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Volumn 6, Issue 5, 2011, Pages

Multiple aggregates and aggresomes of C-terminal truncated human αA-crystallins in mammalian cells and protection by αB-crystallin

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; GAMMA TUBULIN; CRYSTALLIN;

EID: 79955936253     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019876     Document Type: Article
Times cited : (20)

References (34)
  • 1
    • 0015910905 scopus 로고
    • The amino- acid sequence of the alphaA2 chain of bovine alpha-crystallin
    • Van Der Ouderra FJ, De Jong WW, Bloemendal H, (1973) The amino- acid sequence of the alphaA2 chain of bovine alpha-crystallin. Eur J Biochem 39: 207-222.
    • (1973) Eur J Biochem , vol.39 , pp. 207-222
    • van der Ouderra, F.J.1    de Jong, W.W.2    Bloemendal, H.3
  • 3
    • 0016778248 scopus 로고
    • The amino-acid sequence of the A chain of human alpha-crystallin
    • De Jong WW, Terwindt EC, Bloemendal H, (1975) The amino-acid sequence of the A chain of human alpha-crystallin. FEBS Lett 58: 310-313.
    • (1975) FEBS Lett , vol.58 , pp. 310-313
    • de Jong, W.W.1    Terwindt, E.C.2    Bloemendal, H.3
  • 4
    • 0020063988 scopus 로고
    • Four small Drosophila heat shock proteins are related to each other and to mammalian α-crystallin
    • Ingolia TD, Craig EA, (1982) Four small Drosophila heat shock proteins are related to each other and to mammalian α-crystallin. Proc Natl Acad Sci USA 79: 2360-2364.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 2360-2364
    • Ingolia, T.D.1    Craig, E.A.2
  • 5
    • 0026483279 scopus 로고
    • α-Crystallin can function as a molecular chaperone
    • Horwitz J, (1992) α-Crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 89: 10449-10453.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 6
    • 0028282965 scopus 로고
    • The chaperone activity of bovine alpha-crystallin. Interaction with other lens crystallins in native and denatured states
    • Wang K, Spector A, (1994) The chaperone activity of bovine alpha-crystallin. Interaction with other lens crystallins in native and denatured states. J Biol Chem 269: 13601-13608.
    • (1994) J Biol Chem , vol.269 , pp. 13601-13608
    • Wang, K.1    Spector, A.2
  • 7
    • 0028973109 scopus 로고
    • Evidence that alpha-crystallin prevents non-specific protein aggregation in the intact eye lens
    • Rao PV, Huang QL, Horwitz J, Zigler JS, (1995) Evidence that alpha-crystallin prevents non-specific protein aggregation in the intact eye lens. Biochim Biophys Acta 1245: 439-444.
    • (1995) Biochim Biophys Acta , vol.1245 , pp. 439-444
    • Rao, P.V.1    Huang, Q.L.2    Horwitz, J.3    Zigler, J.S.4
  • 8
    • 0141988870 scopus 로고    scopus 로고
    • Influence of the C-terminal residues on oligomerization of αA-crystallin
    • Thampi P, Abraham EC, (2003) Influence of the C-terminal residues on oligomerization of αA-crystallin. Biochemistry 42: 11857-11863.
    • (2003) Biochemistry , vol.42 , pp. 11857-11863
    • Thampi, P.1    Abraham, E.C.2
  • 9
    • 33846050348 scopus 로고    scopus 로고
    • Role of arginine-163 and the 163-REEK-166 motif in the oligomerization of truncated αA-crystallins
    • Rajan S, Chandrashekar R, Aziz A, Abraham EC, (2006) Role of arginine-163 and the 163-REEK-166 motif in the oligomerization of truncated αA-crystallins. Biochemistry 45: 15684-15691.
    • (2006) Biochemistry , vol.45 , pp. 15684-15691
    • Rajan, S.1    Chandrashekar, R.2    Aziz, A.3    Abraham, E.C.4
  • 10
    • 0029144240 scopus 로고
    • Identification of the in vivo truncation sites at the C-terminal region of alpha-A-crystallin from aged bovine and human lens
    • Takemoto LJ, (1995) Identification of the in vivo truncation sites at the C-terminal region of alpha-A-crystallin from aged bovine and human lens. Curr Eye Res 14: 837-841.
    • (1995) Curr Eye Res , vol.14 , pp. 837-841
    • Takemoto, L.J.1
  • 11
    • 0030475908 scopus 로고    scopus 로고
    • Modifications of the water-insoluble human lens alpha-crystallins
    • Lund AL, Smith JB, Smith DL, (1996) Modifications of the water-insoluble human lens alpha-crystallins. Exp Eye Res 63: 661-672.
    • (1996) Exp Eye Res , vol.63 , pp. 661-672
    • Lund, A.L.1    Smith, J.B.2    Smith, D.L.3
  • 12
    • 0037082138 scopus 로고    scopus 로고
    • Posttranslational modification of human αA-crystallin: correlation with electrophoretic migration
    • Colvis C, Garland D, (2002) Posttranslational modification of human αA-crystallin: correlation with electrophoretic migration. Arch Biochem Biophys 397: 319-323.
    • (2002) Arch Biochem Biophys , vol.397 , pp. 319-323
    • Colvis, C.1    Garland, D.2
  • 13
    • 0032128077 scopus 로고    scopus 로고
    • Age-related changes in human lens crystallins identified by HPLC and mass spectrometry
    • Ma Z, Hanson SR, Lampi KJ, David LL, Smith DL, et al. (1998) Age-related changes in human lens crystallins identified by HPLC and mass spectrometry. Exp Eye Res 67: 21-30.
    • (1998) Exp Eye Res , vol.67 , pp. 21-30
    • Ma, Z.1    Hanson, S.R.2    Lampi, K.J.3    David, L.L.4    Smith, D.L.5
  • 14
    • 0028216737 scopus 로고
    • Posttranslational modifications of water-soluble human lens crystallins from young adults
    • Miesbauer LR, Zhou X, Yang Z, Sun Y, Smith DL, et al. (1994) Posttranslational modifications of water-soluble human lens crystallins from young adults. J Biol Chem 269: 12494-12502.
    • (1994) J Biol Chem , vol.269 , pp. 12494-12502
    • Miesbauer, L.R.1    Zhou, X.2    Yang, Z.3    Sun, Y.4    Smith, D.L.5
  • 15
    • 0031889967 scopus 로고    scopus 로고
    • Quantitation of specific cleavage sites at the C-terminal region of alpha-A-crystallin from human lenses of different age
    • Takemoto LJ, (1998) Quantitation of specific cleavage sites at the C-terminal region of alpha-A-crystallin from human lenses of different age. Exp Eye Res 66: 263-266.
    • (1998) Exp Eye Res , vol.66 , pp. 263-266
    • Takemoto, L.J.1
  • 16
    • 0036784934 scopus 로고    scopus 로고
    • Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in diabetic lenses
    • Thampi P, Hassan A, Smith JB, Abraham EC, (2002) Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in diabetic lenses. Invest Ophthalmol Vis Sci 43: 3265-3272.
    • (2002) Invest Ophthalmol Vis Sci , vol.43 , pp. 3265-3272
    • Thampi, P.1    Hassan, A.2    Smith, J.B.3    Abraham, E.C.4
  • 17
    • 33847685168 scopus 로고    scopus 로고
    • Cleavage of the C-terminal serine of human αA-crystallin produces αA1-172 with increased chaperone activity and oligomeric size
    • Aziz A, Santhoshkumar P, Sharma KK, Abraham EC, (2007) Cleavage of the C-terminal serine of human αA-crystallin produces αA1-172 with increased chaperone activity and oligomeric size. Biochemistry 46: 2510-2519.
    • (2007) Biochemistry , vol.46 , pp. 2510-2519
    • Aziz, A.1    Santhoshkumar, P.2    Sharma, K.K.3    Abraham, E.C.4
  • 18
    • 38649094555 scopus 로고    scopus 로고
    • C-Terminal truncation affects subunit exchange of human αA-crystallin with αB-crystallin
    • Kallur LS, Aziz A, Abraham EC, (2008) C-Terminal truncation affects subunit exchange of human αA-crystallin with αB-crystallin. Mol Cell Biochem 308: 85-91.
    • (2008) Mol Cell Biochem , vol.308 , pp. 85-91
    • Kallur, L.S.1    Aziz, A.2    Abraham, E.C.3
  • 19
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito RR, (2000) Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 10: 524-530.
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 20
    • 0036303981 scopus 로고    scopus 로고
    • Hassles with taking out the garbage: aggravating aggresomes
    • Garcia-Mata R, Gao YS, Sztul E, (2002) Hassles with taking out the garbage: aggravating aggresomes. Traffic 3: 388-396.
    • (2002) Traffic , vol.3 , pp. 388-396
    • Garcia-Mata, R.1    Gao, Y.S.2    Sztul, E.3
  • 21
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: a cellular response to misfolded proteins
    • Johnston JA, Ward CL, Kopito RR, (1998) Aggresomes: a cellular response to misfolded proteins. J Cell Biol 143: 1883-1898.
    • (1998) J Cell Biol , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 22
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S, (2004) Inclusion body formation reduces levels of mutant huntingin and the risk of neuronal death. Nature 431: 805-810.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 23
    • 79958290302 scopus 로고    scopus 로고
    • Novel Cell- and Tissue-based Assays for Detecting Misfolded and Aggregated Protein Accumulation within Aggresomes and Inclusion Bodies
    • (In Press)
    • Shen D, Coleman J, Chan E, Nicholson TP, Dai L, et al. (2010) Novel Cell- and Tissue-based Assays for Detecting Misfolded and Aggregated Protein Accumulation within Aggresomes and Inclusion Bodies. Cell Biochem Biophys (In Press).
    • (2010) Cell Biochem Biophys
    • Shen, D.1    Coleman, J.2    Chan, E.3    Nicholson, T.P.4    Dai, L.5
  • 24
    • 0037033074 scopus 로고    scopus 로고
    • Parkin Accumulation in Aggresomes Due to Proteasome Impairment
    • Junn E, Lee SS, Suhr UT, Mouradian MM, (2002) Parkin Accumulation in Aggresomes Due to Proteasome Impairment. J Biol Chem 277: 47870-47877.
    • (2002) J Biol Chem , vol.277 , pp. 47870-47877
    • Junn, E.1    Lee, S.S.2    Suhr, U.T.3    Mouradian, M.M.4
  • 26
    • 77949764687 scopus 로고    scopus 로고
    • Loss of HRD-1 Mediated Protein Degradation Causes Amyloid Precursor Protein Accumulation and Amyloid-β Generation
    • Kaneko M, Koike H, Saito R, Kitamura Y, Okuma Y, et al. (2010) Loss of HRD-1 Mediated Protein Degradation Causes Amyloid Precursor Protein Accumulation and Amyloid-β Generation. J Neurosci 30: 3924-3932.
    • (2010) J Neurosci , vol.30 , pp. 3924-3932
    • Kaneko, M.1    Koike, H.2    Saito, R.3    Kitamura, Y.4    Okuma, Y.5
  • 27
    • 0347917234 scopus 로고    scopus 로고
    • Parkin is recruited into aggresomes in a stress-specific manner: over-expression of parkin reduces aggresome formation but can be dissociated from parkin's neuronal survival
    • Mukit MKM, Davidson SM, Smith PMD, MacCormac LP, Kahns S, et al. (2004) Parkin is recruited into aggresomes in a stress-specific manner: over-expression of parkin reduces aggresome formation but can be dissociated from parkin's neuronal survival. Hum Mol Genet 13: 117-135.
    • (2004) Hum Mol Genet , vol.13 , pp. 117-135
    • Mukit, M.K.M.1    Davidson, S.M.2    Smith, P.M.D.3    MacCormac, L.P.4    Kahns, S.5
  • 29
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin
    • Iwata A, Riley BE, Johnston JA, Kopito RR, (2005) HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J Biol Chem 280: 40282-40292.
    • (2005) J Biol Chem , vol.280 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 30
    • 0035910069 scopus 로고    scopus 로고
    • Wild-type PrP and mutant associated with prion disease are subject to retrograde transport and proteasome degradation
    • Ma A, Lindquist S, (2001) Wild-type PrP and mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc Natl Acad Sci U S A 98: 14955-14960.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 14955-14960
    • Ma, A.1    Lindquist, S.2
  • 31
    • 58149465766 scopus 로고    scopus 로고
    • A critical role for CHIP in the aggresome pathway
    • Sha Y, Pandit L, Zeng S, Eissa NT, (2009) A critical role for CHIP in the aggresome pathway. Mol Cell Biol 29: 116-128.
    • (2009) Mol Cell Biol , vol.29 , pp. 116-128
    • Sha, Y.1    Pandit, L.2    Zeng, S.3    Eissa, N.T.4
  • 32
    • 0038104369 scopus 로고    scopus 로고
    • Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G alphaB-crystallin mutant
    • Chavez Zobel AT, Loranger A, Marceau N, Theriault JR, Lambert H, et al. (2003) Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G alphaB-crystallin mutant. Hum Mol Genet 12: 1609-1620.
    • (2003) Hum Mol Genet , vol.12 , pp. 1609-1620
    • Chavez Zobel, A.T.1    Loranger, A.2    Marceau, N.3    Theriault, J.R.4    Lambert, H.5
  • 33
    • 55549105778 scopus 로고    scopus 로고
    • Triggering aggresome formation. Dissecting aggresome-targeting and aggregation signals in synphilin 1
    • Zaarur N, Merrin AB, Gabai VL, Sherman MY, (2008) Triggering aggresome formation. Dissecting aggresome-targeting and aggregation signals in synphilin 1. J Biol Chem 283: 25575-25584.
    • (2008) J Biol Chem , vol.283 , pp. 25575-25584
    • Zaarur, N.1    Merrin, A.B.2    Gabai, V.L.3    Sherman, M.Y.4
  • 34
    • 0037388418 scopus 로고    scopus 로고
    • Aggresomes protects cells by enhancing the degradation of toxic-polyglutamine containing protein
    • Taylor JP, Tanaka F, Robitschek J, Sandoval JM, Taye A, et al. (2003) Aggresomes protects cells by enhancing the degradation of toxic-polyglutamine containing protein. Hum Mol Genet 12: 749-757.
    • (2003) Hum Mol Genet , vol.12 , pp. 749-757
    • Taylor, J.P.1    Tanaka, F.2    Robitschek, J.3    Sandoval, J.M.4    Taye, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.