggregates; Cystatin B; Cytoskeleton; EPM1; Neurodegeneration; Polymers

Indexed keywords

CYSTATIN B; CYSTEINE; DIMER; DODECYL SULFATE SODIUM; HYDROGEN PEROXIDE; MONOMER; POLYMER; UREA;

EID: 38349087503     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2007.08.007     Document Type: Article
Times cited : (30)

References (60)
  • 1
    • 77957034551 scopus 로고
    • Cystatin, the egg white inhibitor of cysteine proteinases
    • Barret A.J., and Kirschke H. Cystatin, the egg white inhibitor of cysteine proteinases. Methods Enzymol. 80 (1981) 771
    • (1981) Methods Enzymol. , vol.80 , pp. 771
    • Barret, A.J.1    Kirschke, H.2
  • 2
    • 0020467150 scopus 로고
    • Human spleen cysteine proteinase inhibitor. Purification, fractionation into isoelectric variants and some properties of the variants
    • Jarvinen M., and Rinne A. Human spleen cysteine proteinase inhibitor. Purification, fractionation into isoelectric variants and some properties of the variants. Biochim. Biophys. Acta 708 (1982) 210
    • (1982) Biochim. Biophys. Acta , vol.708 , pp. 210
    • Jarvinen, M.1    Rinne, A.2
  • 3
    • 0025817602 scopus 로고
    • The cystatins: proteins inhibitors of cysteine proteinases
    • Turk V., and Bode W. The cystatins: proteins inhibitors of cysteine proteinases. FEBS Lett. 285 (1991) 213
    • (1991) FEBS Lett. , vol.285 , pp. 213
    • Turk, V.1    Bode, W.2
  • 4
    • 0025022426 scopus 로고
    • Evolution of proteins of the cystatin superfamily
    • Rawlings N.D., and Barrett A.J. Evolution of proteins of the cystatin superfamily. J. Mol. Evol. 30 (1990) 60-71
    • (1990) J. Mol. Evol. , vol.30 , pp. 60-71
    • Rawlings, N.D.1    Barrett, A.J.2
  • 5
    • 0031013054 scopus 로고    scopus 로고
    • Friends and relations of the cystatin superfamily-new members and their evolution
    • Brown W.M., and Dziegielewska K.M. Friends and relations of the cystatin superfamily-new members and their evolution. Protein Sci. 6 (1997) 5-12
    • (1997) Protein Sci. , vol.6 , pp. 5-12
    • Brown, W.M.1    Dziegielewska, K.M.2
  • 6
    • 0041813308 scopus 로고    scopus 로고
    • Molecular background of progressive myoclonus epilepsy
    • Lehesjoki A.E. Molecular background of progressive myoclonus epilepsy. EMBO J. 22 (2003) 3473-3478
    • (2003) EMBO J. , vol.22 , pp. 3473-3478
    • Lehesjoki, A.E.1
  • 7
    • 0025301658 scopus 로고
    • The refined 2.4A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction
    • Stubbs M., Laber B., Bode W., Huber R., Jerala R., Lenarcic B., and Turk V. The refined 2.4A 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 (1990) 1939-1947
    • (1990) EMBO J. , vol.9 , pp. 1939-1947
    • Stubbs, M.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5    Lenarcic, B.6    Turk, V.7
  • 10
    • 0036848257 scopus 로고    scopus 로고
    • New insights into the molecular basis of progressive myoclonus epilepsy (EPM1): a multiprotein complex with cystatin B
    • Di Giaimo R., Riccio M., Santi S., Galeotti C., Ambrosetti D.C., and Melli M. New insights into the molecular basis of progressive myoclonus epilepsy (EPM1): a multiprotein complex with cystatin B. Hum. Mol. Genet. 11 (2002) 2941-2950
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2941-2950
    • Di Giaimo, R.1    Riccio, M.2    Santi, S.3    Galeotti, C.4    Ambrosetti, D.C.5    Melli, M.6
  • 12
    • 33646067439 scopus 로고    scopus 로고
    • Towards novel anti-cancer strategies based on cystatin functions
    • Keppler D. Towards novel anti-cancer strategies based on cystatin functions. Cancer Lett. 235 (2006) 159-176
    • (2006) Cancer Lett. , vol.235 , pp. 159-176
    • Keppler, D.1
  • 13
    • 0026806875 scopus 로고
    • Cystatins-inhibitors of cysteine proteinases
    • Bobek L.A., and Levine M.J. Cystatins-inhibitors of cysteine proteinases. Crit. Rev. Oral Biol. Med. 3 (1987) 307-332
    • (1987) Crit. Rev. Oral Biol. Med. , vol.3 , pp. 307-332
    • Bobek, L.A.1    Levine, M.J.2
  • 14
    • 3042704064 scopus 로고    scopus 로고
    • Transcriptomic analysis in the leech Theromyzon tessulatum: involvement of cystatin B in innate immunity
    • Lefebvre C., Cocquerelle C., Vandenbulcke F., Hot D., Huot L., Lemoine L., and Salzet M. Transcriptomic analysis in the leech Theromyzon tessulatum: involvement of cystatin B in innate immunity. Biochem. J. 380 (2004) 617-625
    • (2004) Biochem. J. , vol.380 , pp. 617-625
    • Lefebvre, C.1    Cocquerelle, C.2    Vandenbulcke, F.3    Hot, D.4    Huot, L.5    Lemoine, L.6    Salzet, M.7
  • 15
    • 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., Ito H., Kominami E., and Hirano A. 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 (1993) 185-194
    • (1993) Virchows Arch., A Pathol. Anat. Histopathol. , vol.423 , pp. 185-194
    • Ii, K.1    Ito, H.2    Kominami, E.3    Hirano, A.4
  • 18
    • 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., Skarabot M., Kenig M., Guncar G., Musevic I., Turk D., and Zerovnik E. Different propensity to form amyloid fibrils by two homologous proteins-human stefins A and B: searching for an explanation. Proteins 55 (2004) 417-425
    • (2004) Proteins , vol.55 , pp. 417-425
    • Jenko, S.1    Skarabot, M.2    Kenig, M.3    Guncar, G.4    Musevic, I.5    Turk, D.6    Zerovnik, E.7
  • 19
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • Nilsson M.R. Techniques to study amyloid fibril formation in vitro. Methods 34 (2004) 151-160
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 20
    • 0035801540 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily
    • Staniforth R.A., Giannini S., Higgins L.D., Conroy M.J., Hounslow A.M., Jerala R., Craven C.J., and Waltho J.P. Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. EMBO J. 20 (2001) 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
  • 22
    • 33748480307 scopus 로고    scopus 로고
    • Unverricht-Lundborg disease (PME1)
    • Genton P. Unverricht-Lundborg disease (PME1). Rev. Neurol. (Paris) 162 (2006) 819-826
    • (2006) Rev. Neurol. (Paris) , vol.162 , pp. 819-826
    • Genton, P.1
  • 23
    • 0020561801 scopus 로고
    • 'Baltic' myoclonus epilepsy: hereditary disorder of childhood made worse by phenytoin
    • Eldridge R., Iivanainen M., Stern R., Koerber T., and Wilderý` B.J. 'Baltic' myoclonus epilepsy: hereditary disorder of childhood made worse by phenytoin. Lancet 8 (1983) 838-842
    • (1983) Lancet , vol.8 , pp. 838-842
    • Eldridge, R.1    Iivanainen, M.2    Stern, R.3    Koerber, T.4    Wilderý, B.J.5
  • 29
    • 3142757512 scopus 로고    scopus 로고
    • Multifluorescence labeling and colocalization analysis
    • Riccio M., Dembic M., Cinti C., and Santi S. Multifluorescence labeling and colocalization analysis. Methods Mol. Biol. 285 (2004) 171-177
    • (2004) Methods Mol. Biol. , vol.285 , pp. 171-177
    • Riccio, M.1    Dembic, M.2    Cinti, C.3    Santi, S.4
  • 30
    • 0026795168 scopus 로고
    • Intermediates in denaturation of a small globular protein, recombinant human stefin B
    • Zerovnik E., Jerala R., Kroon-Zitko L., Pain R.H., and Turk V. Intermediates in denaturation of a small globular protein, recombinant human stefin B. J. Biol Chem. 267 (1992) 9041-9046
    • (1992) J. Biol Chem. , vol.267 , pp. 9041-9046
    • Zerovnik, E.1    Jerala, R.2    Kroon-Zitko, L.3    Pain, R.H.4    Turk, V.5
  • 31
    • 0030974942 scopus 로고    scopus 로고
    • Characterization of the equilibrium intermediates in acid denaturation of human stefin B
    • Zerovnik E., Jerala R., Kroon-Zitko L., Turk V., and Lohner K. Characterization of the equilibrium intermediates in acid denaturation of human stefin B. Eur. J. Biochem. 245 (1997) 364-372
    • (1997) Eur. J. Biochem. , vol.245 , pp. 364-372
    • Zerovnik, E.1    Jerala, R.2    Kroon-Zitko, L.3    Turk, V.4    Lohner, K.5
  • 33
    • 0042164949 scopus 로고    scopus 로고
    • Redox proteomics: identification of oxidatively modified proteins
    • Ghezzi P., and Bonetto V. Redox proteomics: identification of oxidatively modified proteins. Proteomics 3 (2003) 1145-1153
    • (2003) Proteomics , vol.3 , pp. 1145-1153
    • Ghezzi, P.1    Bonetto, V.2
  • 34
    • 33646576172 scopus 로고    scopus 로고
    • The role of cystatin C in cerebral amyloid angiopathy and stroke: cell biology and animal models
    • Levy E., Jaskolski M., and Grubb A. The role of cystatin C in cerebral amyloid angiopathy and stroke: cell biology and animal models. Brain Pathol. 16 (2006) 60-70
    • (2006) Brain Pathol. , vol.16 , pp. 60-70
    • Levy, E.1    Jaskolski, M.2    Grubb, A.3
  • 35
    • 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., and Zerovnik E. 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 (2005) 2713-2722
    • (2005) Protein Sci. , vol.14 , pp. 2713-2722
    • Rabzelj, S.1    Turk, V.2    Zerovnik, E.3
  • 36
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski P.J., and Wacker J.L. Modulation of neurodegeneration by molecular chaperones. Nat. Rev., Neurosci. 6 (2005) 11-22
    • (2005) Nat. Rev., Neurosci. , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 37
    • 0035862167 scopus 로고    scopus 로고
    • Nuclear localization of cystatin B, the cathepsin inhibitor implicated in myoclonous epilepsy (EPM1)
    • Di Giaimo R., Pianetti S., Calmieri P.P., Melli M., and Santi S. Nuclear localization of cystatin B, the cathepsin inhibitor implicated in myoclonous epilepsy (EPM1). Exp. Cell Res. 262 (2001) 84-94
    • (2001) Exp. Cell Res. , vol.262 , pp. 84-94
    • Di Giaimo, R.1    Pianetti, S.2    Calmieri, P.P.3    Melli, M.4    Santi, S.5
  • 39
    • 4444330121 scopus 로고    scopus 로고
    • Structural basis of protein kinetic stability: resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward beta-sheet structure
    • Manning M., and Colòn W. Structural basis of protein kinetic stability: resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward beta-sheet structure. Biochemistry 43 (2004) 11248-11254
    • (2004) Biochemistry , vol.43 , pp. 11248-11254
    • Manning, M.1    Colòn, W.2
  • 40
    • 33748304111 scopus 로고    scopus 로고
    • High affinity copper binding by stefin B (cystatin B) and its role in the inhibition of amyloid fibrillation
    • Zerovnik E., Skerget K., Tusek-Znidaric M., Loeschner C., Brazier M.W., and Brown D.R. High affinity copper binding by stefin B (cystatin B) and its role in the inhibition of amyloid fibrillation. FEBS J. 273 (2006) 4250-4263
    • (2006) FEBS J. , vol.273 , pp. 4250-4263
    • Zerovnik, E.1    Skerget, K.2    Tusek-Znidaric, M.3    Loeschner, C.4    Brazier, M.W.5    Brown, D.R.6
  • 41
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., Rowan M.J., and Selkoe D.J. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002) 535-539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 42
    • 14944378094 scopus 로고    scopus 로고
    • Certain inhibitors of synthetic amyloid beta-peptide (Abeta) fibrillogenesis block oligomerization of natural Abeta and thereby rescue long-term potentiation
    • Walsh D.M., Townsend M., Podlisn M.B., Shanka G.M., Fadeev J.V., Agnaf O.E., Hartley D.M., and Selkoe D.J. Certain inhibitors of synthetic amyloid beta-peptide (Abeta) fibrillogenesis block oligomerization of natural Abeta and thereby rescue long-term potentiation. J. Neurosci. 25 (2005) 2455-2462
    • (2005) J. Neurosci. , vol.25 , pp. 2455-2462
    • Walsh, D.M.1    Townsend, M.2    Podlisn, M.B.3    Shanka, G.M.4    Fadeev, J.V.5    Agnaf, O.E.6    Hartley, D.M.7    Selkoe, D.J.8
  • 46
    • 2642567686 scopus 로고    scopus 로고
    • Prevention of domain swapping inhibits dimerization and amyloid fibril formation of cystatin C: use of engineered disulfide bridges, antibodies, and carboxymethylpapain to stabilize the monomeric form of cystatin C
    • Nilsson M., Wang X., Rodziewicz-Motowidlo S., Janowski R., Lindstrom V., Onnerfjord P., Westermark G., Grzonka Z., Jaskolski M., and Grubb A. Prevention of domain swapping inhibits dimerization and amyloid fibril formation of cystatin C: use of engineered disulfide bridges, antibodies, and carboxymethylpapain to stabilize the monomeric form of cystatin C. J. Biol. Chem. 279 (2004) 24236-24245
    • (2004) J. Biol. Chem. , vol.279 , pp. 24236-24245
    • Nilsson, M.1    Wang, X.2    Rodziewicz-Motowidlo, S.3    Janowski, R.4    Lindstrom, V.5    Onnerfjord, P.6    Westermark, G.7    Grzonka, Z.8    Jaskolski, M.9    Grubb, A.10
  • 47
    • 34547111066 scopus 로고    scopus 로고
    • Fibrillogenic oligomers of human cystatin c are formed by propagated domain swapping
    • Wahlbom M., Wang X., Lindström V., Carlemalm E., Jaskolski M., and Grubb A. Fibrillogenic oligomers of human cystatin c are formed by propagated domain swapping. J. Biol. Chem. 282 25 (June 22 2007) 18318-18326
    • (2007) J. Biol. Chem. , vol.282 , Issue.25 , pp. 18318-18326
    • Wahlbom, M.1    Wang, X.2    Lindström, V.3    Carlemalm, E.4    Jaskolski, M.5    Grubb, A.6
  • 48
    • 33646126278 scopus 로고    scopus 로고
    • New insights into prion structure and toxicity
    • Harris D.A., and True H.L. New insights into prion structure and toxicity. Neuron 50 (2006) 353-357
    • (2006) Neuron , vol.50 , pp. 353-357
    • Harris, D.A.1    True, H.L.2
  • 49
    • 0035818579 scopus 로고    scopus 로고
    • Specificity in intracellular protein aggregation and inclusion body formation
    • Rajan R.S., Illing M.E., Bence N.F., and Kopito R.R. Specificity in intracellular protein aggregation and inclusion body formation. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 13060-13065
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 13060-13065
    • Rajan, R.S.1    Illing, M.E.2    Bence, N.F.3    Kopito, R.R.4
  • 50
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10 (2000) 524-530
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 51
    • 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 M.K., Pennacchio L.A., Vilaythong A., Peters C., Noebels J.L., and Myers R.M. Cathepsin B but not cathepsins L or S contributes to the pathogenesis of Unverricht-Lundborg progressive myoclonus epilepsy (EPM1). J. Neurobiol. 56 (2003) 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
  • 53
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: amyloid growth occurs by monomer addition
    • Collins S.R., Douglass A., Vale R.D., and Weissman J.S. Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol. 2 (2004) 1582-1590
    • (2004) PLoS Biol. , vol.2 , pp. 1582-1590
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 54
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 426 (2003) 884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 55
    • 0030728226 scopus 로고    scopus 로고
    • Mad cows meet psichotic yeast: the expansion of the prion hypothesis
    • Lindquist S. Mad cows meet psichotic yeast: the expansion of the prion hypothesis. Cell 89 (1997) 495-498
    • (1997) Cell , vol.89 , pp. 495-498
    • Lindquist, S.1
  • 57
    • 0037986392 scopus 로고    scopus 로고
    • Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis
    • Berson J.F., Theos A.C., Harper D.C., Tenza D., Raposo G., and Marks M.S. Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis. J. Cell Biol. 161 (2003) 521-533
    • (2003) J. Cell Biol. , vol.161 , pp. 521-533
    • Berson, J.F.1    Theos, A.C.2    Harper, D.C.3    Tenza, D.4    Raposo, G.5    Marks, M.S.6
  • 59
    • 0038612852 scopus 로고    scopus 로고
    • Amyloid as a natural product
    • Kelly J.W., and Balch W.E. Amyloid as a natural product. J. Cell Biol. 12 (2003) 461-462
    • (2003) J. Cell Biol. , vol.12 , pp. 461-462
    • Kelly, J.W.1    Balch, W.E.2
  • 60
    • 15244363811 scopus 로고    scopus 로고
    • Protein aggregation as a possible cause for pathology in a subset of familial Unverricht-Lundborg disease
    • Ceru S., Rabzelj S., Kopitar-Jerala N., Turk V., and Zerovnik E. Protein aggregation as a possible cause for pathology in a subset of familial Unverricht-Lundborg disease. Med. Hypotheses 64 (2005) 955
    • (2005) Med. Hypotheses , vol.64 , pp. 955
    • Ceru, S.1    Rabzelj, S.2    Kopitar-Jerala, N.3    Turk, V.4    Zerovnik, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.