메뉴 건너뛰기




Volumn 106, Issue , 2013, Pages 34-39

Accelerated aging of Asp 58 in αA crystallin and human cataract formation

Author keywords

Blindness; Human age related cataract; Posttranslational modification; Protein denaturation; Racemisation

Indexed keywords

ALPHAA CRYSTALLIN; ASPARAGINASE; HEAT SHOCK PROTEIN; UNCLASSIFIED DRUG;

EID: 84870494519     PISSN: 00144835     EISSN: 10960007     Source Type: Journal    
DOI: 10.1016/j.exer.2012.10.013     Document Type: Article
Times cited : (23)

References (41)
  • 1
    • 84858340718 scopus 로고    scopus 로고
    • Pharmacological maintenance of protein homeostasis could postpone age-related disease
    • Alavez S., Lithgow G.J. Pharmacological maintenance of protein homeostasis could postpone age-related disease. Aging Cell 2012, 11:187-191.
    • (2012) Aging Cell , vol.11 , pp. 187-191
    • Alavez, S.1    Lithgow, G.J.2
  • 2
    • 0037163034 scopus 로고    scopus 로고
    • The influence of protein structure on the products emerging from succinimide hydrolysis
    • Athmer L., Kindrachuk J., Georges F., Napper S. The influence of protein structure on the products emerging from succinimide hydrolysis. J. Biol. Chem. 2002, 277:30502-30507.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30502-30507
    • Athmer, L.1    Kindrachuk, J.2    Georges, F.3    Napper, S.4
  • 3
    • 0034141218 scopus 로고    scopus 로고
    • Collagen fragments in urine derived from bone resorption are highly racemized and isomerized: a biological clock of protein aging with clinical potential
    • Cloos P.A., Fledelius C. Collagen fragments in urine derived from bone resorption are highly racemized and isomerized: a biological clock of protein aging with clinical potential. Biochem. J. 2000, 345:473-480.
    • (2000) Biochem. J. , vol.345 , pp. 473-480
    • Cloos, P.A.1    Fledelius, C.2
  • 4
    • 0017658442 scopus 로고
    • Changes in the distribution of proteins in the aging human lens
    • Coghlan S.D., Augusteyn R.C. Changes in the distribution of proteins in the aging human lens. Exp. Eye Res. 1977, 25:603-611.
    • (1977) Exp. Eye Res. , vol.25 , pp. 603-611
    • Coghlan, S.D.1    Augusteyn, R.C.2
  • 5
    • 58249089343 scopus 로고    scopus 로고
    • Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells
    • D'Angelo M.A., Raices M., Panowski S.H., Hetzer M.W. Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. Cell 2009, 136:284-295.
    • (2009) Cell , vol.136 , pp. 284-295
    • D'Angelo, M.A.1    Raices, M.2    Panowski, S.H.3    Hetzer, M.W.4
  • 8
    • 0035909236 scopus 로고    scopus 로고
    • Inversion and isomerization of Asp-58 residue in human [alpha]A-crystallin from normal aged lenses and cataractous lenses
    • Fujii N., Matsumoto S., Hiroki K., Takemoto L. Inversion and isomerization of Asp-58 residue in human [alpha]A-crystallin from normal aged lenses and cataractous lenses. Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. 2001, 1549:179-187.
    • (2001) Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. , vol.1549 , pp. 179-187
    • Fujii, N.1    Matsumoto, S.2    Hiroki, K.3    Takemoto, L.4
  • 9
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation
    • Geiger T., Clarke S. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. J. Biol. Chem. 1987, 262:785-794.
    • (1987) J. Biol. Chem. , vol.262 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 10
    • 0034141745 scopus 로고    scopus 로고
    • Racemization and isomerization of type I collagen C-telopeptides in human bone and soft tissues: assessment of tissue turnover
    • Gineyts E., Cloos P.A., Borel O., Grimaud L., Delmas P.D., Garnero P. Racemization and isomerization of type I collagen C-telopeptides in human bone and soft tissues: assessment of tissue turnover. Biochem. J. 2000, 345:481-485.
    • (2000) Biochem. J. , vol.345 , pp. 481-485
    • Gineyts, E.1    Cloos, P.A.2    Borel, O.3    Grimaud, L.4    Delmas, P.D.5    Garnero, P.6
  • 12
    • 46749117136 scopus 로고    scopus 로고
    • Molecular and cellular aspects of protein misfolding and disease
    • Herczenik E., Gebbink M.F.B.G. Molecular and cellular aspects of protein misfolding and disease. FASEB J. 2008, 22:2115-2133.
    • (2008) FASEB J. , vol.22 , pp. 2115-2133
    • Herczenik, E.1    Gebbink, M.F.B.G.2
  • 13
    • 18044365894 scopus 로고    scopus 로고
    • Massive increase in the stiffness of the human lens nucleus with age: the basis for presbyopia?
    • Heys K.R., Cram S.L., Truscott R.J.W. Massive increase in the stiffness of the human lens nucleus with age: the basis for presbyopia?. Mol. Vis. 2004, 10:956-963.
    • (2004) Mol. Vis. , vol.10 , pp. 956-963
    • Heys, K.R.1    Cram, S.L.2    Truscott, R.J.W.3
  • 14
    • 36249023238 scopus 로고    scopus 로고
    • Presbyopia and heat: changes associated with aging of the human lens suggest a functional role for the small heat shock protein, alpha-crystallin, in maintaining lens flexibility
    • Heys K.R., Friedrich M.G., Truscott R.J.W. Presbyopia and heat: changes associated with aging of the human lens suggest a functional role for the small heat shock protein, alpha-crystallin, in maintaining lens flexibility. Aging Cell 2007, 6:807-815.
    • (2007) Aging Cell , vol.6 , pp. 807-815
    • Heys, K.R.1    Friedrich, M.G.2    Truscott, R.J.W.3
  • 15
    • 79959554464 scopus 로고    scopus 로고
    • Racemisation and human cataract. D-Ser, D-Asp/Asn and D-Thr are higher in the lifelong proteins of cataract lenses than in age-matched normal lenses
    • Hooi M., Truscott R. Racemisation and human cataract. D-Ser, D-Asp/Asn and D-Thr are higher in the lifelong proteins of cataract lenses than in age-matched normal lenses. Age 2011, 33:131-141.
    • (2011) Age , vol.33 , pp. 131-141
    • Hooi, M.1    Truscott, R.2
  • 16
    • 84865661787 scopus 로고    scopus 로고
    • Racemisation of two proteins over our lifespan. Deamidation of asparagine 76 in γS crystallin is greater in cataract than in normal lenses across the age range
    • Hooi M.Y.S., Raftery M.J., Truscott R.J.W. Racemisation of two proteins over our lifespan. Deamidation of asparagine 76 in γS crystallin is greater in cataract than in normal lenses across the age range. Invest. Ophthalmol. Vis. Sci. 2012, 53:3554-3561.
    • (2012) Invest. Ophthalmol. Vis. Sci. , vol.53 , pp. 3554-3561
    • Hooi, M.Y.S.1    Raftery, M.J.2    Truscott, R.J.W.3
  • 17
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. U.S.A. 1992, 89:10449-10453.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 18
    • 36549035313 scopus 로고    scopus 로고
    • Lipofuscin: formation, distribution, and metabolic consequences
    • Jung T., Bader N., Grune T. Lipofuscin: formation, distribution, and metabolic consequences. Ann. N.Y. Acad. Sci. 2007, 1119:97-111.
    • (2007) Ann. N.Y. Acad. Sci. , vol.1119 , pp. 97-111
    • Jung, T.1    Bader, N.2    Grune, T.3
  • 19
    • 0030995490 scopus 로고    scopus 로고
    • Deficiency of a protein-repair enzyme results in the accumulation of altered proteins, retardation of growth, and fatal seizures in mice
    • Kim E., Lowenson J.D., MacLaren D.C., Clarke S., Young S.G. Deficiency of a protein-repair enzyme results in the accumulation of altered proteins, retardation of growth, and fatal seizures in mice. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:6132-6137.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 6132-6137
    • Kim, E.1    Lowenson, J.D.2    MacLaren, D.C.3    Clarke, S.4    Young, S.G.5
  • 21
    • 0023682520 scopus 로고
    • Does the chemical instability of aspartyl and asparaginyl residues in proteins contribute to Erythrocyte aging?
    • Lowenson J., Clarke S. Does the chemical instability of aspartyl and asparaginyl residues in proteins contribute to Erythrocyte aging?. Blood Cells 1988, 14:103-117.
    • (1988) Blood Cells , vol.14 , pp. 103-117
    • Lowenson, J.1    Clarke, S.2
  • 23
    • 0033522885 scopus 로고    scopus 로고
    • Site-directed mutations within the core " α-crystallin" domain of the small heat-shock protein, human αB-crystallin, decrease molecular chaperone functions
    • Muchowski P.J., Wu G.J.S., Liang J.J.N., Adman E.T., Clark J.I. Site-directed mutations within the core " α-crystallin" domain of the small heat-shock protein, human αB-crystallin, decrease molecular chaperone functions. J. Mol. Biol. 1999, 289:397-411.
    • (1999) J. Mol. Biol. , vol.289 , pp. 397-411
    • Muchowski, P.J.1    Wu, G.J.S.2    Liang, J.J.N.3    Adman, E.T.4    Clark, J.I.5
  • 24
    • 33646112406 scopus 로고    scopus 로고
    • Kinetic study of racemization of aspartyl residues in recombinant human αA-crystallin
    • Nakamura T., Sadakane Y., Fujii N. Kinetic study of racemization of aspartyl residues in recombinant human αA-crystallin. Biochim. Biophys. Acta 2006, 1764:800-806.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 800-806
    • Nakamura, T.1    Sadakane, Y.2    Fujii, N.3
  • 26
    • 0027477463 scopus 로고
    • Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease
    • Roher A., Lowenson J., Clarke S., Wolkow C., Wang R., Cotter R., Reardon I., Zurcher-Neely H., Heinrikson R., Ball M. Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease. J. Biol. Chem. 1993, 268:3072-3083.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3072-3083
    • Roher, A.1    Lowenson, J.2    Clarke, S.3    Wolkow, C.4    Wang, R.5    Cotter, R.6    Reardon, I.7    Zurcher-Neely, H.8    Heinrikson, R.9    Ball, M.10
  • 27
    • 0025780051 scopus 로고
    • Marked longevity of human lung parenchymal elastic fibers deduced from prevalence of d-aspartate and nuclear weapons-related radiocarbon
    • Shapiro S., Endicott S., Province M., Pierce J., Campbell E. Marked longevity of human lung parenchymal elastic fibers deduced from prevalence of d-aspartate and nuclear weapons-related radiocarbon. J. Clin. Invest. 1991, 87:1828-1834.
    • (1991) J. Clin. Invest. , vol.87 , pp. 1828-1834
    • Shapiro, S.1    Endicott, S.2    Province, M.3    Pierce, J.4    Campbell, E.5
  • 28
    • 44049093740 scopus 로고    scopus 로고
    • Collagen turnover in normal and degenerate human intervertebral discs as determined by the racemization of aspartic acid
    • Sivan S.-S., Wachtel E., Tsitron E., Sakkee N., van der Ham F., DeGroot J., Roberts S., Maroudas A. Collagen turnover in normal and degenerate human intervertebral discs as determined by the racemization of aspartic acid. J. Biol. Chem. 2008, 283:8796-8801.
    • (2008) J. Biol. Chem. , vol.283 , pp. 8796-8801
    • Sivan, S.-S.1    Wachtel, E.2    Tsitron, E.3    Sakkee, N.4    van der Ham, F.5    DeGroot, J.6    Roberts, S.7    Maroudas, A.8
  • 29
    • 18044364423 scopus 로고    scopus 로고
    • Pathological proteins in Parkinson's disease: focus on the proteasome
    • Snyder H., Wolozin B. Pathological proteins in Parkinson's disease: focus on the proteasome. J. Mol. Neurosci. 2004, 24:425-442.
    • (2004) J. Mol. Neurosci. , vol.24 , pp. 425-442
    • Snyder, H.1    Wolozin, B.2
  • 30
    • 0034571008 scopus 로고    scopus 로고
    • Molecular chaperones and the aging process
    • Soti C., Csermely P. Molecular chaperones and the aging process. Biogerontology 2000, 1:225-233.
    • (2000) Biogerontology , vol.1 , pp. 225-233
    • Soti, C.1    Csermely, P.2
  • 31
    • 50049119429 scopus 로고    scopus 로고
    • Deamidation destabilizes and triggers aggregation of a lens proteins, βA3 crystallin
    • Takata T., Oxford J.T., Demeler B., Lampi K.J. Deamidation destabilizes and triggers aggregation of a lens proteins, βA3 crystallin. Protein Sci. 2008, 17:1565-1575.
    • (2008) Protein Sci. , vol.17 , pp. 1565-1575
    • Takata, T.1    Oxford, J.T.2    Demeler, B.3    Lampi, K.J.4
  • 32
    • 0037377941 scopus 로고    scopus 로고
    • Eye care for the future the Weisenfeld lecture
    • Taylor H.R. Eye care for the future the Weisenfeld lecture. Invest. Ophthalmol. Vis. Sci. 2003, 44:1413-1414.
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 1413-1414
    • Taylor, H.R.1
  • 33
    • 77952409743 scopus 로고    scopus 로고
    • Aspartic acid racemization and collagen degradation markers reveal and accumulation of damage in tendon collagen that is enhanced with aging
    • Thorpe C.T., Streeter I., Pinchbeck G.L., Goodship A.E., Clegg P.D., Birch H.L. Aspartic acid racemization and collagen degradation markers reveal and accumulation of damage in tendon collagen that is enhanced with aging. J. Biol. Chem. 2010, 285:15674-15681.
    • (2010) J. Biol. Chem. , vol.285 , pp. 15674-15681
    • Thorpe, C.T.1    Streeter, I.2    Pinchbeck, G.L.3    Goodship, A.E.4    Clegg, P.D.5    Birch, H.L.6
  • 34
    • 0028177534 scopus 로고
    • Racemization of Asp23 residue affects the aggregation properties of Alzheimer amyloid beta protein analogues
    • Tomiyama T., Asano S., Furiya Y., Shirasawa T., Endo N., Mori H. Racemization of Asp23 residue affects the aggregation properties of Alzheimer amyloid beta protein analogues. J. Biol. Chem. 1994, 269:10205-10208.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10205-10208
    • Tomiyama, T.1    Asano, S.2    Furiya, Y.3    Shirasawa, T.4    Endo, N.5    Mori, H.6
  • 35
    • 61849134343 scopus 로고    scopus 로고
    • Presbyopia. Emerging from a blur towards an understanding of the molecular basis for this most common eye condition
    • Truscott R.J. Presbyopia. Emerging from a blur towards an understanding of the molecular basis for this most common eye condition. Exp. Eye Res. 2009, 88:241-247.
    • (2009) Exp. Eye Res. , vol.88 , pp. 241-247
    • Truscott, R.J.1
  • 36
    • 0017330354 scopus 로고
    • Changes in human lens proteins during nuclear cataract formation
    • Truscott R.J.W., Augusteyn R.C. Changes in human lens proteins during nuclear cataract formation. Exp. Eye Res. 1977, 24:159-170.
    • (1977) Exp. Eye Res. , vol.24 , pp. 159-170
    • Truscott, R.J.W.1    Augusteyn, R.C.2
  • 37
    • 78650202678 scopus 로고    scopus 로고
    • Presbyopia and cataract: a question of heat and time
    • Truscott R.J.W., Zhu X. Presbyopia and cataract: a question of heat and time. Prog. Retin. Eye Res. 2010, 29:487-499.
    • (2010) Prog. Retin. Eye Res. , vol.29 , pp. 487-499
    • Truscott, R.J.W.1    Zhu, X.2
  • 38
    • 0041507039 scopus 로고    scopus 로고
    • Lifespan extension in C. elegans by a molecular chaperone dependent upon insulin-like signals
    • Walker G.A., Lithgow G.J. Lifespan extension in C. elegans by a molecular chaperone dependent upon insulin-like signals. Aging Cell 2003, 2:131-139.
    • (2003) Aging Cell , vol.2 , pp. 131-139
    • Walker, G.A.1    Lithgow, G.J.2
  • 39
    • 4344591769 scopus 로고    scopus 로고
    • Multiple-stress analysis for isolation of Drosophila longevity genes
    • Wang H.-D., Kazemi-Esfarjani P., Benzer S. Multiple-stress analysis for isolation of Drosophila longevity genes. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:12610-12615.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12610-12615
    • Wang, H.-D.1    Kazemi-Esfarjani, P.2    Benzer, S.3
  • 40
    • 0033548661 scopus 로고    scopus 로고
    • Deamidation and isoaspartate formation in smeared tau in paired helical filaments
    • Watanabe A., Takio K., Ihara Y. Deamidation and isoaspartate formation in smeared tau in paired helical filaments. J. Biol. Chem. 1999, 274:7368-7378.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7368-7378
    • Watanabe, A.1    Takio, K.2    Ihara, Y.3
  • 41
    • 78649990084 scopus 로고    scopus 로고
    • Age-dependent denaturation of enzymes in the human lens: a paradigm for organismic aging?
    • Zhu X., Korlimbinis A., Truscott R.J.W. Age-dependent denaturation of enzymes in the human lens: a paradigm for organismic aging?. Rejuvenation Res. 2010, 13:1-8.
    • (2010) Rejuvenation Res. , vol.13 , pp. 1-8
    • Zhu, X.1    Korlimbinis, A.2    Truscott, R.J.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.