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Volumn 51, Issue 27, 2012, Pages 5394-5401

Mechanism of the chaperone-like and antichaperone activities of amyloid fibrils of Peptides from αa-Crystallin

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE; AMYLOID FIBRIL; CHAPERONE-LIKE ACTIVITY; COLLOIDAL DISPERSION; COLLOIDAL STABILITY; CYTOTOXIC; HYDROPHOBIC ENVIRONMENT; HYDROPHOBIC INTERACTIONS; NEGATIVE ZETA POTENTIALS; NEURODEGENERATIVE DISORDERS; POTENTIAL VALUES; PROTEIN AGGREGATION; SUBSTRATE BINDING; SUBSTRATE-BINDING SITES;

EID: 84863753570     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3004236     Document Type: Article
Times cited : (14)

References (40)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • DOI 10.1038/nature02261
    • Dobson, C. M. (2003) Protein folding and misfolding Nature 426, 884-890 (Pubitemid 38056880)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 79951761390 scopus 로고    scopus 로고
    • The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: Oligomer size or conformation?
    • Broersen, K., Rousseau, F., and Schymkowitz, J. (2010) The culprit behind amyloid beta peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation? Alzheimer's Res. Ther. 2, 12
    • (2010) Alzheimer's Res. Ther. , vol.2 , pp. 12
    • Broersen, K.1    Rousseau, F.2    Schymkowitz, J.3
  • 3
    • 0033968166 scopus 로고    scopus 로고
    • Small heat-shock proteins and their potential role in human disease
    • DOI 10.1016/S0959-440X(99)00048-2
    • Clark, J. I. and Muchowski, P. J. (2000) Small heat-shock proteins and their potential role in human disease Curr. Opin. Struct. Biol. 10, 52-59 (Pubitemid 30099327)
    • (2000) Current Opinion in Structural Biology , vol.10 , Issue.1 , pp. 52-59
    • Clark, J.I.1    Muchowski, P.J.2
  • 4
    • 0037325497 scopus 로고    scopus 로고
    • Alpha-crystallin
    • DOI 10.1016/S0014-4835(02)00278-6
    • Horwitz, J. (2003) Alpha-Crystallin Exp. Eye Res. 76, 145-153 (Pubitemid 36266698)
    • (2003) Experimental Eye Research , vol.76 , Issue.2 , pp. 145-153
    • Horwitz, J.1
  • 5
    • 77957296137 scopus 로고    scopus 로고
    • Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function
    • Laganowsky, A., Benesch, J. L., Landau, M., Ding, L., Sawaya, M. R., Cascio, D., Huang, Q., Robinson, C. V., Horwitz, J., and Eisenberg, D. (2010) Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function Protein Sci. 19, 1031-1043
    • (2010) Protein Sci. , vol.19 , pp. 1031-1043
    • Laganowsky, A.1    Benesch, J.L.2    Landau, M.3    Ding, L.4    Sawaya, M.R.5    Cascio, D.6    Huang, Q.7    Robinson, C.V.8    Horwitz, J.9    Eisenberg, D.10
  • 6
    • 0030798628 scopus 로고    scopus 로고
    • Chaperone-like activity and temperature-induced structural changes of α-crystallin
    • DOI 10.1074/jbc.272.38.23559
    • Raman, B. and Rao, C. M. (1997) Chaperone-like activity and temperature-induced structural changes of alpha-Crystallin J. Biol. Chem. 272, 23559-23564 (Pubitemid 27410925)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.38 , pp. 23559-23564
    • Raman, B.1    Rao, Ch.M.2
  • 8
    • 0035861759 scopus 로고    scopus 로고
    • Phe71 is essential for chaperone-like function in alpha A-Crystallin
    • Santhoshkumar, P. and Sharma, K. K. (2001) Phe71 is essential for chaperone-like function in alpha A-Crystallin J. Biol. Chem. 276, 47094-47099
    • (2001) J. Biol. Chem. , vol.276 , pp. 47094-47099
    • Santhoshkumar, P.1    Sharma, K.K.2
  • 9
    • 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 alphaA-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
  • 10
    • 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-alphaB-Crystallin: a functional element of alphaB-Crystallin with chaperone-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
  • 11
    • 27744485379 scopus 로고    scopus 로고
    • Interactive domains for chaperone activity in the small heat shock protein, human αB crystallin
    • DOI 10.1021/bi0503910
    • Ghosh, J. G., Estrada, M. R., and Clark, J. I. (2005) Interactive domains for chaperone activity in the small heat shock protein, human alphaB Crystallin Biochemistry 44, 14854-14869 (Pubitemid 41612265)
    • (2005) Biochemistry , vol.44 , Issue.45 , pp. 14854-14869
    • Ghosh, J.G.1    Estrada, M.R.2    Clark, J.I.3
  • 12
    • 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 alphaA-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
  • 13
    • 0035916279 scopus 로고    scopus 로고
    • Amyloid-induced aggregation and precipitation of soluble proteins: An electrostatic contribution of the Alzheimer's β(25-35) amyloid fibril
    • DOI 10.1021/bi002156h
    • Konno, T. (2001) Amyloid-induced aggregation and precipitation of soluble proteins: an electrostatic contribution of the Alzheimer's beta(25-35) amyloid fibril Biochemistry 40, 2148-2154 (Pubitemid 32165685)
    • (2001) Biochemistry , vol.40 , Issue.7 , pp. 2148-2154
    • Konno, T.1
  • 15
    • 79955709128 scopus 로고    scopus 로고
    • AlphaA-Crystallin peptide SDRDKFVIFLDVKHF accumulating in aging lens impairs the function of alpha-Crystallin and induces lens protein aggregation
    • Santhoshkumar, P., Raju, M., and Sharma, K. K. (2011) alphaA-Crystallin peptide SDRDKFVIFLDVKHF accumulating in aging lens impairs the function of alpha-Crystallin and induces lens protein aggregation PLoS One 6, e19291
    • (2011) PLoS One , vol.6 , pp. 19291
    • Santhoshkumar, P.1    Raju, M.2    Sharma, K.K.3
  • 16
    • 0000134186 scopus 로고
    • Theory of the stability of strongly charged lyophobic sols and of the adhesion of strongly charged particles in solution of electrolytes
    • Derjaguin, B. and Landa, L. (1941) Theory of the stability of strongly charged lyophobic sols and of the adhesion of strongly charged particles in solution of electrolytes Acta Physicochim. URSS 14, 633-662
    • (1941) Acta Physicochim. URSS , vol.14 , pp. 633-662
    • Derjaguin, B.1    Landa, L.2
  • 19
    • 0033543656 scopus 로고    scopus 로고
    • GroEL recognises sequential and non-sequential linear structural motifs compatible with extended β-strands and α-helices
    • DOI 10.1006/jmbi.1999.3040
    • Chatellier, J., Buckle, A. M., and Fersht, A. R. (1999) GroEL recognises sequential and non-sequential linear structural motifs compatible with extended beta-strands and alpha-helices J. Mol. Biol. 292, 163-172 (Pubitemid 29425661)
    • (1999) Journal of Molecular Biology , vol.292 , Issue.1 , pp. 163-172
    • Chatellier, J.1    Buckle, A.M.2    Fersht, A.R.3
  • 20
    • 0033543671 scopus 로고    scopus 로고
    • Identification of substrate binding site of GroEL minichaperone in solution
    • DOI 10.1006/jmbi.1999.3041
    • Tanaka, N. and Fersht, A. R. (1999) Identification of substrate binding site of GroEL minichaperone in solution J. Mol. Biol. 292, 173-180 (Pubitemid 29425662)
    • (1999) Journal of Molecular Biology , vol.292 , Issue.1 , pp. 173-180
    • Tanaka, N.1    Fersht, A.R.2
  • 21
    • 0034671267 scopus 로고    scopus 로고
    • From minichaperone to GroEL 2: Importance of avidity of the multisite ring structure
    • DOI 10.1006/jmbi.2000.4277
    • Chatellier, J., Hill, F., and Fersht, A. R. (2000) From Minichaperone to GroEL 2: Importance of Avidity of the Multisite Ring Structure J. Mol. Biol. 304, 883-896 (Pubitemid 32049014)
    • (2000) Journal of Molecular Biology , vol.304 , Issue.5 , pp. 883-896
    • Chatellier, J.1    Hill, F.2    Fersht, A.R.3
  • 23
    • 9344235453 scopus 로고    scopus 로고
    • Interaction of the N-terminal domain of Escherichia coli heat-shock protein ClpB and protein aggregates during chaperone activity
    • DOI 10.1110/ps.04780704
    • Tanaka, N., Tani, Y., Hattori, H., Tada, T., and Kunugi, S. (2004) Interaction of the N-terminal domain of Escherichia coli heat-shock protein ClpB and protein aggregates during chaperone activity Protein Sci. 13, 3214-3221 (Pubitemid 39557791)
    • (2004) Protein Science , vol.13 , Issue.12 , pp. 3214-3221
    • Tanaka, N.1    Tani, Y.2    Hattori, H.3    Tada, T.4    Kunugi, S.5
  • 24
    • 40749131329 scopus 로고    scopus 로고
    • Linkage-dependent contribution of repeat peptides to self-aggregation of three- or four-repeat microtubule-binding domains in tau protein
    • DOI 10.1111/j.1742-4658.2008.06312.x
    • Okuyama, K., Nishiura, C., Mizushima, F., Minoura, K., Sumida, M., Taniguchi, T., Tomoo, K., and Ishida, T. (2008) Linkage-dependent contribution of repeat peptides to self-aggregation of three- or four-repeat microtubule-binding domains in tau protein FEBS J. 275, 1529-1539 (Pubitemid 351388799)
    • (2008) FEBS Journal , vol.275 , Issue.7 , pp. 1529-1539
    • Okuyama, K.1    Nishiura, C.2    Mizushima, F.3    Minoura, K.4    Sumida, M.5    Taniguchi, T.6    Tomoo, K.7    Ishida, T.8
  • 25
    • 0041819641 scopus 로고    scopus 로고
    • Aggregation analysis of the microtubule binding domain in tau protein by spectroscopic methods
    • DOI 10.1093/jb/mvg116
    • Yao, T. M., Tomoo, K., Ishida, T., Hasegawa, H., Sasaki, M., and Taniguchi, T. (2003) Aggregation analysis of the microtubule binding domain in tau protein by spectroscopic methods J. Biochem. 134, 91-99 (Pubitemid 37071184)
    • (2003) Journal of Biochemistry , vol.134 , Issue.1 , pp. 91-99
    • Yao, T.-M.1    Tomoo, K.2    Ishida, T.3    Hasegawa, H.4    Sasaki, M.5    Taniguchi, T.6
  • 26
    • 0344442884 scopus 로고    scopus 로고
    • Prevention of thermal inactivation and aggregation of lysozyme by polyamines
    • DOI 10.1046/j.1432-1033.2003.03850.x
    • Kudou, M., Shiraki, K., Fujiwara, S., Imanaka, T., and Takagi, M. (2003) Prevention of thermal inactivation and aggregation of lysozyme by polyamines Eur. J. Biochem. 270, 4547-4554 (Pubitemid 37452531)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.22 , pp. 4547-4554
    • Kudou, M.1    Shiraki, K.2    Fujiwara, S.3    Imanaka, T.4    Takagi, M.5
  • 27
    • 0028788591 scopus 로고
    • Prevention of in vitro protein thermal aggregation by the Sulfolobus solfataricus chaperonin. Evidence for nonequivalent binding surfaces on the chaperonin molecule
    • Guagliardi, A., Cerchia, L., and Rossi, M. (1995) Prevention of in vitro protein thermal aggregation by the Sulfolobus solfataricus chaperonin. Evidence for nonequivalent binding surfaces on the chaperonin molecule J. Biol. Chem. 270, 28126-28132
    • (1995) J. Biol. Chem. , vol.270 , pp. 28126-28132
    • Guagliardi, A.1    Cerchia, L.2    Rossi, M.3
  • 28
    • 78650386372 scopus 로고    scopus 로고
    • Fibrillation of beta-lactoglobulin at low pH in the presence of a complexing anionic polysaccharide
    • Jones, O. G., Adamcik, J., Handschin, S., Bolisetty, S., and Mezzenga, R. (2010) Fibrillation of beta-lactoglobulin at low pH in the presence of a complexing anionic polysaccharide Langmuir 26, 17449-17458
    • (2010) Langmuir , vol.26 , pp. 17449-17458
    • Jones, O.G.1    Adamcik, J.2    Handschin, S.3    Bolisetty, S.4    Mezzenga, R.5
  • 29
    • 71549161144 scopus 로고    scopus 로고
    • Physical instability of a therapeutic Fc fusion protein: Domain contributions to conformational and colloidal stability
    • Fast, J. L., Cordes, A. A., Carpenter, J. F., and Randolph, T. W. (2009) Physical instability of a therapeutic Fc fusion protein: domain contributions to conformational and colloidal stability Biochemistry 48, 11724-11736
    • (2009) Biochemistry , vol.48 , pp. 11724-11736
    • Fast, J.L.1    Cordes, A.A.2    Carpenter, J.F.3    Randolph, T.W.4
  • 30
    • 0029784838 scopus 로고    scopus 로고
    • Amyloid β-protein and the genetics of Alzheimer's disease
    • Selkoe, D. J. (1996) Amyloid beta-protein and the genetics of Alzheimer's disease J. Biol. Chem. 271, 18295-18298 (Pubitemid 26322675)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.31 , pp. 18295-18298
    • Selkoe, D.J.1
  • 31
    • 84880187571 scopus 로고    scopus 로고
    • Tau protein, the paired helical filament and Alzheimer's disease
    • Goedert, M., Klug, A., and Crowther, R. A. (2006) Tau protein, the paired helical filament and Alzheimer's disease J. Alzheimer's Dis. 9, 195-207 (Pubitemid 44253313)
    • (2006) Journal of Alzheimer's Disease , vol.9 , Issue.SUPPL. 3 , pp. 195-207
    • Goedert, M.1    Klug, A.2    Crowther, R.A.3
  • 32
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer's disease amyloid hypothesis: A genetic perspective
    • DOI 10.1016/j.cell.2005.02.008
    • Tanzi, R. E. and Bertram, L. (2005) Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective Cell 120, 545-555 (Pubitemid 40269768)
    • (2005) Cell , vol.120 , Issue.4 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 33
    • 9444229933 scopus 로고    scopus 로고
    • Inhibition of amyloid fibrillogenesis and toxicity by a peptide chaperone
    • DOI 10.1023/B:MCBI.0000049373.15558.b8
    • Santhoshkumar, P. and Sharma, K. K. (2004) Inhibition of amyloid fibrillogenesis and toxicity by a peptide chaperone Mol. Cell. Biochem. 267, 147-155 (Pubitemid 39562395)
    • (2004) Molecular and Cellular Biochemistry , vol.267 , Issue.1-2 , pp. 147-155
    • Santhoshkumar, P.1    Sharma, K.K.2
  • 34
    • 0026755755 scopus 로고
    • Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro
    • Wille, H., Drewes, G., Biernat, J., Mandelkow, E. M., and Mandelkow, E. (1992) Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro J. Cell Biol. 118, 573-584
    • (1992) J. Cell Biol. , vol.118 , pp. 573-584
    • Wille, H.1    Drewes, G.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 38
    • 0037144424 scopus 로고    scopus 로고
    • Amyloid Fibril Formation by Pentapeptide and Tetrapeptide Fragments of Human Calcitonin
    • Reches, M., Porat, Y., and Gazit, E. (2002) Amyloid Fibril Formation by Pentapeptide and Tetrapeptide Fragments of Human Calcitonin J. Biol. Chem. 277, 35475-35480
    • (2002) J. Biol. Chem. , vol.277 , pp. 35475-35480
    • Reches, M.1    Porat, Y.2    Gazit, E.3


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