메뉴 건너뛰기




Volumn 40, Issue 1, 2006, Pages 1-9

Dimerisation of N-acetyl-L-tyrosine ethyl ester and Aβ peptides via formation of dityrosine

Author keywords

Alzheimer's disease; Amyloid peptide; Dityrosine; Horseradish peroxidase; Metal catalyzed oxidation; Oxidative stress

Indexed keywords

AMYLOID BETA PROTEIN; HORSERADISH PEROXIDASE; HYDROGEN PEROXIDE; N ACETYLTYROSINE ETHYL ESTER; TYROSINE;

EID: 29744443811     PISSN: 10715762     EISSN: 10292470     Source Type: Journal    
DOI: 10.1080/10715760500329721     Document Type: Article
Times cited : (25)

References (45)
  • 1
    • 0036591849 scopus 로고    scopus 로고
    • Lipid peroxidation and protein oxidation in Alzheimer's disease brain: Potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress
    • [Review]
    • Butterfield, DA and Lauderback, CM. (2002) Lipid peroxidation and protein oxidation in Alzheimer's disease brain: Potential causes and consequences involving amyloid beta-peptide-associated free radical oxidative stress Free Radic Biol Med, 32(11), pp. 1050-1060. [Review]
    • (2002) Free Radic Biol Med , vol.32 , Issue.11 , pp. 1050-1060
    • Butterfield, D.A.1    Lauderback, C.M.2
  • 2
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence
    • Dong, J Atwood, CS Anderson, VE Siedlak, SL Smith, MA Perry, G and Carey, PR. (2003) Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence Biochemistry, 42(10), pp. 2768-2773.
    • (2003) Biochemistry , vol.42 , Issue.10 , pp. 2768-2773
    • Dong, J.1    Atwood, C.S.2    Anderson, V.E.3    Siedlak, S.L.4    Smith, M.A.5    Perry, G.6    Carey, P.R.7
  • 3
    • 3242735769 scopus 로고    scopus 로고
    • An i-4, i, i+4 reductive and nucleophilic zipper shared by both prion protein and beta-amyloid peptide sequences supports a common putative molecular mechanism
    • www.chemistrymag.org/cji/2000/027035le.htm
    • Yang, C. (2000) An i-4, i, i+4 reductive and nucleophilic zipper shared by both prion protein and beta-amyloid peptide sequences supports a common putative molecular mechanism Chem J Internet, 2(7), pp. 35. www.chemistrymag.org/cji/2000/027035le.htm
    • (2000) Chem J Internet , vol.2 , Issue.7 , pp. 35
    • Yang, C.1
  • 4
    • 2942737245 scopus 로고    scopus 로고
    • Metal catalyzed oxidative damage and oligomerization of the amyloid-β peptide (Aβ) of Alzheimer's disease
    • Ali, F.E. Barnham, K.J. Barrow, C.J. and Separovic, F. (2004) Metal catalyzed oxidative damage and oligomerization of the amyloid-β peptide (Aβ) of Alzheimer's disease Aust J Chem, 57, pp. 507 - 518.
    • (2004) Aust J Chem , vol.57 , pp. 507-518
    • Ali, F.E.1    Barnham, K.J.2    Barrow, C.J.3    Separovic, F.4
  • 5
    • 15044359925 scopus 로고    scopus 로고
    • Copper catalysed oxidation of amino acids and Alzheimer's disease
    • Ali, FE Barnham, KJ Barrow, CJ and Separovic, F. (2004) Copper catalysed oxidation of amino acids and Alzheimer's disease Lett Pept Sci, 10(5-6), pp. 405 - 412.
    • (2004) Lett Pept Sci , vol.10 , Issue.5-6 , pp. 405-412
    • Ali, F.E.1    Barnham, K.J.2    Barrow, C.J.3    Separovic, F.4
  • 6
    • 0242417426 scopus 로고    scopus 로고
    • Dityrosine cross-linked Aβ peptides: Fibrillar β-structure in Aβ(1-40) is conducive to formation of dityrosine cross-links but a dityrosine cross-link in Aβ(8-14) does not induce β-structure
    • Yoburn, JC Tian, W Brower, JO Nowick, JS Glabe, CG and Van Vranken, DL. (2003) Dityrosine cross-linked Aβ peptides: Fibrillar β-structure in Aβ(1-40) is conducive to formation of dityrosine cross-links but a dityrosine cross-link in Aβ(8-14) does not induce β-structure Chem Res Toxicol, 16(4), pp. 531-535.
    • (2003) Chem Res Toxicol , vol.16 , Issue.4 , pp. 531-535
    • Yoburn, J.C.1    Tian, W.2    Brower, J.O.3    Nowick, J.S.4    Glabe, C.G.5    Van Vranken, D.L.6
  • 7
    • 0032543380 scopus 로고    scopus 로고
    • A critical role for tyrosine residues in His(6)Ni-mediated protein cross-linking Biochem
    • Fancy, DA and Kodadek, T. (1998) A critical role for tyrosine residues in His(6)Ni-mediated protein cross-linking Biochem Biophys Res Commun, 247(2), pp. 420 - 426.
    • (1998) Biophys Res Commun , vol.247 , Issue.2 , pp. 420-426
    • Fancy, D.A.1    Kodadek, T.2
  • 10
    • 0035819340 scopus 로고    scopus 로고
    • Oxidative phenol coupling-tyrosine dimers and libraries containing tyrosyl peptide dimers
    • Eickhoff, H Jung, G and Rieker, A. (2001) Oxidative phenol coupling-tyrosine dimers and libraries containing tyrosyl peptide dimers Tetrahedron, 57(2), pp. 353 - 364.
    • (2001) Tetrahedron , vol.57 , Issue.2 , pp. 353-364
    • Eickhoff, H.1    Jung, G.2    Rieker, A.3
  • 11
    • 0035250633 scopus 로고    scopus 로고
    • Ab initio studies on the mechanism of tyrosine coupling
    • Shamovsky, IL Riopelle, RJ and Ross GM. (2001) Ab initio studies on the mechanism of tyrosine coupling J Phys Chem A, 105(6), pp. 1061 - 1070.
    • (2001) J Phys Chem A , vol.105 , Issue.6 , pp. 1061-1070
    • Shamovsky, I.L.1    Riopelle, R.J.2    Ross, G.M.3
  • 12
    • 0030569333 scopus 로고    scopus 로고
    • Dityrosine bridge formation and thyroid hormone synthesis are tightly linked and are both dependent on N-glycans
    • Baudry, N Lejeune, PJ Niccoli, P Vinet, L Carayon, P and Mallet, B. (1996) Dityrosine bridge formation and thyroid hormone synthesis are tightly linked and are both dependent on N-glycans FEBS Lett, 396(2-3), pp. 223 - 226.
    • (1996) FEBS Lett , vol.396 , Issue.2-3 , pp. 223-226
    • Baudry, N.1    Lejeune, P.J.2    Niccoli, P.3    Vinet, L.4    Carayon, P.5    Mallet, B.6
  • 13
    • 0034610314 scopus 로고    scopus 로고
    • Structural studies on some dityrosine-cross-linked globular proteins: Stability is weakened, but activity is not abolished
    • Kanwar, R and Balasubramanian, D. (2000) Structural studies on some dityrosine-cross-linked globular proteins: Stability is weakened, but activity is not abolished Biochemistr39(48), pp. 14976 - 14983.
    • (2000) Biochemistry , vol.39 , Issue.48 , pp. 14976-14983
    • Kanwar, R.1    Balasubramanian, D.2
  • 14
    • 0023149376 scopus 로고
    • Dityrosine formation in calmodulin
    • Malencik, DA and Anderson, SR. (1987) Dityrosine formation in calmodulin Biochemistry, 26(3), pp. 695 - 704.
    • (1987) Biochemistry , vol.26 , Issue.3 , pp. 695-704
    • Malencik, D.A.1    Anderson, S.R.2
  • 15
    • 0029919963 scopus 로고    scopus 로고
    • Dityrosine formation in calmodulin - Cross-linking and polymerization catalyzed by arthromyces peroxidase
    • Malencik, DA and Anderson, SR. (1996) Dityrosine formation in calmodulin - cross-linking and polymerization catalyzed by arthromyces peroxidase Biochemistry, 35(14), pp. 4375 - 4386.
    • (1996) Biochemistry , vol.35 , Issue.14 , pp. 4375-4386
    • Malencik, D.A.1    Anderson, S.R.2
  • 16
    • 29744462467 scopus 로고
    • Lipid peroxidation by peroxidase-catalyzed bioactivation of tyrosine
    • Guerin, MC and Torreilles, J. (1995) Lipid peroxidation by peroxidase-catalyzed bioactivation of tyrosine Redox Rep, 1(4), pp. 287 - 290.
    • (1995) Redox Rep , vol.1 , Issue.4 , pp. 287-290
    • Guerin, M.C.1    Torreilles, J.2
  • 17
    • 0033117503 scopus 로고    scopus 로고
    • Mechanisms of oxidative damage by myeloperoxidase in atherosclerosis and other inflammatory disorders
    • Heinecke, JW. (1999) Mechanisms of oxidative damage by myeloperoxidase in atherosclerosis and other inflammatory disorders J Lab Clin Med, 133(4), pp. 321 - 325.
    • (1999) J Lab Clin Med , vol.133 , Issue.4 , pp. 321-325
    • Heinecke, J.W.1
  • 18
    • 0027267487 scopus 로고
    • Oxidative tyrosylation of high density lipoprotein by peroxidase enhances cholesterol removal from cultured fibroblasts and macrophage foam cells
    • Francis, GA Mendez, AJ Bierman, EL and Heinecke, JW. (1993) Oxidative tyrosylation of high density lipoprotein by peroxidase enhances cholesterol removal from cultured fibroblasts and macrophage foam cells Proc Natl Acad Sci USA, 90(14), pp. 6631 - 6635.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.14 , pp. 6631-6635
    • Francis, G.A.1    Mendez, A.J.2    Bierman, E.L.3    Heinecke, J.W.4
  • 19
    • 0027292790 scopus 로고
    • Tyrosyl radical generated by myeloperoxidase catalyzes the oxidative cross-linking of proteins
    • Heinecke, JW Li, W Francis, GA and Goldstein, JA. (1993) Tyrosyl radical generated by myeloperoxidase catalyzes the oxidative cross-linking of proteins J Clin Investing, 91(6), pp. 2866 - 2872.
    • (1993) J Clin Investing , vol.91 , Issue.6 , pp. 2866-2872
    • Heinecke, J.W.1    Li, W.2    Francis, G.A.3    Goldstein, J.A.4
  • 20
    • 0027417395 scopus 로고
    • Dityrosine, a specific marker of oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophils and macrophages
    • Heinecke, JW Li, W Daehnke, HL, III and Goldstein, JA. (1993) Dityrosine, a specific marker of oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophils and macrophages J Biol Chem, 268(6), pp. 4069 - 4077.
    • (1993) J Biol Chem , vol.268 , Issue.6 , pp. 4069-4077
    • Heinecke, J.W.1    Li, W.2    Daehnke III, H.L.3    Goldstein, J.A.4
  • 21
    • 0029808085 scopus 로고    scopus 로고
    • Human phagocytes employ the myeloperoxidase-hydrogen peroxide system to synthesize dityrosine, trityrosine, pulcherosine, and isodityrosine by a tyrosyl radical-dependent pathway
    • Jacob, JS Cistola, DP Hsu, FF Muzaffar, S Mueller, DM Hazen, SL and Heinecke, JW. (1996) Human phagocytes employ the myeloperoxidase-hydrogen peroxide system to synthesize dityrosine, trityrosine, pulcherosine, and isodityrosine by a tyrosyl radical-dependent pathway J Biol Chem, 271(33), pp. 19950 - 19956.
    • (1996) J Biol Chem , vol.271 , Issue.33 , pp. 19950-19956
    • Jacob, J.S.1    Cistola, D.P.2    Hsu, F.F.3    Muzaffar, S.4    Mueller, D.M.5    Hazen, S.L.6    Heinecke, J.W.7
  • 22
    • 0029557684 scopus 로고
    • Kinetics of oxidation of tyrosine and dityrosine by myeloperoxidase compounds i and ii - Implications for lipoprotein peroxidation studies
    • Marquez, LA and Dunford, HB. (1995) Kinetics of oxidation of tyrosine and dityrosine by myeloperoxidase compounds i and ii - implications for lipoprotein peroxidation studies J Biol Chem, 270(51), pp. 30434-30440.
    • (1995) J Biol Chem , vol.270 , Issue.51 , pp. 30434-30440
    • Marquez, L.A.1    Dunford, H.B.2
  • 23
    • 0028076845 scopus 로고
    • Tyrosyl radical generated by myeloperoxidase is a physiological catalyst for the initiation of lipid peroxidation in low density lipoprotein
    • Savenkova, MI Mueller, DM and Heinecke, JW. (1994) Tyrosyl radical generated by myeloperoxidase is a physiological catalyst for the initiation of lipid peroxidation in low density lipoprotein J Biol Chem, 269(32), pp. 20394-20400.
    • (1994) J Biol Chem , vol.269 , Issue.32 , pp. 20394-20400
    • Savenkova, M.I.1    Mueller, D.M.2    Heinecke, J.W.3
  • 24
    • 0032493470 scopus 로고    scopus 로고
    • A kinetic model of the myeloperoxidase hydrogen peroxide chloride ion system in phagolysosomes
    • Stanbro, WD. (1998) A kinetic model of the myeloperoxidase hydrogen peroxide chloride ion system in phagolysosomes J Theor Biol, 193(1), pp. 59 - 68.
    • (1998) J Theor Biol , vol.193 , Issue.1 , pp. 59-68
    • Stanbro, W.D.1
  • 25
    • 0030967399 scopus 로고    scopus 로고
    • Myeloperoxidase-dependent generation of a tyrosine peroxide by neutrophils
    • Winterbourn, CC Pichorner, H and Kettle, AJ. (1997) Myeloperoxidase-dependent generation of a tyrosine peroxide by neutrophils Arch Biochem Biophys, 338(1), pp. 15 - 21.
    • (1997) Arch Biochem Biophys , vol.338 , Issue.1 , pp. 15-21
    • Winterbourn, C.C.1    Pichorner, H.2    Kettle, A.J.3
  • 26
    • 0027137992 scopus 로고
    • Neutrophil-catalysed dimerisation of tyrosyl peptides
    • Salmantabcheh, S Rabgaoui, N and Torreilles, J. (1993) Neutrophil-catalysed dimerisation of tyrosyl peptides Free Radic Res Commun, 19(4), pp. 217 - 227.
    • (1993) Free Radic Res Commun , vol.19 , Issue.4 , pp. 217-227
    • Salmantabcheh, S.1    Rabgaoui, N.2    Torreilles, J.3
  • 27
    • 0031441428 scopus 로고    scopus 로고
    • Dimer formation by cytochrome c-catalyzed oxidation of tyrosine and enkephalins
    • Foppoli, C Demarco, C Blarzino, C Coccia, R Mosca, L and Rosei, MA. (1997) Dimer formation by cytochrome c-catalyzed oxidation of tyrosine and enkephalins Amino Acids, 13(3-4), pp. 273 - 280.
    • (1997) Amino Acids , vol.13 , Issue.3-4 , pp. 273-280
    • Foppoli, C.1    Demarco, C.2    Blarzino, C.3    Coccia, R.4    Mosca, L.5    Rosei, M.A.6
  • 28
    • 0032806289 scopus 로고    scopus 로고
    • Hydroxyl radical generation during exercise increases mitochondrial protein oxidation and levels of urinary dityrosine
    • Leeuwenburgh, C Hansen, PA Holloszy, JO and Heinecke, JW. (1999) Hydroxyl radical generation during exercise increases mitochondrial protein oxidation and levels of urinary dityrosine Free Radic Biol Med, 27(1-2), pp. 186 - 192.
    • (1999) Free Radic Biol Med , vol.27 , Issue.1-2 , pp. 186-192
    • Leeuwenburgh, C.1    Hansen, P.A.2    Holloszy, J.O.3    Heinecke, J.W.4
  • 29
    • 0032531735 scopus 로고    scopus 로고
    • Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation
    • Hensley, K Maidt, ML Yu, Z Sang, H Markesbery, WR and Floyd, RA. (1998) Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation J Neurol Sci 18(20), pp. 8126 - 8132.
    • (1998) J Neurol Sci , vol.18 , Issue.20 , pp. 8126-8132
    • Hensley, K.1    Maidt, M.L.2    Yu, Z.3    Sang, H.4    Markesbery, W.R.5    Floyd, R.A.6
  • 30
    • 0032422401 scopus 로고    scopus 로고
    • Immunohistochemical and ELISA assays for biomarkers of oxidative stress in aging and disease
    • Towards Prolongation of the Health Life Span
    • Onorato, JM Thorpe, SR and Baynes, JW. (1998) Immunohistochemical and ELISA assays for biomarkers of oxidative stress in aging and disease Ann N Y Acad Sci, 854, pp. 277 - 290. Towards Prolongation of the Health Life Span
    • (1998) Ann N Y Acad Sci , vol.854 , pp. 277-290
    • Onorato, J.M.1    Thorpe, S.R.2    Baynes, J.W.3
  • 31
    • 0033045848 scopus 로고    scopus 로고
    • In vitro peroxidase oxidation induces stable dimers of β-amyloid (1-42) through dityrosine bridge formation
    • Galeazzi, L Ronchi, P Franceschi, C and Giunta, S. (1999) In vitro peroxidase oxidation induces stable dimers of β-amyloid (1-42) through dityrosine bridge formation Amyloid, 6(1), pp. 7 - 13.
    • (1999) Amyloid , vol.6 , Issue.1 , pp. 7-13
    • Galeazzi, L.1    Ronchi, P.2    Franceschi, C.3    Giunta, S.4
  • 33
    • 0034609516 scopus 로고    scopus 로고
    • The oligomerization of amyloid β-protein begins intracellularly in cells derived from human brain
    • Walsh, DM Tseng, BP Rydel, RE Podlisny, MB and Selkoe, DJ. (2000) The oligomerization of amyloid β-protein begins intracellularly in cells derived from human brain Biochemistry, 39(35), pp. 10831 - 10839.
    • (2000) Biochemistry , vol.39 , Issue.35 , pp. 10831-10839
    • Walsh, D.M.1    Tseng, B.P.2    Rydel, R.E.3    Podlisny, M.B.4    Selkoe, D.J.5
  • 34
    • 0032569073 scopus 로고    scopus 로고
    • Total synthesis of bastadins 2, 3, and 6
    • Guo, ZW Machiya, K Salamonczyk, GM and Sih, CJ. (1998) Total synthesis of bastadins 2, 3, and 6 J Org Chem, 63(13), pp. 4269 - 4276.
    • (1998) J Org Chem , vol.63 , Issue.13 , pp. 4269-4276
    • Guo, Z.W.1    Machiya, K.2    Salamonczyk, G.M.3    Sih, C.J.4
  • 35
    • 0033578402 scopus 로고    scopus 로고
    • The Aβ 3-pyroglut tamyl and 11-pyroglutamyl peptides found in senile plaque have greater βsheet forming and aggregation propensities in vitro than full-length Aβ
    • He, W and Barrow, CJ. (1999) The Aβ 3-pyroglut tamyl and 11-pyroglutamyl peptides found in senile plaque have greater βsheet forming and aggregation propensities in vitro than full-length Aβ Biochemistry, 38(33), pp. 10871 - 10877.
    • (1999) Biochemistry , vol.38 , Issue.33 , pp. 10871-10877
    • He, W.1    Barrow, C.J.2
  • 37
    • 0029661424 scopus 로고    scopus 로고
    • Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay
    • Ida, N Hartmann, T Pantel, J Schroder, J Zerfass, R Forstl, H Sandbrink, R Masters, CL and Beyreuther, K. (1996) Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay J Biol Chem, 271(37), pp. 22908 - 22914.
    • (1996) J Biol Chem , vol.271 , Issue.37 , pp. 22908-22914
    • Ida, N.1    Hartmann, T.2    Pantel, J.3    Schroder, J.4    Zerfass, R.5    Forstl, H.6    Sandbrink, R.7    Masters, C.L.8    Beyreuther, K.9
  • 38
    • 0035451917 scopus 로고    scopus 로고
    • The hydrogen peroxide/copper ion system, but not other metal-catalyzed oxidation systems, produces protein-bound dityrosine
    • Kato, Y Kitamoto, N Kawai, Y and Osawa, T. (2001) The hydrogen peroxide/ copper ion system, but not other metal-catalyzed oxidation systems, produces protein-bound dityrosine Free Radic Biol Med, 31(5), pp. 624 - 632.
    • (2001) Free Radic Biol Med , vol.31 , Issue.5 , pp. 624-632
    • Kato, Y.1    Kitamoto, N.2    Kawai, Y.3    Osawa, T.4
  • 39
    • 0018370397 scopus 로고
    • Preparation and isolation of dityrosine
    • Malanik, V and Ledvina, M. (1979) Preparation and isolation of dityrosine Prep Biochem, 9(3), pp. 273 - 280.
    • (1979) Prep Biochem , vol.9 , Issue.3 , pp. 273-280
    • Malanik, V.1    Ledvina, M.2
  • 41
    • 0027180882 scopus 로고
    • Formation of o-tyrosine and dityrosine in proteins during radiolytic and metal-catalyzed oxidation
    • Huggins, TG Wells-Knecht, MC Detorie, NA Baynes, JW and Thorpe, SR. (1993) Formation of o-tyrosine and dityrosine in proteins during radiolytic and metal-catalyzed oxidation J Biol Chem, 268(17), pp. 12341 - 12347.
    • (1993) J Biol Chem , vol.268 , Issue.17 , pp. 12341-12347
    • Huggins, T.G.1    Wells-Knecht, M.C.2    Detorie, N.A.3    Baynes, J.W.4    Thorpe, S.R.5
  • 42
    • 0031788660 scopus 로고    scopus 로고
    • Immunohistochemical detection of dityrosine in lipofuscin pigments in the aged human brain
    • Kato, Y Maruyama, W Naoi, M Hashizume, Y and Osawa, T. (1998) Immunohistochemical detection of dityrosine in lipofuscin pigments in the aged human brain FEBS Lett, 439(3), pp. 231 - 234.
    • (1998) FEBS Lett , vol.439 , Issue.3 , pp. 231-234
    • Kato, Y.1    Maruyama, W.2    Naoi, M.3    Hashizume, Y.4    Osawa, T.5
  • 43
    • 0027254198 scopus 로고
    • Oxidized amino acids in lens protein with age - Measurement of o-tyrosine and dityrosine in the aging human lens
    • Wellsknecht, MC Huggins, TG Dyer, DG Thorpe, SR and Baynes, JW. (1993) Oxidized amino acids in lens protein with age - measurement of o-tyrosine and dityrosine in the aging human lens J Biol Chem, 268(17), pp. 12348 - 12352.
    • (1993) J Biol Chem , vol.268 , Issue.17 , pp. 12348-12352
    • Wellsknecht, M.C.1    Huggins, T.G.2    Dyer, D.G.3    Thorpe, S.R.4    Baynes, J.W.5
  • 44
    • 0031260095 scopus 로고    scopus 로고
    • Caloric restriction attenuates dityrosine cross-linking of cardiac and skeletal muscle proteins in aging mice
    • Leeuwenburgh, C Wagner, P and JO Sohal, RS and Heinecke, JW. (1997) Caloric restriction attenuates dityrosine cross-linking of cardiac and skeletal muscle proteins in aging mice Arch Biochem Biophys, 346(1), pp. 74 - 80.
    • (1997) Arch Biochem Biophys , vol.346 , Issue.1 , pp. 74-80
    • Leeuwenburgh, C.1    Wagner, P.J.O.2    Sohal, R.S.3    Heinecke, J.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.