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Volumn 121, Issue 1, 2003, Pages 27-32

Small heat shock proteins participate in the regulation of cellular aggregates of misfolded protein

Author keywords

B crystallin; Comformational disease; Hsp27; Inclusion body

Indexed keywords

ALPHA B CRYSTALLIN; ALPHA CRYSTALLIN; CHAPERONE; DESMIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 27; POLYGLUTAMINE; PROTEASOME INHIBITOR; UNCLASSIFIED DRUG;

EID: 0037239023     PISSN: 00155691     EISSN: None     Source Type: Journal    
DOI: 10.1254/fpj.121.27     Document Type: Review
Times cited : (7)

References (28)
  • 2
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman MY and Goldberg AL: Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 29, 15-32 (2001)
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 3
    • 0028903455 scopus 로고
    • The expanding small heat-shock protein family, and structure predictions of the conserved "α-crystallin domain"
    • Caspers GJ, Leunissen JA and de Jong WW: The expanding small heat-shock protein family, and structure predictions of the conserved "α-crystallin domain". J Mol Evol 40, 238-248 (1995)
    • (1995) J Mol Evol , vol.40 , pp. 238-248
    • Caspers, G.J.1    Leunissen, J.A.2    De Jong, W.W.3
  • 4
    • 0026774629 scopus 로고
    • Copurification of small heat-shock protein with αB-crystallin from human skeletal muscle
    • Kato K, Shinohara H, Goto S, Inaguma Y, Morishita R and Asano T: Copurification of small heat-shock protein with αB-crystallin from human skeletal muscle. J Biol Chem 267, 7718-7725 (1992)
    • (1992) J Biol Chem , vol.267 , pp. 7718-7725
    • Kato, K.1    Shinohara, H.2    Goto, S.3    Inaguma, Y.4    Morishita, R.5    Asano, T.6
  • 6
    • 0028346451 scopus 로고
    • Dissocisation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27
    • Kato K, Hasegawa K, Goto S and Inaguma Y: Dissocisation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27. J Biol Chem 269, 11274-11278 (1994)
    • (1994) J Biol Chem , vol.269 , pp. 11274-11278
    • Kato, K.1    Hasegawa, K.2    Goto, S.3    Inaguma, Y.4
  • 7
    • 0030613774 scopus 로고    scopus 로고
    • Phosphorylation of αB-crystallin in response to various types of stress
    • Ito H, Okamoto K, Nakayama H, Isobe T and Kato K: Phosphorylation of αB-crystallin in response to various types of stress. J Biol Chem 272, 29934-29941 (1997)
    • (1997) J Biol Chem , vol.272 , pp. 29934-29941
    • Ito, H.1    Okamoto, K.2    Nakayama, H.3    Isobe, T.4    Kato, K.5
  • 8
    • 0035895908 scopus 로고    scopus 로고
    • Phosphorylation-induced change of the oligomerization state of αB-crystallin
    • Ito H, Kamei K, Iwamoto I, Inaguma Y, Nohara D and Kato K: Phosphorylation-induced change of the oligomerization state of αB-crystallin. J Biol Chem 276, 5346-5352 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 5346-5352
    • Ito, H.1    Kamei, K.2    Iwamoto, I.3    Inaguma, Y.4    Nohara, D.5    Kato, K.6
  • 9
    • 0026575146 scopus 로고
    • Translocation of αB crystallin by heat-shock in rat glioma (GA-1) cells
    • Inaguma Y, Shinohara H, Goto S and Kato K: Translocation of αB crystallin by heat-shock in rat glioma (GA-1) cells. Biochem Biophys Res Commun 182, 844-850 (1992)
    • (1992) Biochem Biophys Res Commun , vol.182 , pp. 844-850
    • Inaguma, Y.1    Shinohara, H.2    Goto, S.3    Kato, K.4
  • 10
    • 0028365670 scopus 로고
    • Purification and characterization of a 20-kDa protein that is highly homologous to αB crystallin
    • Kato K, Goto S, Inaguma Y, Hasegawa K, Morishita R and Asano T: Purification and characterization of a 20-kDa protein that is highly homologous to αB crystallin. J Biol Chem 269, 15302-15309 (1994)
    • (1994) J Biol Chem , vol.269 , pp. 15302-15309
    • Kato, K.1    Goto, S.2    Inaguma, Y.3    Hasegawa, K.4    Morishita, R.5    Asano, T.6
  • 12
    • 0036239489 scopus 로고    scopus 로고
    • Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of HSP27 and aB-crystallin to aggresomes
    • Ito H, Kamei K, Iwamoto I, Inaguma Y, García-Mata R, Sztul E and Kato K: Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of HSP27 and aB-crystallin to aggresomes. J Biochem (Tokyo) 131, 593-603 (2002)
    • (2002) J Biochem (Tokyo) , vol.131 , pp. 593-603
    • Ito, H.1    Kamei, K.2    Iwamoto, I.3    Inaguma, Y.4    García-Mata, R.5    Sztul, E.6    Kato, K.7
  • 13
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston JA, Ward CL and Kopito RR: Aggresomes: a cellular response to misfolded proteins. J Cell Biol 143, 1883-1898 (1998)
    • (1998) J Cell Biol , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 14
    • 0033749379 scopus 로고    scopus 로고
    • Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis
    • Johnston JA, Dalton MJ, Gurney ME and Kopito RR: Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 97, 12571-12576 (2000)
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12571-12576
    • Johnston, J.A.1    Dalton, M.J.2    Gurney, M.E.3    Kopito, R.R.4
  • 15
    • 0036566675 scopus 로고    scopus 로고
    • Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntington
    • Wyttenbach A, Sauvageot O, Carmichael J, Diaz-Latoud C, Arrigo AP and Rubinsztein DC: Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntington. Hum Mol Genet 11, 1137-1151 (2002)
    • (2002) Hum Mol Genet , vol.11 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3    Diaz-Latoud, C.4    Arrigo, A.P.5    Rubinsztein, D.C.6
  • 16
    • 0033499931 scopus 로고    scopus 로고
    • Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease
    • Chai Y, Koppenhafer SL, Bonini NM and Paulson HL: Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease. J Neurosci 19, 10338-10347 (1999)
    • (1999) J Neurosci , vol.19 , pp. 10338-10347
    • Chai, Y.1    Koppenhafer, S.L.2    Bonini, N.M.3    Paulson, H.L.4
  • 17
    • 0034708793 scopus 로고    scopus 로고
    • Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract
    • Kobayashi Y, Kume A, Li M, Doyu M, Hata M, Ohtsuka K and Sobue G: Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract. J Biol Chem 275, 8772-8778 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 8772-8778
    • Kobayashi, Y.1    Kume, A.2    Li, M.3    Doyu, M.4    Hata, M.5    Ohtsuka, K.6    Sobue, G.7
  • 18
    • 0024521440 scopus 로고
    • αB crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain
    • Iwaki T, Kume-Iwaki A, Liem RKH and Goldman JE: αB crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell 57, 71-78 (1989)
    • (1989) Cell , vol.57 , pp. 71-78
    • Iwaki, T.1    Kume-Iwaki, A.2    Liem, R.K.H.3    Goldman, J.E.4
  • 19
    • 0026076159 scopus 로고
    • Rosenthal fibers contain ubiquitinated aB-crystallin
    • Goldman JE and Corbin E: Rosenthal fibers contain ubiquitinated aB-crystallin. Am J Pathol 139, 933-938 (1991)
    • (1991) Am J Pathol , vol.139 , pp. 933-938
    • Goldman, J.E.1    Corbin, E.2
  • 20
    • 0035146830 scopus 로고    scopus 로고
    • Ser-59 is the major phosphorylation site in αB-crystallin accumulated in the brains of patients with Alexander's disease
    • Kato K, Inaguma Y, Ito H, Iida K, Iwamoto I, Kamei K, Ochi N, Ohta H and Kishikawa M: Ser-59 is the major phosphorylation site in αB-crystallin accumulated in the brains of patients with Alexander's disease. J Neurochem 76, 730-736 (2001)
    • (2001) J Neurochem , vol.76 , pp. 730-736
    • Kato, K.1    Inaguma, Y.2    Ito, H.3    Iida, K.4    Iwamoto, I.5    Kamei, K.6    Ochi, N.7    Ohta, H.8    Kishikawa, M.9
  • 22
    • 0032956263 scopus 로고    scopus 로고
    • Formation of GFAP cytoplasmic inclusions in astrocytes and their disaggregation by aB-crystallin
    • Koyama Y and Goldman JE: Formation of GFAP cytoplasmic inclusions in astrocytes and their disaggregation by aB-crystallin. Am J Pathol 154, 1563-1572 (1999)
    • (1999) Am J Pathol , vol.154 , pp. 1563-1572
    • Koyama, Y.1    Goldman, J.E.2
  • 24
    • 0031934121 scopus 로고    scopus 로고
    • Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA
    • Litt M, Kramer P, LaMorticella DM, Murphey W, Lovrien EW and Weleber RG: Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. Hum Mol Genet 7, 471-474 (1998)
    • (1998) Hum Mol Genet , vol.7 , pp. 471-474
    • Litt, M.1    Kramer, P.2    LaMorticella, D.M.3    Murphey, W.4    Lovrien, E.W.5    Weleber, R.G.6
  • 25
    • 0033588379 scopus 로고    scopus 로고
    • Structural and functional consequences of the mutation of a conserved arginine residue in αA and αB crystallins
    • Kumar LV, Ramakrishna T and Rao CM: Structural and functional consequences of the mutation of a conserved arginine residue in αA and αB crystallins. J Biol Chem 274, 24137-24141 (1999)
    • (1999) J Biol Chem , vol.274 , pp. 24137-24141
    • Kumar, L.V.1    Ramakrishna, T.2    Rao, C.M.3
  • 26
    • 0032586878 scopus 로고    scopus 로고
    • Mutation R120G in αB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function
    • Bova MP, Yaron O, Huang Q, Ding L, Haley DA, Stewart PL and Horwitz J: Mutation R120G in αB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. Proc Natl Acad Sci USA 96, 6137-6142 (1999)
    • (1999) Proc Natl Acad Sci USA , 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.6    Horwitz, J.7
  • 27
    • 0000843475 scopus 로고    scopus 로고
    • The cardiomyopathy and lens cataract mutation in αB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro
    • Perng MD, Muchowski PJ, van Den IP, Wu GJ, Hutcheson AM, Clark JI and Quinlan RA: The cardiomyopathy and lens cataract mutation in αB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro. J Biol Chem 274, 33235-33243 (1999)
    • (1999) J Biol Chem , vol.274 , pp. 33235-33243
    • Perng, M.D.1    Muchowski, P.J.2    Van Den, I.P.3    Wu, G.J.4    Hutcheson, A.M.5    Clark, J.I.6    Quinlan, R.A.7
  • 28
    • 0035816115 scopus 로고    scopus 로고
    • Expression of R120G-αB-crystallin causes aberrant desmin and αB-crystallin aggregation and cardiomyopathy in mice
    • Wang X, Osinska H, Klevitsky R, Gerdes AM, Nieman M, Lorenz J, Hewett T and Robbins J: Expression of R120G-αB-crystallin causes aberrant desmin and αB-crystallin aggregation and cardiomyopathy in mice. Circ Res 89, 84-91 (2001)
    • (2001) Circ Res , vol.89 , pp. 84-91
    • Wang, X.1    Osinska, H.2    Klevitsky, R.3    Gerdes, A.M.4    Nieman, M.5    Lorenz, J.6    Hewett, T.7    Robbins, J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.