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Volumn 7, Issue 9, 2012, Pages

αA-Crystallin-Derived Mini-Chaperone Modulates Stability and Function of Cataract Causing αAG98R-Crystallin

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; ALPHA CRYSTALLIN DERIVED MINI CHAPERONE; CHAPERONE; MUTANT PROTEIN; N BENZOYLPHENYLALANINE DERIVATIVE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 84866056432     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0044077     Document Type: Article
Times cited : (21)

References (46)
  • 1
    • 0017389118 scopus 로고
    • The vertebrate eye lens
    • Bloemendal H, (1977) The vertebrate eye lens. Science 197: 127-138.
    • (1977) Science , vol.197 , pp. 127-138
    • Bloemendal, H.1
  • 2
    • 0020063988 scopus 로고
    • Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin
    • Ingolia TD, Craig EA, (1982) Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-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
  • 3
    • 0027524175 scopus 로고
    • Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. A family of chaperones
    • Merck KB, Groenen PJ, Voorter CE, de Haard-Hoekman WA, Horwitz J, et al. (1993) Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. A family of chaperones. J Biol Chem 268: 1046-1052.
    • (1993) J Biol Chem , vol.268 , pp. 1046-1052
    • Merck, K.B.1    Groenen, P.J.2    Voorter, C.E.3    de Haard-Hoekman, W.A.4    Horwitz, J.5
  • 5
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz J, (1992) Alpha-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
    • 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 Jr, (1995) Evidence that alpha-crystallin prevents non-specific protein aggregation in the intact eye lens. Biochim Biophys Acta 1245: 439-447.
    • (1995) Biochim Biophys Acta , vol.1245 , pp. 439-447
    • Rao, P.V.1    Huang, Q.L.2    Horwitz, J.3    Zigler Jr., J.S.4
  • 7
    • 0034486034 scopus 로고    scopus 로고
    • The function of alpha-crystallin in vision
    • Horwitz J, (2000) The function of alpha-crystallin in vision. Semin Cell Dev Biol 11: 53-60.
    • (2000) Semin Cell Dev Biol , vol.11 , pp. 53-60
    • Horwitz, J.1
  • 8
    • 0035947181 scopus 로고    scopus 로고
    • Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation
    • Rajaraman K, Raman B, Ramakrishna T, Rao CM, (2001) Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation. FEBS Lett 497: 118-123.
    • (2001) FEBS Lett , vol.497 , pp. 118-123
    • Rajaraman, K.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 9
    • 0034741246 scopus 로고    scopus 로고
    • alphaA- and alphaB-crystallins protect glucose-6-phosphate dehydrogenase against UVB irradiation-induced inactivation
    • Reddy GB, Reddy PY, Suryanarayana P, (2001) alphaA- and alphaB-crystallins protect glucose-6-phosphate dehydrogenase against UVB irradiation-induced inactivation. Biochem Biophysl Res Comm 282: 712-716.
    • (2001) Biochem Biophysl Res Comm , vol.282 , pp. 712-716
    • Reddy, G.B.1    Reddy, P.Y.2    Suryanarayana, P.3
  • 10
    • 0023260557 scopus 로고
    • Confirmation of assignment of the human alpha 1-crystallin gene (CRYA1) to chromosome 21 with regional localization to q22.3
    • Hawkins JW, Van Keuren ML, Piatigorsky J, Law ML, Patterson D, et al. (1987) Confirmation of assignment of the human alpha 1-crystallin gene (CRYA1) to chromosome 21 with regional localization to q22.3. Human Genetics 76: 375-380.
    • (1987) Human Genetics , vol.76 , pp. 375-380
    • Hawkins, J.W.1    van Keuren, M.L.2    Piatigorsky, J.3    Law, M.L.4    Patterson, D.5
  • 11
    • 0021137749 scopus 로고
    • Genetical and biochemical studies of a dominant cataract mutant in mice
    • Graw J, Kratochvilova J, Summer KH, (1984) Genetical and biochemical studies of a dominant cataract mutant in mice. Exp Eye Res 39: 37-45.
    • (1984) Exp Eye Res , vol.39 , pp. 37-45
    • Graw, J.1    Kratochvilova, J.2    Summer, K.H.3
  • 12
    • 61849122908 scopus 로고    scopus 로고
    • Genetics of crystallins: cataract and beyond
    • Graw J, (2009) Genetics of crystallins: cataract and beyond. Exp Eye Res 88: 173-189.
    • (2009) Exp Eye Res , vol.88 , pp. 173-189
    • Graw, J.1
  • 14
    • 35148832522 scopus 로고    scopus 로고
    • Genetic heterogeneity in microcornea-cataract: five novel mutations in CRYAA, CRYGD, and GJA8
    • Hansen L, Yao W, Eiberg H, Kjaer KW, Baggesen K, et al. (2007) Genetic heterogeneity in microcornea-cataract: five novel mutations in CRYAA, CRYGD, and GJA8. Invest Ophthalmol Vis Sci 48: 3937-3944.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 3937-3944
    • Hansen, L.1    Yao, W.2    Eiberg, H.3    Kjaer, K.W.4    Baggesen, K.5
  • 15
    • 33746912684 scopus 로고    scopus 로고
    • Congenital cataract and macular hypoplasia in humans associated with a de novo mutation in CRYAA and compound heterozygous mutations in P
    • Graw J, Klopp N, Illig T, Preising MN, Lorenz B, (2006) Congenital cataract and macular hypoplasia in humans associated with a de novo mutation in CRYAA and compound heterozygous mutations in P. Graefe's Arch Clin Exp Ophthalmol 244: 912-919.
    • (2006) Graefe's Arch Clin Exp Ophthalmol , vol.244 , pp. 912-919
    • Graw, J.1    Klopp, N.2    Illig, T.3    Preising, M.N.4    Lorenz, B.5
  • 16
    • 0242287938 scopus 로고    scopus 로고
    • Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q
    • Mackay DS, Andley UP, Shiels A, (2003) Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q. Eur J Hum Genet 11: 784-793.
    • (2003) Eur J Hum Genet , vol.11 , pp. 784-793
    • Mackay, D.S.1    Andley, U.P.2    Shiels, A.3
  • 17
    • 33746708291 scopus 로고    scopus 로고
    • Arginine 54 and Tyrosine 118 residues of alphaA-crystallin are crucial for lens formation and transparency
    • Xia CH, Liu H, Chang B, Cheng C, Cheung D, et al. (2006) Arginine 54 and Tyrosine 118 residues of alphaA-crystallin are crucial for lens formation and transparency. Invest Ophthalmol Vis Sci 47: 3004-3010.
    • (2006) Invest Ophthalmol Vis Sci , vol.47 , pp. 3004-3010
    • Xia, C.H.1    Liu, H.2    Chang, B.3    Cheng, C.4    Cheung, D.5
  • 18
    • 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, et al. (1998) Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. Hum Mol Genet 7: 471-474.
    • (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
  • 19
    • 33745913948 scopus 로고    scopus 로고
    • Identification of a novel, putative cataract-causing allele in CRYAA (G98R) in an Indian family
    • Santhiya ST, Soker T, Klopp N, Illig T, Prakash MV, et al. (2006) Identification of a novel, putative cataract-causing allele in CRYAA (G98R) in an Indian family. Molecular Vision 12: 768-773.
    • (2006) Molecular Vision , vol.12 , pp. 768-773
    • Santhiya, S.T.1    Soker, T.2    Klopp, N.3    Illig, T.4    Prakash, M.V.5
  • 20
    • 33751518175 scopus 로고    scopus 로고
    • The cataract-causing mutation G98R in human alphaA-crystallin leads to folding defects and loss of chaperone activity
    • Singh D, Raman B, Ramakrishna T, Rao Ch M, (2006) The cataract-causing mutation G98R in human alphaA-crystallin leads to folding defects and loss of chaperone activity. Molecular Vision 12: 1372-1379.
    • (2006) Molecular Vision , vol.12 , pp. 1372-1379
    • Singh, D.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 21
    • 37349125494 scopus 로고    scopus 로고
    • Cataract-causing alphaAG98R mutant shows substrate-dependent chaperone activity
    • Murugesan R, Santhoshkumar P, Sharma KK, (2007) Cataract-causing alphaAG98R mutant shows substrate-dependent chaperone activity. Molecular Vision 13: 2301-2309.
    • (2007) Molecular Vision , vol.13 , pp. 2301-2309
    • Murugesan, R.1    Santhoshkumar, P.2    Sharma, K.K.3
  • 22
    • 79551717234 scopus 로고    scopus 로고
    • Cataract-causing alphaAG98R-crystallin mutant dissociates into monomers having chaperone activity
    • Raju M, Santhoshkumar P, Sharma KK, (2011) Cataract-causing alphaAG98R-crystallin mutant dissociates into monomers having chaperone activity. Molecular Vision 17: 7-15.
    • (2011) Molecular Vision , vol.17 , pp. 7-15
    • Raju, M.1    Santhoshkumar, P.2    Sharma, K.K.3
  • 23
    • 0036702298 scopus 로고    scopus 로고
    • ER-associated degradation in protein quality control and cellular regulation
    • Hampton RY, (2002) ER-associated degradation in protein quality control and cellular regulation. Curr Opin Cell Biol 14: 476-482.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 476-482
    • Hampton, R.Y.1
  • 24
    • 3042540232 scopus 로고    scopus 로고
    • Pharmacological chaperones: potential treatment for conformational diseases
    • Bernier V, Lagace M, Bichet DG, Bouvier M, (2004) Pharmacological chaperones: potential treatment for conformational diseases. Trends Endocri Metbol 15: 222-228.
    • (2004) Trends Endocri Metbol , vol.15 , pp. 222-228
    • Bernier, V.1    Lagace, M.2    Bichet, D.G.3    Bouvier, M.4
  • 25
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • Cohen FE, Kelly JW, (2003) Therapeutic approaches to protein-misfolding diseases. Nature 426: 905-909.
    • (2003) Nature , vol.426 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 26
    • 0034635397 scopus 로고    scopus 로고
    • Synthesis and characterization of a peptide identified as a functional element in alphaA-crystallin
    • Sharma KK, Kumar RS, Kumar GS, Quinn PT, (2000) Synthesis and characterization of a peptide identified as a functional element in alphaA-crystallin. J Biol Chem 275: 3767-3771.
    • (2000) J Biol Chem , vol.275 , pp. 3767-3771
    • Sharma, K.K.1    Kumar, R.S.2    Kumar, G.S.3    Quinn, P.T.4
  • 27
    • 0021763606 scopus 로고
    • Primary structures of the alpha-crystallin A chains of twenty-eight mammalian species, chicken and frog
    • de Jong WW, Zweers A, Versteeg M, Nuy-Terwindt EC, (1984) Primary structures of the alpha-crystallin A chains of twenty-eight mammalian species, chicken and frog. Eur J Biochem 141: 131-140.
    • (1984) Eur J Biochem , vol.141 , pp. 131-140
    • de Jong, W.W.1    Zweers, A.2    Versteeg, M.3    Nuy-Terwindt, E.C.4
  • 28
    • 0033831993 scopus 로고    scopus 로고
    • Chaperone-like activity of a synthetic peptide toward oxidized gamma-crystallin
    • Kumar RS, Sharma KK, (2000) Chaperone-like activity of a synthetic peptide toward oxidized gamma-crystallin. J Peptide Res 56: 157-164.
    • (2000) J Peptide Res , vol.56 , pp. 157-164
    • Kumar, R.S.1    Sharma, K.K.2
  • 29
    • 0034891055 scopus 로고    scopus 로고
    • Conformational specificity of mini-alphaA-crystallin as a molecular chaperone
    • Bhattacharyya J, Sharma KK, (2001) Conformational specificity of mini-alphaA-crystallin as a molecular chaperone. J Peptide Res 57: 428-434.
    • (2001) J Peptide Res , vol.57 , pp. 428-434
    • Bhattacharyya, J.1    Sharma, K.K.2
  • 30
    • 52549105587 scopus 로고    scopus 로고
    • Interaction of alpha-lactalbumin with mini-alphaA-crystallin
    • Sreelakshmi Y, Sharma KK, (2001) Interaction of alpha-lactalbumin with mini-alphaA-crystallin. J Prot Chem 20: 123-130.
    • (2001) J Prot Chem , vol.20 , pp. 123-130
    • Sreelakshmi, Y.1    Sharma, K.K.2
  • 31
    • 9444229933 scopus 로고    scopus 로고
    • Inhibition of amyloid fibrillogenesis and toxicity by a peptide chaperone
    • Santhoshkumar P, Sharma KK, (2004) Inhibition of amyloid fibrillogenesis and toxicity by a peptide chaperone. Mol Cell Biochem 267: 147-155.
    • (2004) Mol Cell Biochem , vol.267 , pp. 147-155
    • Santhoshkumar, P.1    Sharma, K.K.2
  • 32
    • 70450255057 scopus 로고    scopus 로고
    • Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin
    • Moreau KL, King J, (2009) Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin. J Biol Chem 284: 33285-33295.
    • (2009) J Biol Chem , vol.284 , pp. 33285-33295
    • Moreau, K.L.1    King, J.2
  • 33
    • 0032078066 scopus 로고    scopus 로고
    • Mutation of alpha B-crystallin: effects on chaperone-like activity
    • Horwitz J, Bova M, Huang QL, Ding L, Yaron O, et al. (1998) Mutation of alpha B-crystallin: effects on chaperone-like activity. Int J Biol Macromol 22: 263-269.
    • (1998) Int J Biol Macromol , vol.22 , pp. 263-269
    • Horwitz, J.1    Bova, M.2    Huang, Q.L.3    Ding, L.4    Yaron, O.5
  • 34
    • 33645401324 scopus 로고    scopus 로고
    • A novel alphaB-crystallin mutation associated with autosomal dominant congenital lamellar cataract
    • Liu Y, Zhang X, Luo L, Wu M, Zeng R, et al. (2006) A novel alphaB-crystallin mutation associated with autosomal dominant congenital lamellar cataract. Invest Ophthalmol Vis Sci 47: 1069-1075.
    • (2006) Invest Ophthalmol Vis Sci , vol.47 , pp. 1069-1075
    • Liu, Y.1    Zhang, X.2    Luo, L.3    Wu, M.4    Zeng, R.5
  • 35
    • 33744903422 scopus 로고    scopus 로고
    • Mechanism of a hereditary cataract phenotype. Mutations in alphaA-crystallin activate substrate binding
    • Koteiche HA, McHaourab HS, (2006) Mechanism of a hereditary cataract phenotype. Mutations in alphaA-crystallin activate substrate binding. J Biol Chem 281: 14273-14279.
    • (2006) J Biol Chem , vol.281 , pp. 14273-14279
    • Koteiche, H.A.1    McHaourab, H.S.2
  • 36
    • 0032021185 scopus 로고    scopus 로고
    • Estimation of the binding site of drugs by means of new types of photoactive ligands
    • Dorman G, (1998) Estimation of the binding site of drugs by means of new types of photoactive ligands. Acta Pharm Hung 68: 95-105.
    • (1998) Acta Pharm Hung , vol.68 , pp. 95-105
    • Dorman, G.1
  • 37
    • 0028235205 scopus 로고
    • Benzophenone photophores in biochemistry
    • Dorman G, Prestwich GD, (1994) Benzophenone photophores in biochemistry. Biochemistry 33: 5661-5673.
    • (1994) Biochemistry , vol.33 , pp. 5661-5673
    • Dorman, G.1    Prestwich, G.D.2
  • 38
    • 0029842449 scopus 로고    scopus 로고
    • The use of photolabelled peptides to localize the substance-P-binding site in the human neurokinin-1 tachykinin receptor
    • Girault S, Sagan S, Bolbach G, Lavielle S, Chassaing G, (1996) The use of photolabelled peptides to localize the substance-P-binding site in the human neurokinin-1 tachykinin receptor. Eur J Biochem 240: 215-222.
    • (1996) Eur J Biochem , vol.240 , pp. 215-222
    • Girault, S.1    Sagan, S.2    Bolbach, G.3    Lavielle, S.4    Chassaing, G.5
  • 39
    • 5644275139 scopus 로고    scopus 로고
    • Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function
    • Biswas A, Das KP, (2004) Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function. J Biol Chem 279: 42648-42657.
    • (2004) J Biol Chem , vol.279 , pp. 42648-42657
    • Biswas, A.1    Das, K.P.2
  • 40
    • 0031870836 scopus 로고    scopus 로고
    • The effect of glutathione upon chaperone activity of alpha-crystallin is probably mediated through target modulation
    • Pal J, Bera S, Ghosh SK, (1998) The effect of glutathione upon chaperone activity of alpha-crystallin is probably mediated through target modulation. Ophthal Res 30: 271-279.
    • (1998) Ophthal Res , vol.30 , pp. 271-279
    • Pal, J.1    Bera, S.2    Ghosh, S.K.3
  • 41
    • 0037907479 scopus 로고    scopus 로고
    • Structural perturbation and enhancement of the chaperone-like activity of alpha-crystallin by arginine hydrochloride
    • Srinivas V, Raman B, Rao KS, Ramakrishna T, Rao Ch M, (2003) Structural perturbation and enhancement of the chaperone-like activity of alpha-crystallin by arginine hydrochloride. Protein Sci 12: 1262-1270.
    • (2003) Protein Sci , vol.12 , pp. 1262-1270
    • Srinivas, V.1    Raman, B.2    Rao, K.S.3    Ramakrishna, T.4    Rao, C.M.5
  • 42
    • 25444512697 scopus 로고    scopus 로고
    • Arginine hydrochloride enhances the dynamics of subunit assembly and the chaperone-like activity of alpha-crystallin
    • Srinivas V, Raman B, Rao KS, Ramakrishna T, Rao Ch M, (2005) Arginine hydrochloride enhances the dynamics of subunit assembly and the chaperone-like activity of alpha-crystallin. Molecular Vision 11: 249-255.
    • (2005) Molecular Vision , vol.11 , pp. 249-255
    • Srinivas, V.1    Raman, B.2    Rao, K.S.3    Ramakrishna, T.4    Rao, C.M.5
  • 43
    • 0028811434 scopus 로고
    • Effect of cross-linking on the chaperone-like function of alpha crystallin
    • Sharma KK, Ortwerth BJ, (1995) Effect of cross-linking on the chaperone-like function of alpha crystallin. Exp Eye Res 61: 413-421.
    • (1995) Exp Eye Res , vol.61 , pp. 413-421
    • Sharma, K.K.1    Ortwerth, B.J.2
  • 44
    • 3042834124 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase A is important for lens cell viability and resistance to oxidative stress
    • Kantorow M, Hawse JR, Cowell TL, Benhamed S, Pizarro GO, et al. (2004) Methionine sulfoxide reductase A is important for lens cell viability and resistance to oxidative stress. Proc Natl Acad Sci USA 101: 9654-9659.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9654-9659
    • Kantorow, M.1    Hawse, J.R.2    Cowell, T.L.3    Benhamed, S.4    Pizarro, G.O.5
  • 45
    • 0037154149 scopus 로고    scopus 로고
    • A peptide that binds and stabilizes p53 core domain: chaperone strategy for rescue of oncogenic mutants
    • Friedler A, Hansson LO, Veprintsev DB, Freund SM, Rippin TM, et al. (2002) A peptide that binds and stabilizes p53 core domain: chaperone strategy for rescue of oncogenic mutants. Proc Natl Acad Sci USA 99: 937-942.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 937-942
    • Friedler, A.1    Hansson, L.O.2    Veprintsev, D.B.3    Freund, S.M.4    Rippin, T.M.5
  • 46
    • 0030961889 scopus 로고    scopus 로고
    • Restoration of the growth suppression function of mutant p53 by a synthetic peptide derived from the p53 C-terminal domain
    • Selivanova G, Iotsova V, Okan I, Fritsche M, Strom M, et al. (1997) Restoration of the growth suppression function of mutant p53 by a synthetic peptide derived from the p53 C-terminal domain. Nature Med 3: 632-638.
    • (1997) Nature Med , vol.3 , pp. 632-638
    • Selivanova, G.1    Iotsova, V.2    Okan, I.3    Fritsche, M.4    Strom, M.5


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