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Volumn 287, Issue 43, 2012, Pages 36423-36434

Chaperone activity of small heat shock proteins underlies therapeutic efficacy in experimental autoimmune encephalomyelitis

Author keywords

[No Author keywords available]

Indexed keywords

ADDITIONAL STRUCTURES; AMYLOID FIBRIL; CHAPERONE ACTIVITY; CRYSTALLIN; EXPERIMENTAL AUTOIMMUNE ENCEPHALOMYELITIS; HYDROPHOBIC AMINO ACIDS; LINEAR REGION; MYCOBACTERIAL; SMALL HEAT SHOCK PROTEINS; THERAPEUTIC ACTIVITY; THERAPEUTIC EFFICACY; THERAPEUTIC FUNCTIONS;

EID: 84867808822     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.371229     Document Type: Article
Times cited : (50)

References (49)
  • 1
  • 2
    • 0036359595 scopus 로고    scopus 로고
    • Evolution and diversity of prokaryotic small heat shock proteins
    • Kappé, G., Leunissen, J. A., and de Jong, W. W. (2002) Evolution and diversity of prokaryotic small heat shock proteins. Prog. Mol. Subcell Biol. 28, 1-17
    • (2002) Prog. Mol. Subcell Biol. , vol.28 , pp. 1-17
    • Kappé, G.1    Leunissen, J.A.A.2    De Jong, W.W.3
  • 3
    • 0036195722 scopus 로고    scopus 로고
    • α-Crystallin-type heat shock proteins. Socializingminichaperones in the context of a multichaperone network
    • Narberhaus, F. (2002) α-Crystallin-type heat shock proteins. Socializingminichaperones in the context of a multichaperone network. Microbiol. Mol. Biol. Rev. 66, 64-93
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 64-93
    • Narberhaus, F.1
  • 4
    • 0035844174 scopus 로고    scopus 로고
    • The small heat shock protein αB-crystallin negatively regulates cytochrome c- And caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation
    • Kamradt, M. C., Chen, F., and Cryns, V. L. (2001) The small heat shock protein αB-crystallin negatively regulates cytochrome c- and caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation. J. Biol. Chem. 276, 16059-16063
    • (2001) J. Biol. Chem. , vol.276 , pp. 16059-16063
    • Kamradt, M.C.1    Chen, F.A.2    Cryns, V.L.3
  • 6
    • 33846297971 scopus 로고    scopus 로고
    • Small heat shock protein αB-crystallin binds to p53 to sequester its translocation to mitochondria during hydrogen peroxide-induced apoptosis
    • DOI 10.1016/j.bbrc.2006.12.152, PII S0006291X06028300
    • Liu, S., Li, J., Tao, Y., and Xiao, X. (2007) Small heat shock protein αB-crystallinbinds to p53 to sequester its translocation to mitochondria during hydrogen peroxide-induced apoptosis. Biochem. Biophys. Res. Commun. 354, 109-114 (Pubitemid 46123208)
    • (2007) Biochemical and Biophysical Research Communications , vol.354 , Issue.1 , pp. 109-114
    • Liu, S.1    Li, J.2    Tao, Y.3    Xiao, X.4
  • 7
    • 2442681777 scopus 로고    scopus 로고
    • s to sequester their translocation during staurosporine-induced apoptosis
    • DOI 10.1038/sj.cdd.4401384
    • Mao, Y. W., Liu, J. P., Xiang, H., and Li, D. W. (2004) Human αA- andαB-crystallins bind to Bax and Bcl-X(S) to sequester their translocationduring staurosporine-induced apoptosis. Cell Death Differ. 11, 512-526 (Pubitemid 38660137)
    • (2004) Cell Death and Differentiation , vol.11 , Issue.5 , pp. 512-526
    • Mao, Y.-W.1    Liu, J.-P.2    Xiang, H.3    Li, D.W.-C.4
  • 9
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • DOI 10.1038/29106
    • Kim, K. K., Kim, R., and Kim, S. H. (1998) Crystal structure of a small heat shock protein. Nature 394, 595-599 (Pubitemid 28366837)
    • (1998) Nature , vol.394 , Issue.6693 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.-H.3
  • 12
    • 1442289304 scopus 로고    scopus 로고
    • Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae
    • DOI 10.1038/sj.emboj.7600080
    • Haslbeck, M., Braun, N., Stromer, T., Richter, B., Model, N., Weinkauf, S., and Buchner, J. (2004) Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. EMBO J. 23, 638-649 (Pubitemid 38282395)
    • (2004) EMBO Journal , vol.23 , Issue.3 , pp. 638-649
    • Haslbeck, M.1    Braun, N.2    Stromer, T.3    Richter, B.4    Model, N.5    Weinkauf, S.6    Buchner, J.7
  • 13
    • 0036366373 scopus 로고    scopus 로고
    • The small heat shock proteins of the nematode Caenorhabditis elegans. Structure, regulation, and biology
    • Candido, E. P. (2002) The small heat shock proteins of the nematode Caenorhabditis elegans. Structure, regulation, and biology. Prog. Mol. Subcell. Biol. 28, 61-78
    • (2002) Prog. Mol. Subcell. Biol. , vol.28 , pp. 61-78
    • Candido, E.P.1
  • 14
    • 16544382615 scopus 로고    scopus 로고
    • The IXI/V motif in the C-terminal extension of α-crystallins: Alternative interactions and oligomeric assemblies
    • Pasta, S. Y., Raman, B., Ramakrishna, T., and Rao, ChM. (2004) The IXI/V motif in the C-terminal extension of α-crystallins. Alternative interactionsand oligomeric assemblies. Mol. Vis. 10, 655-662 (Pubitemid 41358231)
    • (2004) Molecular Vision , vol.10 , pp. 655-662
    • Pasta, S.Y.1    Raman, B.2    Ramakrishna, T.3    Rao, C..M.4
  • 15
    • 0033984092 scopus 로고    scopus 로고
    • Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation
    • DOI 10.1074/jbc.275.2.1095
    • Sugiyama, Y., Suzuki, A., Kishikawa, M., Akutsu, R., Hirose, T., Waye, M. M., Tsui, S. K., Yoshida, S., and Ohno, S. (2000) Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation. J. Biol. Chem. 275, 1095-1104 (Pubitemid 30051159)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.2 , pp. 1095-1104
    • Sugiyama, Y.1    Suzuki, A.2    Kishikawa, M.3    Akutsu, R.4    Hirose, T.5    Waye, M.M.Y.6    Tsui, S.K.W.7    Yoshida, S.8    Ohno, S.9
  • 18
    • 34548067977 scopus 로고    scopus 로고
    • Residue R120 is essential for the quaternary structure and functional integrity of human αB-crystallin
    • DOI 10.1021/bi7003125
    • Simon, S., Michiel, M., Skouri-Panet, F., Lechaire, J. P., Vicart, P., and Tardieu, A. (2007) Residue Arg-120 is essential for the quaternary structure and functional integrity of human αB-crystallin. Biochemistry 46, 9605-9614 (Pubitemid 47291967)
    • (2007) Biochemistry , vol.46 , Issue.33 , pp. 9605-9614
    • Simon, S.1    Michiel, M.2    Skouri-Panet, F.3    Lechaire, J.P.4    Vicart, P.5    Tardieu, A.6
  • 19
    • 2342455798 scopus 로고    scopus 로고
    • Desmin Aggregate Formation by R120G αB-Crystallin Is Caused by Altered Filament Interactions and Is Dependent upon Network Status in Cells
    • DOI 10.1091/mbc.E03-12-0893
    • Perng, M. D., Wen, S. F., van den IJssel, P., Prescott, A. R., and Quinlan, R. A. (2004) Desmin aggregate formation by R120G αB-crystallin is causedby altered filament interactions and is dependent upon network status in cells. Mol. Biol. Cell 15, 2335-2346 (Pubitemid 38580650)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.5 , pp. 2335-2346
    • Perng, M.D.1    Wen, S.F.2    Van Den, I.P.3    Prescott, A.R.4    Quinlan, R.A.5
  • 20
    • 0032586878 scopus 로고    scopus 로고
    • Mutation R120G in αB-crystallin, which islinked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function
    • Bova, M. P., Yaron, O., Huang, Q., Ding, L., Haley, D. A., Stewart, P. L., and Horwitz, J. (1999) Mutation R120G in αB-crystallin, which islinked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. Proc. Natl. Acad. Sci. U.S.A. 96, 6137- 6142
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6137-6142
    • Bova, M.P.1    Yaron, O.2    Huang, Q.3    Ding, L.4    Haley, D.A.5    Stewart, P.L.A.6    Horwitz, J.7
  • 21
    • 79953253901 scopus 로고    scopus 로고
    • Crystal structure of R120G disease mutant of human αB-crystallin domaindimer shows closure of a groove
    • Clark, A. R., Naylor, C. E., Bagnéris, C., Keep, N. H., and Slingsby, C. (2011) Crystal structure of R120G disease mutant of human αB-crystallin domaindimer shows closure of a groove. J. Mol. Biol. 408, 118-134
    • (2011) J. Mol. Biol. , vol.408 , pp. 118-134
    • Clark, A.R.1    Naylor, C.E.2    Bagnéris, C.3    Keep, N.H.A.4    Slingsby, C.5
  • 22
    • 0037358061 scopus 로고    scopus 로고
    • The human genome encodes 10 β-crystallin-related small heat shock proteins: HspB1-10
    • DOI 10.1379/1466-1268(2003)8<53:THGECS>2.0.CO;2
    • Kappé, G., Franck, E., Verschuure, P., Boelens, W. C., Leunissen, J. A., and de Jong, W. W. (2003) The human genome encodes 10 β-crystallin-relatedsmall heat shock proteins. HspB1-10. Cell Stress Chaperones 8, 53-61 (Pubitemid 36444090)
    • (2003) Cell Stress and Chaperones , vol.8 , Issue.1 , pp. 53-61
    • Kappe, G.1    Franck, E.2    Verschuure, P.3    Boelens, W.C.4    Leunissen, J.A.M.5    De Jong, W.W.6
  • 28
    • 79958761661 scopus 로고    scopus 로고
    • Functional rescue of experimental ischemic optic neuropathy with αB-crystallin
    • Pangratz-Fuehrer, S., Kaur, K., Ousman, S. S., Steinman, L., and Liao, Y. J. (2011) Functional rescue of experimental ischemic optic neuropathy with αB-crystallin. Eye 25, 809-817
    • (2011) Eye , vol.25 , pp. 809-817
    • Pangratz-Fuehrer, S.1    Kaur, K.2    Ousman, S.S.3    Steinman, L.A.4    Liao, Y.J.5
  • 30
    • 20444393171 scopus 로고    scopus 로고
    • A rapid and efficient protocol to purify biologically active recombinant proteins from mammalian cells
    • DOI 10.1016/j.pep.2005.03.035, PII S1046592805001245
    • Cazalla, D., Sanford, J. R., and Cáceres, J. F. (2005) A rapid and efficient protocol to purify biologically active recombinant proteins from mammalian cells. Protein Expr. Purif. 42, 54-58 (Pubitemid 40793393)
    • (2005) Protein Expression and Purification , vol.42 , Issue.1 , pp. 54-58
    • Cazalla, D.1    Sanford, J.R.2    Caceres, J.F.3
  • 31
    • 79955035421 scopus 로고    scopus 로고
    • Chaperone activity of αB-crystallin is responsible for its incorrect assignment as an autoantigenin multiple sclerosis
    • Rothbard, J. B., Zhao, X., Sharpe, O., Strohman, M. J., Kurnellas, M., Mellins, E. D., Robinson, W. H., and Steinman, L. (2011) Chaperone activity of αB-crystallin is responsible for its incorrect assignment as an autoantigenin multiple sclerosis. J. Immunol. 186, 4263-4268
    • (2011) J. Immunol. , vol.186 , pp. 4263-4268
    • Rothbard, J.B.1    Zhao, X.2    Sharpe, O.3    Strohman, M.J.4    Kurnellas, M.5    Mellins, E.D.6    Robinson, W.H.A.7    Steinman, L.8
  • 32
    • 0034700141 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake. Peptoid molecular transporters
    • Wender, P. A., Mitchell, D. J., Pattabiraman, K., Pelkey, E. T., Steinman, L., and Rothbard, J. B. (2000) The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake. Peptoid molecular transporters. Proc. Natl. Acad. Sci. U.S.A. 97, 13003-13008
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13003-13008
    • Wender, P.A.1    Mitchell, D.J.2    Pattabiraman, K.3    Pelkey, E.T.4    Steinman, L.A.5    Rothbard, J.B.6
  • 33
    • 33644690454 scopus 로고    scopus 로고
    • Mini-αB-crystallin: A functional element of αB-crystallin with chaperone-like activity
    • DOI 10.1021/bi0518141
    • Bhattacharyya, J., Padmanabha Udupa, E. G., Wang, J., and Sharma, K. K. (2006) Mini-αB-crystallin. A functional element of αB-crystallin withchaperone-like activity. Biochemistry 45, 3069-3076 (Pubitemid 43334555)
    • (2006) Biochemistry , vol.45 , Issue.9 , pp. 3069-3076
    • Bhattacharyya, J.1    Udupa, E.G.P.2    Wang, J.3    Sharma, K.K.4
  • 35
    • 33745728404 scopus 로고    scopus 로고
    • How to successfully apply animal studies in experimental allergic encephalomyelitis to research on multiple sclerosis
    • Steinman, L., and Zamvil, S. S. (2006) How to successfully apply animal studies in experimental allergic encephalomyelitis to research on multiple sclerosis. Ann. Neurol. 60, 12-21
    • (2006) Ann. Neurol. , vol.60 , pp. 12-21
    • Steinman, L.A.1    Zamvil, S.S.2
  • 36
    • 33751120442 scopus 로고    scopus 로고
    • Conserved F84 and P86 residues in αB-crystallin are essential to effectively prevent the aggregation of substrate proteins
    • DOI 10.1110/ps.062338206
    • Santhoshkumar, P., and Sharma, K. K. (2006) Conserved Phe-84 and Pro-86 residues in αB-crystallin are essential to effectively prevent theaggregation of substrate proteins. Protein Sci. 15, 2488-2498 (Pubitemid 44771686)
    • (2006) Protein Science , vol.15 , Issue.11 , pp. 2488-2498
    • Santhoshkumar, P.1    Sharma, K.K.2
  • 37
    • 0034635397 scopus 로고    scopus 로고
    • Synthesis and characterization of a peptide identified as a functional element in αA-crystallin
    • DOI 10.1074/jbc.275.6.3767
    • Sharma, K. K., Kumar, R. S., Kumar, G. S., and Quinn, P. T. (2000) Synthesis and characterization of a peptide identified as a functional element in αA-crystallin. J. Biol. Chem. 275, 3767-3771 (Pubitemid 30094597)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.6 , pp. 3767-3771
    • Sharma, K.K.1    Kumar, R.S.2    Kumar, G.S.3    Quinn, P.T.4
  • 38
    • 40149109190 scopus 로고    scopus 로고
    • Amyloid fibril formation and chaperone-like activity of peptides from αA-Crystallin
    • DOI 10.1021/bi701823g
    • Tanaka, N., Tanaka, R., Tokuhara, M., Kunugi, S., Lee, Y. F., and Hamada, D. (2008) Amyloid fibril formation and chaperone-like activity of peptides from αA-crystallin. Biochemistry 47, 2961-2967 (Pubitemid 351328849)
    • (2008) Biochemistry , vol.47 , Issue.9 , pp. 2961-2967
    • Tanaka, N.1    Tanaka, R.2    Tokuhara, M.3    Kunugi, S.4    Lee, Y.-F.5    Hamada, D.6
  • 41
    • 20444440728 scopus 로고    scopus 로고
    • Structure of the cross-β spine of amyloid-like fibrils
    • DOI 10.1038/nature03680
    • Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. Ø., Riekel, C., Grothe, R., and Eisenberg, D. (2005) Structure of the cross-β spine of amyloid-like fibrils. Nature 435, 773-778 (Pubitemid 40839722)
    • (2005) Nature , vol.435 , Issue.7043 , pp. 773-778
    • Nelson, R.1    Sawaya, M.R.2    Balbirnie, M.3    Madsen, A.O.4    Riekel, C.5    Grothe, R.6    Eisenberg, D.7
  • 42
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • DOI 10.1038/nbt1012
    • Fernandez-Escamilla, A. M., Rousseau, F., Schymkowitz, J., and Serrano, L. (2004) Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 22, 1302-1306 (Pubitemid 39336784)
    • (2004) Nature Biotechnology , vol.22 , Issue.10 , pp. 1302-1306
    • Fernandez-Escamilla, A.-M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 45
  • 46
    • 0032502739 scopus 로고    scopus 로고
    • Interaction of 1,1′-bi(4-anilino)-naphthalene-5,5′-disulfonic acid with α-crystallin
    • Sharma, K. K., Kaur, H., Kumar, G. S., and Kester, K. (1998) Interaction of 1,1′-bi(4-anilino)-naphthalene-5,5′-disulfonic acid with α-crystallin.J. Biol. Chem. 273, 8965-8970
    • (1998) J. Biol. Chem. , vol.273 , pp. 8965-8970
    • Sharma, K.K.1    Kaur, H.2    Kumar, G.S.A.3    Kester, K.4
  • 48
    • 84864553199 scopus 로고    scopus 로고
    • Reversal of paralysis and reduced inflammation from peripheral administration of β-amyloid in TH1 and TH17 versions of experimental autoimmune encephalomyelitis
    • Grant, J. L., Ghosn, E. E., Axtell, R. C., Herges, K., Kuipers, H. F., Woodling, N. S., Andreasson, K., Herzenberg, L. A., and Steinman, L. (2012) Reversal of paralysis and reduced inflammation from peripheral administration of β-amyloid in TH1 and TH17 versions of experimental autoimmune encephalomyelitis.Sci. Transl. Med. 4, 145
    • (2012) Sci. Transl. Med. , vol.4 , pp. 145
    • Grant, J.L.1    Ghosn, E.E.2    Axtell, R.C.3    Herges, K.4    Kuipers, H.F.5    Woodling, N.S.6    Andreasson, K.7    Herzenberg, L.A.A.8    Steinman, L.9
  • 49
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg, D., and Jucker, M. (2012) The amyloid state of proteins in human diseases. Cell 148, 1188-1203
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.A.1    Jucker, M.2


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