메뉴 건너뛰기




Volumn 289, Issue 6, 2014, Pages 3736-3748

Oxidation-induced structural changes of Ceruloplasmin Foster NGR Motif Deamidation That Promotes Integrin binding and signaling

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER DISEASE; CERULOPLASMIN; INTEGRINS; ISONGR MOTIF; NGR MOTIF; OXIDATIVE STRESS; PROTEIN DEAMIDATION; PROTEIN MISFOLDING; STRUCTURAL BIOLOGY;

EID: 84893667859     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.520981     Document Type: Article
Times cited : (27)

References (47)
  • 1
    • 38449123879 scopus 로고    scopus 로고
    • Chronoregulation by asparagine deamidation
    • Weintraub, S. J., and Deverman, B. E. (2007) Chronoregulation by asparagine deamidation. Sci. STKE 2007, re7
    • (2007) Sci. STKE , vol.2007
    • Weintraub, S.J.1    Deverman, B.E.2
  • 4
    • 0033926856 scopus 로고    scopus 로고
    • Increased methyl esterification of altered aspartyl residues in erythrocyte membrane proteins in response to oxidative stress
    • Ingrosso, D., D'Angelo, S., di Carlo, E., Perna, A. F., Zappia, V., and Galletti, P. (2000) Increased methyl esterification of altered aspartyl residues in erythrocyte membrane proteins in response to oxidative stress. Eur. J. Biochem. 267, 4397-4405
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4397-4405
    • Ingrosso, D.1    D'Angelo, S.2    Di Carlo, E.3    Perna, A.F.4    Zappia, V.5    Galletti, P.6
  • 5
    • 0036239339 scopus 로고    scopus 로고
    • Protein methylation as a marker of aspartate damage in glucose-6-phosphate dehydrogenase-deficient erythrocytes. Role of oxidative stress
    • Ingrosso, D., Cimmino, A., D'Angelo, S., Alfinito, F., Zappia, V., and Galletti, P. (2002) Protein methylation as a marker of aspartate damage in glucose-6-phosphate dehydrogenase-deficient erythrocytes. Role of oxidative stress. Eur. J. Biochem. 269, 2032-2039
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2032-2039
    • Ingrosso, D.1    Cimmino, A.2    D'Angelo, S.3    Alfinito, F.4    Zappia, V.5    Galletti, P.6
  • 6
    • 0033548661 scopus 로고    scopus 로고
    • Deamidation and isoaspartate formation in smeared tau in paired helical filaments. Unusual properties of the microtubule-binding domain of tau
    • Watanabe, A., Takio, K., and Ihara, Y. (1999) Deamidation and isoaspartate formation in smeared tau in paired helical filaments. Unusual properties of the microtubule-binding domain of tau. J. Biol. Chem. 274, 7368-7378
    • (1999) J. Biol. Chem. , vol.274 , pp. 7368-7378
    • Watanabe, A.1    Takio, K.2    Ihara, Y.3
  • 7
    • 24944532072 scopus 로고    scopus 로고
    • Biological significance of isoaspartate and its repair system
    • Shimizu, T., Matsuoka, Y., and Shirasawa, T. (2005) Biological significance of isoaspartate and its repair system. Biol. Pharm. Bull. 28, 1590-1596
    • (2005) Biol. Pharm. Bull. , vol.28 , pp. 1590-1596
    • Shimizu, T.1    Matsuoka, Y.2    Shirasawa, T.3
  • 8
    • 0026787130 scopus 로고
    • Protein sequence and mass spectrometric analyses of tau in the alzheimer's disease brain
    • Hasegawa, M., Morishima-Kawashima, M., Takio, K., Suzuki, M., Titani, K., and Ihara, Y. (1992) Protein sequence and mass spectrometric analyses of Tau in the Alzheimer's disease brain. J. Biol. Chem. 267, 17047-17054
    • (1992) J. Biol. Chem. , vol.267 , pp. 17047-17054
    • Hasegawa, M.1    Morishima-Kawashima, M.2    Takio, K.3    Suzuki, M.4    Titani, K.5    Ihara, Y.6
  • 14
    • 79951839235 scopus 로고    scopus 로고
    • Isoaspartate-dependent molecular switches for integrin-ligand recognition
    • Corti, A., and Curnis, F. (2011) Isoaspartate-dependent molecular switches for integrin-ligand recognition. J. Cell Sci. 124, 515-522
    • (2011) J. Cell Sci. , vol.124 , pp. 515-522
    • Corti, A.1    Curnis, F.2
  • 15
    • 0036400025 scopus 로고    scopus 로고
    • Ceruloplasmin metabolism and function
    • Hellman, N. E., and Gitlin, J. D. (2002) Ceruloplasmin metabolism and function. Annu. Rev. Nutr. 22, 439-458
    • (2002) Annu. Rev. Nutr. , vol.22 , pp. 439-458
    • Hellman, N.E.1    Gitlin, J.D.2
  • 16
    • 84879585295 scopus 로고    scopus 로고
    • Multi-copper oxidases and human iron metabolism
    • Vashchenko, G., and MacGillivray, R. T. (2013) Multi-copper oxidases and human iron metabolism. Nutrients 5, 2289-2313
    • (2013) Nutrients , vol.5 , pp. 2289-2313
    • Vashchenko, G.1    MacGillivray, R.T.2
  • 18
    • 78650142376 scopus 로고    scopus 로고
    • Protein oxidative modifications in the ageing brain. Consequence for the onset of neurodegenerative disease
    • Grimm, S., Hoehn, A., Davies, K. J., and Grune, T. (2011) Protein oxidative modifications in the ageing brain. Consequence for the onset of neurodegenerative disease. Free Radic. Res. 45, 73-88
    • (2011) Free Radic. Res. , vol.45 , pp. 73-88
    • Grimm, S.1    Hoehn, A.2    Davies, K.J.3    Grune, T.4
  • 20
    • 0021271971 scopus 로고
    • Clinical diagnosis of alzheimer's disease
    • Report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease.
    • McKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D., and Stadlan, E. M. (1984) Clinical diagnosis of Alzheimer's disease. Report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease. Neurology 34, 939-944
    • (1984) Neurology , vol.34 , pp. 939-944
    • McKhann, G.1    Drachman, D.2    Folstein, M.3    Katzman, R.4    Price, D.5    Stadlan, E.M.6
  • 21
    • 39449115394 scopus 로고    scopus 로고
    • I-tasser server for protein 3d structure prediction
    • Zhang, Y. (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9, 40
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 22
    • 46249092554 scopus 로고    scopus 로고
    • Gromacs 4. Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., Kutzner, C., van der Spoel, D., and Lindahl, E. (2008) GROMACS 4. Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 25
    • 33846678076 scopus 로고    scopus 로고
    • Ceruloplasmin revisited. Structural and functional roles of various metal cationbinding sites
    • Bento, I., Peixoto, C., Zaitsev, V. N., and Lindley, P. F. (2007) Ceruloplasmin revisited. Structural and functional roles of various metal cationbinding sites. Acta Crystallogr. D Biol. Crystallogr. 63, 240-248
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 240-248
    • Bento, I.1    Peixoto, C.2    Zaitsev, V.N.3    Lindley, P.F.4
  • 26
    • 0027373145 scopus 로고
    • Age-related changes in human ceruloplasmin. Evidence for oxidative modifications
    • Musci, G., Bonaccorsi di Patti, M. C., Fagiolo, U., and Calabrese, L. (1993) Age-related changes in human ceruloplasmin. Evidence for oxidative modifications. J. Biol. Chem. 268, 13388-13395
    • (1993) J. Biol. Chem. , vol.268 , pp. 13388-13395
    • Musci, G.1    Bonaccorsi Di Patti, M.C.2    Fagiolo, U.3    Calabrese, L.4
  • 27
    • 0035824113 scopus 로고    scopus 로고
    • Oxidative modification of human ceruloplasmin by peroxyl radicals
    • Kang, J. H., Kim, K. S., Choi, S. Y., Kwon, H. Y., and Won, M. H. (2001) Oxidative modification of human ceruloplasmin by peroxyl radicals. Biochim. Biophys. Acta 1568, 30-36
    • (2001) Biochim. Biophys. Acta , vol.1568 , pp. 30-36
    • Kang, J.H.1    Kim, K.S.2    Choi, S.Y.3    Kwon, H.Y.4    Won, M.H.5
  • 28
    • 38949166834 scopus 로고    scopus 로고
    • Role of copper in thermal stability of human ceruloplasmin
    • Sedlák, E., Zoldák, G., and Wittung-Stafshede, P. (2008) Role of copper in thermal stability of human ceruloplasmin. Biophys. J. 94, 1384-1391
    • (2008) Biophys. J. , vol.94 , pp. 1384-1391
    • Sedlák, E.1    Zoldák, G.2    Wittung-Stafshede, P.3
  • 29
    • 84864067477 scopus 로고    scopus 로고
    • A mechanism-based kinetic analysis of succinimide-mediated deamidation, racemization, and covalent adduct formation in a model peptide in amorphous lyophiles
    • Dehart, M. P., and Anderson, B. D. (2012) A mechanism-based kinetic analysis of succinimide-mediated deamidation, racemization, and covalent adduct formation in a model peptide in amorphous lyophiles. J. Pharm. Sci. 101, 3096-3109
    • (2012) J. Pharm. Sci. , vol.101 , pp. 3096-3109
    • Dehart, M.P.1    Anderson, B.D.2
  • 30
    • 33845918167 scopus 로고    scopus 로고
    • Protein repair in the brain, proteomic analysis of endogenous substrates for protein l-isoaspartyl methyltransferase in mouse brain
    • Zhu, J. X., Doyle, H. A., Mamula, M. J., and Aswad, D. W. (2006) Protein repair in the brain, proteomic analysis of endogenous substrates for protein L-isoaspartyl methyltransferase in mouse brain. J. Biol. Chem. 281, 33802-33813
    • (2006) J. Biol. Chem. , vol.281 , pp. 33802-33813
    • Zhu, J.X.1    Doyle, H.A.2    Mamula, M.J.3    Aswad, D.W.4
  • 31
    • 59149084006 scopus 로고    scopus 로고
    • Ceruloplasmin in neurodegenerative diseases
    • Texel, S. J., Xu, X., and Harris, Z. L. (2008) Ceruloplasmin in neurodegenerative diseases. Biochem. Soc. Trans. 36, 1277-1281
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1277-1281
    • Texel, S.J.1    Xu, X.2    Harris, Z.L.3
  • 33
    • 0242363670 scopus 로고    scopus 로고
    • Molecular pathways of neurodegeneration in parkinson's disease
    • Dawson, T. M., and Dawson, V. L. (2003) Molecular pathways of neurodegeneration in Parkinson's disease. Science 302, 819-822
    • (2003) Science , Issue.302 , pp. 819-822
    • Dawson, T.M.1    Dawson, V.2
  • 35
    • 77049115153 scopus 로고    scopus 로고
    • Clinical utility of copper, ceruloplasmin, and metallothionein plasma determinations in human neurodegenerative patients and their first-degree relatives
    • Arnal, N., Cristalli, D. O., de Alaniz, M. J., and Marra, C. A. (2010) Clinical utility of copper, ceruloplasmin, and metallothionein plasma determinations in human neurodegenerative patients and their first-degree relatives. Brain Res. 1319, 118-130
    • (2010) Brain Res. , vol.1319 , pp. 118-130
    • Arnal, N.1    Cristalli, D.O.2    De Alaniz, M.J.3    Marra, C.A.4
  • 37
    • 84865127699 scopus 로고    scopus 로고
    • Copper and oxidative stress in the pathogenesis of alzheimer's disease
    • Eskici, G., and Axelsen, P. H. (2012) Copper and oxidative stress in the pathogenesis of Alzheimer's disease. Biochemistry 51, 6289-6311
    • (2012) Biochemistry , vol.51 , pp. 6289-6311
    • Eskici, G.1    Axelsen, P.H.2
  • 38
    • 0036703490 scopus 로고    scopus 로고
    • Ceruloplasmin regulates iron levels in the cns and prevents free radical injury
    • Patel, B. N., Dunn, R. J., Jeong, S. Y., Zhu, Q., Julien, J. P., and David, S. (2002) Ceruloplasmin regulates iron levels in the CNS and prevents free radical injury. J. Neurosci. 22, 6578-6586
    • (2002) J. Neurosci. , vol.22 , pp. 6578-6586
    • Patel, B.N.1    Dunn, R.J.2    Jeong, S.Y.3    Zhu, Q.4    Julien, J.P.5    David, S.6
  • 39
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • Luo, B. H., Carman, C. V., and Springer, T. A. (2007) Structural basis of integrin regulation and signaling. Annu. Rev. Immunol. 25, 619-647
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 619-647
    • Luo, B.H.1    Carman, C.V.2    Springer, T.3
  • 40
    • 0037439642 scopus 로고    scopus 로고
    • Aberrant activation of focal adhesion proteins mediates fibrillar amyloid-induced neuronal dystrophy
    • Grace, E. A., and Busciglio, J. (2003) Aberrant activation of focal adhesion proteins mediates fibrillar amyloid-induced neuronal dystrophy. J. Neurosci. 23, 493-502
    • (2003) J. Neurosci. , vol.23 , pp. 493-502
    • Grace, E.A.1    Busciglio, J.2
  • 42
    • 33947164895 scopus 로고    scopus 로고
    • Focal adhesions regulatea-signaling and cell death in alzheimer's disease
    • Caltagarone, J., Jing, Z., and Bowser, R. (2007) Focal adhesions regulateA-signaling and cell death in Alzheimer's disease. Biochim. Biophys. Acta 1772, 438-445
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 438-445
    • Caltagarone, J.1    Jing, Z.2    Bowser, R.3
  • 43
    • 77950363010 scopus 로고    scopus 로고
    • Mechanisms underlying inflammation in neurodegeneration
    • Glass, C. K., Saijo, K., Winner, B., Marchetto, M. C., and Gage, F. H. (2010) Mechanisms underlying inflammation in neurodegeneration. Cell 140, 918-934
    • (2010) Cell , vol.140 , pp. 918-934
    • Glass, C.K.1    Saijo, K.2    Winner, B.3    Marchetto, M.C.4    Gage, F.H.5
  • 44
    • 34548623301 scopus 로고    scopus 로고
    • Activation of microglial cells by ceruloplasmin
    • Lee, K. H., Yun, S. J., Nam, K. N., Gho, Y. S., and Lee, E. H. (2007) Activation of microglial cells by ceruloplasmin. Brain Res. 1171, 1-8
    • (2007) Brain Res. , vol.1171 , pp. 1-8
    • Lee, K.H.1    Yun, S.J.2    Nam, K.N.3    Gho, Y.S.4    Lee, E.H.5
  • 45
    • 69949118812 scopus 로고    scopus 로고
    • Oxidative stress damage and oxidative stress responses in the choroid plexus in alzheimer's disease
    • Perez-Gracia, E., Blanco, R., Carmona, M., Carro, E., and Ferrer, I. (2009) Oxidative stress damage and oxidative stress responses in the choroid plexus in Alzheimer's disease. Acta Neuropathol. 118, 497-504
    • (2009) Acta Neuropathol. , vol.118 , pp. 497-504
    • Perez-Gracia, E.1    Blanco, R.2    Carmona, M.3    Carro, E.4    Ferrer, I.5
  • 46
    • 84865988805 scopus 로고    scopus 로고
    • Pathological alteration in the choroid plexus of alzheimer's disease. Implication for new therapy approaches
    • Krzyzanowska, A., and Carro, E. (2012) Pathological alteration in the choroid plexus of Alzheimer's disease. Implication for new therapy approaches. Front. Pharmacol. 3, 75
    • (2012) Front. Pharmacol. , vol.3 , pp. 75
    • Krzyzanowska, A.1    Carro, E.2
  • 47
    • 84861497648 scopus 로고    scopus 로고
    • A possible role for csf turnover and choroid plexus in the pathogenesis of late onset alzheimer disease
    • Serot, J. M., Zmudka, J., and Jouanny, P. (2012) A possible role for CSF turnover and choroid plexus in the pathogenesis of late onset Alzheimer disease. J. Alzheimers Dis. 30, 17-26
    • (2012) J. Alzheimers Dis. , vol.30 , pp. 17-26
    • Serot, J.M.1    Zmudka, J.2    Jouanny, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.