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Volumn 400, Issue 4, 2010, Pages 889-907

Protein N-homocysteinylation induces the formation of toxic amyloid-like protofibrils

Author keywords

Homocysteine; Homocysteine thiolactone; Protein aggregation; Protein homocysteinylation

Indexed keywords

AMYLOID; BOVINE SERUM ALBUMIN; CONGO RED; HOMOCYSTEINE THIOLACTONE; THIOFLAVINE;

EID: 77954357800     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.05.039     Document Type: Article
Times cited : (68)

References (49)
  • 1
    • 0014964473 scopus 로고
    • Acylation of lysine and of arginine-rich histones with carbamyl phosphate and 1,3 diphosphoglycerate
    • Ramponi G., Grisolia S. Acylation of lysine and of arginine-rich histones with carbamyl phosphate and 1,3 diphosphoglycerate. Biochem. Biophys. Res. Commun. 1970, 38:1056-1063.
    • (1970) Biochem. Biophys. Res. Commun. , vol.38 , pp. 1056-1063
    • Ramponi, G.1    Grisolia, S.2
  • 2
    • 0013631017 scopus 로고
    • Homocitrulline formation following carbamylation of histones with carbamyl phosphate
    • Ramponi G., Leaver J.L., Grisolia S. Homocitrulline formation following carbamylation of histones with carbamyl phosphate. FEBS Lett. 1971, 16:311-314.
    • (1971) FEBS Lett. , vol.16 , pp. 311-314
    • Ramponi, G.1    Leaver, J.L.2    Grisolia, S.3
  • 3
    • 0016732890 scopus 로고
    • Nonenzymatic acetylation of histones with acetyl phosphate and acetyl adenylate
    • Ramponi G., Manao G., Camici G. Nonenzymatic acetylation of histones with acetyl phosphate and acetyl adenylate. Biochemistry 1975, 14:2681-2685.
    • (1975) Biochemistry , vol.14 , pp. 2681-2685
    • Ramponi, G.1    Manao, G.2    Camici, G.3
  • 4
    • 0035941951 scopus 로고    scopus 로고
    • Carbamoylation of glomerular and tubular proteins in patients with kidney failure: a potential mechanism of ongoing renal damage
    • Kraus L.M., Gaber L., Handorf C.R., Marti H.P., Kraus A.P. Carbamoylation of glomerular and tubular proteins in patients with kidney failure: a potential mechanism of ongoing renal damage. Swiss Med. Wkly. 2001, 131:139-145.
    • (2001) Swiss Med. Wkly. , vol.131 , pp. 139-145
    • Kraus, L.M.1    Gaber, L.2    Handorf, C.R.3    Marti, H.P.4    Kraus, A.P.5
  • 5
    • 0030585373 scopus 로고    scopus 로고
    • Inhibition of 6-phosphogluconate dehydrogenase by carbamylation and protection by alpha-crystallin, a chaperone-like protein
    • Ganea E., Harding J.J. Inhibition of 6-phosphogluconate dehydrogenase by carbamylation and protection by alpha-crystallin, a chaperone-like protein. Biochem. Biophys. Res. Commun. 1996, 222:626-631.
    • (1996) Biochem. Biophys. Res. Commun. , vol.222 , pp. 626-631
    • Ganea, E.1    Harding, J.J.2
  • 6
    • 0014480042 scopus 로고
    • Structural changes in human serum albumin induced by ingestion of acetylsalicylic acid
    • Hawkins D., Pinckard R.N., Crawford I.P., Farr R.S. Structural changes in human serum albumin induced by ingestion of acetylsalicylic acid. J. Clin. Invest. 1969, 48:536-542.
    • (1969) J. Clin. Invest. , vol.48 , pp. 536-542
    • Hawkins, D.1    Pinckard, R.N.2    Crawford, I.P.3    Farr, R.S.4
  • 7
    • 0023767723 scopus 로고
    • Identification of lysine residue 199 of human serum albumin as a binding site for benzylpenicilloyl groups
    • Yvon M., Wal J.M. Identification of lysine residue 199 of human serum albumin as a binding site for benzylpenicilloyl groups. FEBS Lett. 1988, 239:237-240.
    • (1988) FEBS Lett. , vol.239 , pp. 237-240
    • Yvon, M.1    Wal, J.M.2
  • 8
    • 33846994092 scopus 로고    scopus 로고
    • Amyloid-like aggregates of neuronal tau induced by formaldehyde promote apoptosis of neuronal cells
    • Nie C.L., Wang X.S., Liu Y., Perrett S., He R.Q. Amyloid-like aggregates of neuronal tau induced by formaldehyde promote apoptosis of neuronal cells. BMC Neurosci. 2007, 8:9.
    • (2007) BMC Neurosci. , vol.8 , pp. 9
    • Nie, C.L.1    Wang, X.S.2    Liu, Y.3    Perrett, S.4    He, R.Q.5
  • 9
    • 0037096983 scopus 로고    scopus 로고
    • Effects of modifications of alpha-crystallin on its chaperone and other properties
    • Derham B.K., Harding J.J. Effects of modifications of alpha-crystallin on its chaperone and other properties. Biochem. J. 2002, 364:711-717.
    • (2002) Biochem. J. , vol.364 , pp. 711-717
    • Derham, B.K.1    Harding, J.J.2
  • 10
    • 0028147210 scopus 로고
    • Alzheimer's disease. A glycation connection
    • Harrington C.R., Colaco C.A. Alzheimer's disease. A glycation connection. Nature 1994, 370:247-248.
    • (1994) Nature , vol.370 , pp. 247-248
    • Harrington, C.R.1    Colaco, C.A.2
  • 11
    • 0020537502 scopus 로고
    • Comparative evaluation of fifteen anti-sickling agents
    • Chang H., Ewert S.M., Bookchin R.M., Nagel R.L. Comparative evaluation of fifteen anti-sickling agents. Blood 1983, 61:693-704.
    • (1983) Blood , vol.61 , pp. 693-704
    • Chang, H.1    Ewert, S.M.2    Bookchin, R.M.3    Nagel, R.L.4
  • 12
    • 0027534543 scopus 로고
    • Synthesis of homocysteine thiolactone by methionyl-tRNA synthetase in cultured mammalian cells
    • Jakubowski H., Goldman E. Synthesis of homocysteine thiolactone by methionyl-tRNA synthetase in cultured mammalian cells. FEBS Lett. 1993, 317:237-240.
    • (1993) FEBS Lett. , vol.317 , pp. 237-240
    • Jakubowski, H.1    Goldman, E.2
  • 13
    • 0032778517 scopus 로고    scopus 로고
    • Protein homocysteinylation: possible mechanism underlying pathological consequences of elevated homocysteine levels
    • Jakubowski H. Protein homocysteinylation: possible mechanism underlying pathological consequences of elevated homocysteine levels. FASEB J. 1999, 13:2277-2283.
    • (1999) FASEB J. , vol.13 , pp. 2277-2283
    • Jakubowski, H.1
  • 14
    • 0033981289 scopus 로고    scopus 로고
    • Homocysteine thiolactone: metabolic origin and protein homocysteinylation in humans
    • Jakubowski H. Homocysteine thiolactone: metabolic origin and protein homocysteinylation in humans. J. Nutr. 2000, 130:377S-381S.
    • (2000) J. Nutr. , vol.130
    • Jakubowski, H.1
  • 15
    • 0031035742 scopus 로고    scopus 로고
    • Metabolism of homocysteine thiolactone in human cell cultures. Possible mechanism for pathological consequences of elevated homocysteine levels
    • Jakubowski H. Metabolism of homocysteine thiolactone in human cell cultures. Possible mechanism for pathological consequences of elevated homocysteine levels. J. Biol. Chem. 1997, 272:1935-1942.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1935-1942
    • Jakubowski, H.1
  • 16
    • 0034617073 scopus 로고    scopus 로고
    • Homocysteine thiolactone and protein homocysteinylation in human endothelial cells: implications for atherosclerosis
    • Jakubowski H., Zhang L., Bardeguez A., Aviv A. Homocysteine thiolactone and protein homocysteinylation in human endothelial cells: implications for atherosclerosis. Circ. Res. 2000, 87:45-51.
    • (2000) Circ. Res. , vol.87 , pp. 45-51
    • Jakubowski, H.1    Zhang, L.2    Bardeguez, A.3    Aviv, A.4
  • 17
    • 34249775796 scopus 로고    scopus 로고
    • Mutations in methylenetetrahydrofolate reductase or cystathionine beta-synthase gene, or a high-methionine diet, increase homocysteine thiolactone levels in humans and mice
    • Chwatko G., Boers G.H., Strauss K.A., Shih D.M., Jakubowski H. Mutations in methylenetetrahydrofolate reductase or cystathionine beta-synthase gene, or a high-methionine diet, increase homocysteine thiolactone levels in humans and mice. FASEB J. 2007, 21:1707-1713.
    • (2007) FASEB J. , vol.21 , pp. 1707-1713
    • Chwatko, G.1    Boers, G.H.2    Strauss, K.A.3    Shih, D.M.4    Jakubowski, H.5
  • 18
    • 57349180605 scopus 로고    scopus 로고
    • Mutations in cystathionine beta-synthase or methylenetetrahydrofolate reductase gene increase N-homocysteinylated protein levels in humans
    • Jakubowski H., Boers G.H., Strauss K.A. Mutations in cystathionine beta-synthase or methylenetetrahydrofolate reductase gene increase N-homocysteinylated protein levels in humans. FASEB J. 2008, 22:4071-4076.
    • (2008) FASEB J. , vol.22 , pp. 4071-4076
    • Jakubowski, H.1    Boers, G.H.2    Strauss, K.A.3
  • 19
    • 67649371083 scopus 로고    scopus 로고
    • Genetic or nutritional disorders in homocysteine or folate metabolism increase protein N-homocysteinylation in mice
    • Jakubowski H., Perla-Kajan J., Finnell R.H., Cabrera R.M., Wang H., Gupta S., et al. Genetic or nutritional disorders in homocysteine or folate metabolism increase protein N-homocysteinylation in mice. FASEB J. 2009, 23:1721-1727.
    • (2009) FASEB J. , vol.23 , pp. 1721-1727
    • Jakubowski, H.1    Perla-Kajan, J.2    Finnell, R.H.3    Cabrera, R.M.4    Wang, H.5    Gupta, S.6
  • 20
    • 0034802174 scopus 로고    scopus 로고
    • Protein N-homocysteinylation: implications for atherosclerosis
    • Jakubowski H. Protein N-homocysteinylation: implications for atherosclerosis. Biomed. Pharmacother. 2001, 55:443-447.
    • (2001) Biomed. Pharmacother. , vol.55 , pp. 443-447
    • Jakubowski, H.1
  • 21
    • 1542373560 scopus 로고    scopus 로고
    • Molecular basis of homocysteine toxicity in humans
    • Jakubowski H. Molecular basis of homocysteine toxicity in humans. Cell. Mol. Life Sci. 2004, 61:470-487.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 470-487
    • Jakubowski, H.1
  • 22
    • 33646788784 scopus 로고    scopus 로고
    • Pathophysiological consequences of homocysteine excess
    • Jakubowski H. Pathophysiological consequences of homocysteine excess. J. Nutr. 2006, 136:1741S-1749S.
    • (2006) J. Nutr. , vol.136
    • Jakubowski, H.1
  • 23
    • 36848998882 scopus 로고    scopus 로고
    • The molecular basis of homocysteine thiolactone-mediated vascular disease
    • Jakubowski H. The molecular basis of homocysteine thiolactone-mediated vascular disease. Clin. Chem. Lab. Med. 2007, 45:1704-1716.
    • (2007) Clin. Chem. Lab. Med. , vol.45 , pp. 1704-1716
    • Jakubowski, H.1
  • 24
    • 64049095638 scopus 로고    scopus 로고
    • The pathophysiological hypothesis of homocysteine thiolactone-mediated vascular disease
    • Jakubowski H. The pathophysiological hypothesis of homocysteine thiolactone-mediated vascular disease. J. Physiol. Pharmacol. 2008, 59:155-167.
    • (2008) J. Physiol. Pharmacol. , vol.59 , pp. 155-167
    • Jakubowski, H.1
  • 27
    • 2442641844 scopus 로고    scopus 로고
    • Cross-talk between Cys34 and lysine residues in human serum albumin revealed by N-homocysteinylation
    • Glowacki R., Jakubowski H. Cross-talk between Cys34 and lysine residues in human serum albumin revealed by N-homocysteinylation. J. Biol. Chem. 2004, 279:10864-10871.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10864-10871
    • Glowacki, R.1    Jakubowski, H.2
  • 28
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: amyloid pores from pathogenic mutations
    • Lashuel H.A., Hartley D., Petre B.M., Walz T., Lansbury P.T. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 2002, 418:291.
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury, P.T.5
  • 29
    • 40749146313 scopus 로고    scopus 로고
    • Multilevel structural nature and interactions of bovine serum albumin during heat-induced aggregation process
    • Rongxin S., Wei Q., Zhimin H., Yubin Z., Fengmin J. Multilevel structural nature and interactions of bovine serum albumin during heat-induced aggregation process. Food Hydrocolloids 2008, 22:995-1005.
    • (2008) Food Hydrocolloids , vol.22 , pp. 995-1005
    • Rongxin, S.1    Wei, Q.2    Zhimin, H.3    Yubin, Z.4    Fengmin, J.5
  • 30
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of helical and strand segment in proteins using CD spectroscopy
    • Sreerema N., Venyaminov S.Y., Woody R.W. Estimation of the number of helical and strand segment in proteins using CD spectroscopy. Protein Sci. 1999, 8:370-380.
    • (1999) Protein Sci. , vol.8 , pp. 370-380
    • Sreerema, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 31
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by congo red spectral shift assay
    • Klunk W.E., Jacob R.F., Mason R.P. Quantifying amyloid by congo red spectral shift assay. Methods Enzymol. 1999, 309:285-305.
    • (1999) Methods Enzymol. , vol.309 , pp. 285-305
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 33
    • 1642452936 scopus 로고    scopus 로고
    • Formation of amyloid fibrils from fully reduced hen egg white lysozyme
    • Aoneng C., Daoying H., Luhua L. Formation of amyloid fibrils from fully reduced hen egg white lysozyme. Protein Sci. 2004, 13:319-324.
    • (2004) Protein Sci. , vol.13 , pp. 319-324
    • Aoneng, C.1    Daoying, H.2    Luhua, L.3
  • 35
    • 2542618547 scopus 로고    scopus 로고
    • Autoantibodies against N-homocysteinylated proteins in humans: implications for atherosclerosis
    • Undas A., Perla J., Lacinski M., Trzeciak W., Kazmierski R., Jakubowski H. Autoantibodies against N-homocysteinylated proteins in humans: implications for atherosclerosis. Stroke 2004, 35:1299-1304.
    • (2004) Stroke , vol.35 , pp. 1299-1304
    • Undas, A.1    Perla, J.2    Lacinski, M.3    Trzeciak, W.4    Kazmierski, R.5    Jakubowski, H.6
  • 36
    • 0037163003 scopus 로고    scopus 로고
    • Homocysteine is a protein amino acid in humans. Implications for homocysteine-linked disease.
    • Jakubowski H. Homocysteine is a protein amino acid in humans. Implications for homocysteine-linked disease. J. Biol. Chem. 2002, 277:30425-30428.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30425-30428
    • Jakubowski, H.1
  • 37
    • 33748567808 scopus 로고    scopus 로고
    • Homocysteinylation of low-density lipoproteins (LDL) from subjects with Type 1 diabetes: effect on oxidative damage of human endothelial cells
    • Ferretti G., Bacchetti T., Rabini R.A., Vignini A., Nanetti L., Moroni C., Mazzanti L. Homocysteinylation of low-density lipoproteins (LDL) from subjects with Type 1 diabetes: effect on oxidative damage of human endothelial cells. Diabet. Med. 2006, 23:808-813.
    • (2006) Diabet. Med. , vol.23 , pp. 808-813
    • Ferretti, G.1    Bacchetti, T.2    Rabini, R.A.3    Vignini, A.4    Nanetti, L.5    Moroni, C.6    Mazzanti, L.7
  • 38
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
    • Conway K.A., Rochet J.C., Bieganski R.M., Lansbury P.T. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 2001, 294:1346-1349.
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury, P.T.4
  • 39
    • 0034614415 scopus 로고    scopus 로고
    • Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein
    • Okochi M., Walter J., Koyama A., Nakajo S., Baba M., Iwatsubo T., et al. Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein. J. Biol. Chem. 2000, 275:390-397.
    • (2000) J. Biol. Chem. , vol.275 , pp. 390-397
    • Okochi, M.1    Walter, J.2    Koyama, A.3    Nakajo, S.4    Baba, M.5    Iwatsubo, T.6
  • 40
    • 0037846441 scopus 로고    scopus 로고
    • Serine 776 of ataxin-1 is critical for polyglutamine-induced disease in SCA1 transgenic mice
    • Emamian E., Kaytor M., Duvick L., Zu T., Tousey S., Zoghbi H., et al. Serine 776 of ataxin-1 is critical for polyglutamine-induced disease in SCA1 transgenic mice. Neuron 2003, 38:375-387.
    • (2003) Neuron , vol.38 , pp. 375-387
    • Emamian, E.1    Kaytor, M.2    Duvick, L.3    Zu, T.4    Tousey, S.5    Zoghbi, H.6
  • 41
    • 0034602442 scopus 로고    scopus 로고
    • Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions
    • Giasson B.I., Duda J.E., Murray I.V., Chen Q., Souza J.M., Hurtig H.I., et al. Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions. Science 2000, 290:985-989.
    • (2000) Science , vol.290 , pp. 985-989
    • Giasson, B.I.1    Duda, J.E.2    Murray, I.V.3    Chen, Q.4    Souza, J.M.5    Hurtig, H.I.6
  • 43
    • 39549101751 scopus 로고    scopus 로고
    • Formaldehyde at low concentration induces protein tau into globular amyloid-like aggregates in vitro and in vivo
    • Nie C.L., Wei Y., Chen X., Liu Y.Y., Dui W., Liu Y., et al. Formaldehyde at low concentration induces protein tau into globular amyloid-like aggregates in vitro and in vivo. PLoS ONE 2007, 2:e629.
    • (2007) PLoS ONE , vol.2
    • Nie, C.L.1    Wei, Y.2    Chen, X.3    Liu, Y.Y.4    Dui, W.5    Liu, Y.6
  • 44
    • 63249093042 scopus 로고    scopus 로고
    • Rapid glycation with d-ribose induces globular amyloid-like aggregations of BSA with high cytotoxicity to SH-SY5Y cells
    • Wei Y., Chen L., Chen J., Ge L., He R.Q. Rapid glycation with d-ribose induces globular amyloid-like aggregations of BSA with high cytotoxicity to SH-SY5Y cells. BMC Cell Biol. 2009, 10:10.
    • (2009) BMC Cell Biol. , vol.10 , pp. 10
    • Wei, Y.1    Chen, L.2    Chen, J.3    Ge, L.4    He, R.Q.5
  • 45
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 47
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 49
    • 0029819081 scopus 로고    scopus 로고
    • Amyloid beta toxicity consists of a Ca(2+)-independent early phase and a Ca(2+)-dependent late phase
    • Abe K., Kimura H. Amyloid beta toxicity consists of a Ca(2+)-independent early phase and a Ca(2+)-dependent late phase. J. Neurochem. 1996, 67:2074-2078.
    • (1996) J. Neurochem. , vol.67 , pp. 2074-2078
    • Abe, K.1    Kimura, H.2


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