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Volumn 13, Issue 2, 2014, Pages 226-234

Human protein aging: Modification and crosslinking through dehydroalanine and dehydrobutyrine intermediates

Author keywords

Aging; Glutathione; Lens; Protein protein crosslinking

Indexed keywords

AMINO ACID; BETA CRYSTALLIN; DEHYDROALANINE; DEHYDROBUTYRINE; GLUTATHIONE; LENS PROTEIN; PHOSPHORIC ACID; PHOSPHOSERINE; PHOSPHOTHREONINE; SERINE; THREONINE; UNCLASSIFIED DRUG;

EID: 84895822337     PISSN: 14749718     EISSN: 14749726     Source Type: Journal    
DOI: 10.1111/acel.12164     Document Type: Article
Times cited : (67)

References (46)
  • 1
    • 40649107852 scopus 로고    scopus 로고
    • Dehydroalanine derived from cysteine is a common post-translational modification in human serum albumin
    • Bar-Or R, Rael LT, Bar-Or D (2008) Dehydroalanine derived from cysteine is a common post-translational modification in human serum albumin. Rapid Commun. Mass Spectrom. 22, 711-716.
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 711-716
    • Bar-Or, R.1    Rael, L.T.2    Bar-Or, D.3
  • 3
    • 0023177775 scopus 로고
    • Lanthionine, a protein cross-link in cataractous human lenses
    • Bessems GJ, Rennen HJ, Hoenders HJ (1987) Lanthionine, a protein cross-link in cataractous human lenses. Exp. Eye Res. 44, 691-695.
    • (1987) Exp. Eye Res. , vol.44 , pp. 691-695
    • Bessems, G.J.1    Rennen, H.J.2    Hoenders, H.J.3
  • 4
    • 0034575026 scopus 로고    scopus 로고
    • Age-related de-phosphorylation of proteins in dentin: a biological tool for assessment of protein age
    • Cloos PA, Jensen AL (2000) Age-related de-phosphorylation of proteins in dentin: a biological tool for assessment of protein age. Biogerontology 1, 341-356.
    • (2000) Biogerontology , vol.1 , pp. 341-356
    • Cloos, P.A.1    Jensen, A.L.2
  • 6
    • 0016252758 scopus 로고
    • Changes to the proteins of the human lens nucleus in cataract
    • Dilley KJ, Pirie A (1974) Changes to the proteins of the human lens nucleus in cataract. Exp. Eye Res. 19, 59-72.
    • (1974) Exp. Eye Res. , vol.19 , pp. 59-72
    • Dilley, K.J.1    Pirie, A.2
  • 7
    • 83455171579 scopus 로고    scopus 로고
    • Protein aggregation in congenital myopathies
    • Goebel HH, Blaschek A (2011) Protein aggregation in congenital myopathies. Semin. Pediatr. Neurol. 4, 272-276.
    • (2011) Semin. Pediatr. Neurol. , vol.4 , pp. 272-276
    • Goebel, H.H.1    Blaschek, A.2
  • 8
    • 70349263467 scopus 로고    scopus 로고
    • Age-related changes in the spatial distribution of human lens alpha-crystallin products by MALDI imaging mass spectrometry
    • Grey AC, Schey KL (2009) Age-related changes in the spatial distribution of human lens alpha-crystallin products by MALDI imaging mass spectrometry. Invest. Ophthalmol. Vis. Sci. 50, 4319-4329.
    • (2009) Invest. Ophthalmol. Vis. Sci. , vol.50 , pp. 4319-4329
    • Grey, A.C.1    Schey, K.L.2
  • 9
    • 4344677922 scopus 로고    scopus 로고
    • Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease
    • Grune T, Jung T, Merker K, Davies KJ (2004) Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int. J. Biochem. Cell Biol. 36, 2519-2530.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2519-2530
    • Grune, T.1    Jung, T.2    Merker, K.3    Davies, K.J.4
  • 10
    • 0014787125 scopus 로고
    • Free and protein-bound glutathione in normal and cataractous human lenses
    • Harding JJ (1970) Free and protein-bound glutathione in normal and cataractous human lenses. Biochem. J. 117, 957-960.
    • (1970) Biochem. J. , vol.117 , pp. 957-960
    • Harding, J.J.1
  • 11
    • 4043127599 scopus 로고    scopus 로고
    • Crystallins in water soluble-high molecular weight protein fractions and water insoluble protein fractions in aging and cataractous human lenses
    • Harrington V, McCall S, Huynh S, Srivastava K, Srivastava OP (2004) Crystallins in water soluble-high molecular weight protein fractions and water insoluble protein fractions in aging and cataractous human lenses. Mol. Vis. 10, 476-489.
    • (2004) Mol. Vis. , vol.10 , pp. 476-489
    • Harrington, V.1    McCall, S.2    Huynh, S.3    Srivastava, K.4    Srivastava, O.P.5
  • 12
    • 79551718144 scopus 로고    scopus 로고
    • Phosphoproteomics characterization of novel phosphorylated sites of lens proteins from normal and cataractous human eye lenses
    • Huang C-H, Wang Y-T, Tsai C-F, Chen Y-J, Lee J-S, Chiou SH (2011) Phosphoproteomics characterization of novel phosphorylated sites of lens proteins from normal and cataractous human eye lenses. Mol. Vis. 17, 186-198.
    • (2011) Mol. Vis. , vol.17 , pp. 186-198
    • Huang, C.-H.1    Wang, Y.-T.2    Tsai, C.-F.3    Chen, Y.-J.4    Lee, J.-S.5    Chiou, S.H.6
  • 13
    • 77956389018 scopus 로고    scopus 로고
    • Evaluation of nonenzymatic posttranslational modification-derived products as biomarkers of molecular aging of proteins
    • Jaisson S, Gillery P (2010) Evaluation of nonenzymatic posttranslational modification-derived products as biomarkers of molecular aging of proteins. Clin. Chem. 56, 1401-1412.
    • (2010) Clin. Chem. , vol.56 , pp. 1401-1412
    • Jaisson, S.1    Gillery, P.2
  • 14
    • 0023176263 scopus 로고
    • Detection of the cross-linking amino acid, histidinoalanine, in human brown cataractous lens protein
    • Kanayama T, Miyanaga Y, Horiuchi K, Fujimoto D (1987) Detection of the cross-linking amino acid, histidinoalanine, in human brown cataractous lens protein. Exp. Eye Res. 44, 165-169.
    • (1987) Exp. Eye Res. , vol.44 , pp. 165-169
    • Kanayama, T.1    Miyanaga, Y.2    Horiuchi, K.3    Fujimoto, D.4
  • 16
    • 20944446301 scopus 로고    scopus 로고
    • Glutathionylation of lens proteins through the formation of thioether bond
    • Linetsky M, LeGrand RD (2005) Glutathionylation of lens proteins through the formation of thioether bond. Mol. Cell. Biochem. 272, 133-144.
    • (2005) Mol. Cell. Biochem. , vol.272 , pp. 133-144
    • Linetsky, M.1    LeGrand, R.D.2
  • 19
    • 0042198801 scopus 로고    scopus 로고
    • Redox regulation in the lens
    • Lou MF (2003) Redox regulation in the lens. Prog. Retin. Eye Res. 22, 657-682.
    • (2003) Prog. Retin. Eye Res. , vol.22 , pp. 657-682
    • Lou, M.F.1
  • 20
    • 45149103497 scopus 로고    scopus 로고
    • Radiocarbon dating of the human eye lens crystallins reveal proteins without carbon turnover throughout life
    • Lynnerup N, Kjeldsen H, Heegaard S, Jacobsen C, Heinemeier J (2008) Radiocarbon dating of the human eye lens crystallins reveal proteins without carbon turnover throughout life. PLoS ONE 3, e1529.
    • (2008) PLoS ONE , vol.3
    • Lynnerup, N.1    Kjeldsen, H.2    Heegaard, S.3    Jacobsen, C.4    Heinemeier, J.5
  • 22
    • 0021815553 scopus 로고
    • In vivo decomposition of phosphoserine and serine in noncollagenous protein from human dentin
    • Masters PM (1985) In vivo decomposition of phosphoserine and serine in noncollagenous protein from human dentin. Calcif. Tissue Int. 37, 236-241.
    • (1985) Calcif. Tissue Int. , vol.37 , pp. 236-241
    • Masters, P.M.1
  • 23
    • 0028053274 scopus 로고
    • Domain interactions and connecting peptides in lens crystallins
    • Mayr EM, Jaenicke R, Glockshuber R (1994) Domain interactions and connecting peptides in lens crystallins. J. Mol. Biol. 235, 84-88.
    • (1994) J. Mol. Biol. , vol.235 , pp. 84-88
    • Mayr, E.M.1    Jaenicke, R.2    Glockshuber, R.3
  • 24
    • 0025748591 scopus 로고
    • High correlation between pentosidine protein crosslinks and pigmentation implicates ascorbate oxidation in human lens senescence and cataractogenesis
    • Nagaraj RH, Sell DR, Prabhakaram M, Ortwerth BJ, Monnier VM (1991) High correlation between pentosidine protein crosslinks and pigmentation implicates ascorbate oxidation in human lens senescence and cataractogenesis. Proc. Natl Acad. Sci. USA 88, 10257-10261.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 10257-10261
    • Nagaraj, R.H.1    Sell, D.R.2    Prabhakaram, M.3    Ortwerth, B.J.4    Monnier, V.M.5
  • 25
    • 80155157847 scopus 로고    scopus 로고
    • The seeds of neurodegeneration: prion-like spreading in ALS
    • Polymenidou M, Cleveland DW (2011) The seeds of neurodegeneration: prion-like spreading in ALS. Cell 147, 498-508.
    • (2011) Cell , vol.147 , pp. 498-508
    • Polymenidou, M.1    Cleveland, D.W.2
  • 26
    • 0021337196 scopus 로고
    • Lenticular glutathione synthesis: rate-limiting factors in its regulation and decline
    • Rathbun WB (1984) Lenticular glutathione synthesis: rate-limiting factors in its regulation and decline. Curr. Eye Res. 3, 101-108.
    • (1984) Curr. Eye Res. , vol.3 , pp. 101-108
    • Rathbun, W.B.1
  • 28
    • 55549092818 scopus 로고
    • Elimination reactions and hydrolysis of serine phosphate
    • Samuel D, Silver BL (1963) Elimination reactions and hydrolysis of serine phosphate. J. Chem. Soc., 289-296.
    • (1963) J. Chem. Soc. , pp. 289-296
    • Samuel, D.1    Silver, B.L.2
  • 30
    • 40449093778 scopus 로고    scopus 로고
    • Acid catalyzed 1, 2 Michael addition reaction: a viable synthetic route in designing fullerene core starlike macromolecule
    • Singh R, Goswami T (2008) Acid catalyzed 1, 2 Michael addition reaction: a viable synthetic route in designing fullerene core starlike macromolecule. J. Phys. Org. Chem. 21, 225-236.
    • (2008) J. Phys. Org. Chem. , vol.21 , pp. 225-236
    • Singh, R.1    Goswami, T.2
  • 31
    • 0025371285 scopus 로고
    • Quaternary interactions in eye lens beta-crystallins: basic and acidic subunits of beta-crystallins favor heterologous association
    • Slingsby C, Bateman OA (1990) Quaternary interactions in eye lens beta-crystallins: basic and acidic subunits of beta-crystallins favor heterologous association. Biochemistry 29, 6592-6599.
    • (1990) Biochemistry , vol.29 , pp. 6592-6599
    • Slingsby, C.1    Bateman, O.A.2
  • 32
    • 40649129442 scopus 로고    scopus 로고
    • Nonenzymatic posttranslational protein modifications in ageing
    • Soskić V, Groebe K, Schrattenholz A (2008) Nonenzymatic posttranslational protein modifications in ageing. Exp. Gerontol. 43, 247-257.
    • (2008) Exp. Gerontol. , vol.43 , pp. 247-257
    • Soskić, V.1    Groebe, K.2    Schrattenholz, A.3
  • 33
    • 0029151027 scopus 로고
    • Oxidative stress-induced cataract: mechanism of action
    • Spector A (1995) Oxidative stress-induced cataract: mechanism of action. FASEB J. 9, 1173-1182.
    • (1995) FASEB J. , vol.9 , pp. 1173-1182
    • Spector, A.1
  • 34
    • 1642524490 scopus 로고    scopus 로고
    • Characterization of covalent multimers of crystallins in aging human lenses
    • Srivastava OP, Kirk MC, Srivastava K (2004) Characterization of covalent multimers of crystallins in aging human lenses. J. Biol. Chem. 279, 10901-10909.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10901-10909
    • Srivastava, O.P.1    Kirk, M.C.2    Srivastava, K.3
  • 35
    • 0035039021 scopus 로고    scopus 로고
    • Protein oxidation in aging and age-related diseases
    • Stadtman ER (2001) Protein oxidation in aging and age-related diseases. Ann. N. Y. Acad. Sci. 928, 22-38.
    • (2001) Ann. N. Y. Acad. Sci. , vol.928 , pp. 22-38
    • Stadtman, E.R.1
  • 37
    • 0020520185 scopus 로고
    • Amino and carboxy-terminal regions in globular proteins
    • Thornton JM, Sibanda BL (1983) Amino and carboxy-terminal regions in globular proteins. J. Mol. Biol. 167, 443-460.
    • (1983) J. Mol. Biol. , vol.167 , pp. 443-460
    • Thornton, J.M.1    Sibanda, B.L.2
  • 38
    • 18044388716 scopus 로고    scopus 로고
    • Age-related nuclear cataract - oxidation is the key
    • Truscott RJW (2005) Age-related nuclear cataract - oxidation is the key. Exp. Eye Res. 80, 709-725.
    • (2005) Exp. Eye Res. , vol.80 , pp. 709-725
    • Truscott, R.J.W.1
  • 39
    • 80052338389 scopus 로고    scopus 로고
    • Macromolecular deterioration as the ultimate constraint on human lifespan
    • Truscott R (2011) Macromolecular deterioration as the ultimate constraint on human lifespan. Ageing Res. Rev. 10, 397-403.
    • (2011) Ageing Res. Rev. , vol.10 , pp. 397-403
    • Truscott, R.1
  • 40
    • 0017330354 scopus 로고
    • Changes in human lens proteins during nuclear cataract formation
    • Truscott RJW, Augusteyn RC (1977a) Changes in human lens proteins during nuclear cataract formation. Exp. Eye Res. 24, 159-170.
    • (1977) Exp. Eye Res. , vol.24 , pp. 159-170
    • Truscott, R.J.W.1    Augusteyn, R.C.2
  • 41
    • 0017656230 scopus 로고
    • The state of sulphydryl groups in normal and cataractous human lenses
    • Truscott RJW, Augusteyn RC (1977b) The state of sulphydryl groups in normal and cataractous human lenses. Exp. Eye Res. 25, 139-148.
    • (1977) Exp. Eye Res. , vol.25 , pp. 139-148
    • Truscott, R.J.W.1    Augusteyn, R.C.2
  • 42
    • 80052521522 scopus 로고    scopus 로고
    • Aquaporin-0 interacts with the FERM domain of ezrin/radixin/moesin proteins in the ocular lens
    • Wang Z, Schey KL (2011) Aquaporin-0 interacts with the FERM domain of ezrin/radixin/moesin proteins in the ocular lens. Invest. Ophthalmol. Vis. Sci. 52, 5079-5087.
    • (2011) Invest. Ophthalmol. Vis. Sci. , vol.52 , pp. 5079-5087
    • Wang, Z.1    Schey, K.L.2
  • 43
    • 77949894828 scopus 로고    scopus 로고
    • Posttranslational modifications of the bovine lens beaded filament proteins filensin and CP49
    • Wang Z, Obidike JE, Schey KL (2010) Posttranslational modifications of the bovine lens beaded filament proteins filensin and CP49. Invest. Ophthalmol. Vis. Sci. 51, 1565-1574.
    • (2010) Invest. Ophthalmol. Vis. Sci. , vol.51 , pp. 1565-1574
    • Wang, Z.1    Obidike, J.E.2    Schey, K.L.3
  • 44
    • 84862956256 scopus 로고    scopus 로고
    • Proteomic analysis of urine exosomes by multidimensional protein identification technology (MudPIT)
    • Wang Z, Hill S, Luther JM, Hachey DL, Schey KL (2012) Proteomic analysis of urine exosomes by multidimensional protein identification technology (MudPIT). Proteomics 2, 329-338.
    • (2012) Proteomics , vol.2 , pp. 329-338
    • Wang, Z.1    Hill, S.2    Luther, J.M.3    Hachey, D.L.4    Schey, K.L.5
  • 45
    • 84874976592 scopus 로고    scopus 로고
    • Proteomics and phosphoproteomics analysis of human lens fiber cell membranes
    • Wang Z, Han J, David LL, Schey KL (2013) Proteomics and phosphoproteomics analysis of human lens fiber cell membranes. Invest. Ophthalmol. Vis. Sci. 54, 1135-1143.
    • (2013) Invest. Ophthalmol. Vis. Sci. , vol.54 , pp. 1135-1143
    • Wang, Z.1    Han, J.2    David, L.L.3    Schey, K.L.4
  • 46
    • 38649131282 scopus 로고    scopus 로고
    • Identification and characterization of disulfide bonds in proteins and peptides from tandem MS data by use of the MassMatrix MS/MS search engine
    • Xu H, Zhang L, Freitas MA (2008) Identification and characterization of disulfide bonds in proteins and peptides from tandem MS data by use of the MassMatrix MS/MS search engine. J. Proteome Res. 7, 138-144.
    • (2008) J. Proteome Res. , vol.7 , pp. 138-144
    • Xu, H.1    Zhang, L.2    Freitas, M.A.3


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