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Volumn 5, Issue 6, 2008, Pages 562-571

Disease state, age, sex, and post-mortem time-dependent expression of proteins in AD vs. control frontal cortex brain samples

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; ASPARTATE AMINOTRANSFERASE; BCL 2 ASSOCIATED TRANSCRIPTION FACTOR 1; BRAIN PROTEIN; DIHYDROPYRIMIDASE RELATED PROTEIN 2; FRUCTOSE BISPHOSPHATE ALDOLASE; FRUCTOSE BISPHOSPHATE ALDOLASE A; HEAT SHOCK PROTEIN 70; HEMOGLOBIN; METHYLMALONATE SEMIALDEHYDE DEHYDROGENASE (ACYLATING); NEUROFILAMENT M PROTEIN; PROTEIN NIPSNAP2; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UBIQUITIN THIOLESTERASE; UNCLASSIFIED DRUG; UNIQUITIN CARBOXYL TERMINAL HYDROLASE ISOZYME L1;

EID: 58049221284     PISSN: 15672050     EISSN: None     Source Type: Journal    
DOI: 10.2174/156720508786898488     Document Type: Article
Times cited : (21)

References (42)
  • 1
    • 0035656206 scopus 로고    scopus 로고
    • Proteomic analysis of the brain in Alzheimer's disease: Molecular phenotype of a complex disease process
    • Schonberger SJ, Edgar PF, Kydd R, Faull RL and Cooper GJ. Proteomic analysis of the brain in Alzheimer's disease: molecular phenotype of a complex disease process. Proteomics 1: 1519-1528 (2001).
    • (2001) Proteomics , vol.1 , pp. 1519-1528
    • Schonberger, S.J.1    Edgar, P.F.2    Kydd, R.3    Faull, R.L.4    Cooper, G.J.5
  • 4
    • 4344570364 scopus 로고    scopus 로고
    • Proteomic characterization of postmortem amyloid plaques isolated by laser capture microdissection
    • Liao L, Cheng D, Wang J, Duong DM, Losik TG, Gearing M, et al. Proteomic characterization of postmortem amyloid plaques isolated by laser capture microdissection. J Biol Chem 279: 37061-37068 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 37061-37068
    • Liao, L.1    Cheng, D.2    Wang, J.3    Duong, D.M.4    Losik, T.G.5    Gearing, M.6
  • 5
    • 41549129862 scopus 로고    scopus 로고
    • Assessing quantitative post-mortem changes in the gray matter of the human frontal cortex proteome by 2-D DIGE
    • Crecelius A, Gotz A, Arzberger T, Frohlich T, Arnold GJ, Ferrer I, et al. Assessing quantitative post-mortem changes in the gray matter of the human frontal cortex proteome by 2-D DIGE. Proteomics 8: 1276-1291 (2008).
    • (2008) Proteomics , vol.8 , pp. 1276-1291
    • Crecelius, A.1    Gotz, A.2    Arzberger, T.3    Frohlich, T.4    Arnold, G.J.5    Ferrer, I.6
  • 6
    • 33846110316 scopus 로고    scopus 로고
    • Brain protein preservation largely depends on the postmortem storage temperature: Implications for study of proteins in human neurologic diseases and management of brain banks: a BrainNet Europe Study
    • Ferrer I, Santpere G, Arzberger T, Bell J, Blanco R, Boluda S, et al. Brain protein preservation largely depends on the postmortem storage temperature: implications for study of proteins in human neurologic diseases and management of brain banks: a BrainNet Europe Study. J Neuropathol Exp Neurol 66: 35-46 (2007).
    • (2007) J Neuropathol Exp Neurol , vol.66 , pp. 35-46
    • Ferrer, I.1    Santpere, G.2    Arzberger, T.3    Bell, J.4    Blanco, R.5    Boluda, S.6
  • 7
    • 0142244521 scopus 로고    scopus 로고
    • Dihydropyrimidinase related protein-2 as a biomarker for temperature and time dependent post mortem changes in the mouse brain proteome
    • Franzen B, Yang Y, Sunnemark D, Wickman M, Ottervald J, Oppermann M, et al. Dihydropyrimidinase related protein-2 as a biomarker for temperature and time dependent post mortem changes in the mouse brain proteome. Proteomics 3: 1920-1929 (2003).
    • (2003) Proteomics , vol.3 , pp. 1920-1929
    • Franzen, B.1    Yang, Y.2    Sunnemark, D.3    Wickman, M.4    Ottervald, J.5    Oppermann, M.6
  • 8
    • 0030071040 scopus 로고    scopus 로고
    • Effects of postmortem interval, age, and Alzheimer's disease on G-proteins in human brain
    • Li X, Greenwood AF, Powers R and Jope RS. Effects of postmortem interval, age, and Alzheimer's disease on G-proteins in human brain. Neurobiol Aging 17: 115-122 (1996).
    • (1996) Neurobiol Aging , vol.17 , pp. 115-122
    • Li, X.1    Greenwood, A.F.2    Powers, R.3    Jope, R.S.4
  • 9
    • 0042343867 scopus 로고    scopus 로고
    • Post-mortem interval effects on the phosphorylation of signaling proteins
    • Li J, Gould TD, Yuan P, Manji HK and Chen G. Post-mortem interval effects on the phosphorylation of signaling proteins. Neuropsychopharmacology 28: 1017-1025 (2003).
    • (2003) Neuropsychopharmacology , vol.28 , pp. 1017-1025
    • Li, J.1    Gould, T.D.2    Yuan, P.3    Manji, H.K.4    Chen, G.5
  • 10
    • 0028989692 scopus 로고
    • Synaptophysin immunoreactivity is stable 36 h postmortem
    • Liu X and Brun A. Synaptophysin immunoreactivity is stable 36 h postmortem. Dementia 6: 211-217 (1995).
    • (1995) Dementia , vol.6 , pp. 211-217
    • Liu, X.1    Brun, A.2
  • 11
    • 0027981303 scopus 로고
    • Postmortem changes in the levels and localization of microtubule-associated proteins (tau, MAP2 and MAP1B) in the rat and human hippocampus
    • Schwab C, Bondada V, Sparks DL, Cahan LD and Geddes JW. Postmortem changes in the levels and localization of microtubule-associated proteins (tau, MAP2 and MAP1B) in the rat and human hippocampus. Hippocampus 4: 210-225 (1994).
    • (1994) Hippocampus , vol.4 , pp. 210-225
    • Schwab, C.1    Bondada, V.2    Sparks, D.L.3    Cahan, L.D.4    Geddes, J.W.5
  • 12
    • 5644235607 scopus 로고    scopus 로고
    • Measurement of pre- and post-synaptic proteins in cerebral cortex: Effects of post-mortem delay
    • Siew LK, Love S, Dawbarn D, Wilcock GK and Allen SJ. Measurement of pre- and post-synaptic proteins in cerebral cortex: effects of post-mortem delay. J Neurosci Methods 139: 153-159 (2004).
    • (2004) J Neurosci Methods , vol.139 , pp. 153-159
    • Siew, L.K.1    Love, S.2    Dawbarn, D.3    Wilcock, G.K.4    Allen, S.J.5
  • 13
    • 0030926318 scopus 로고    scopus 로고
    • The effect of postmortem delay on the distribution of microtubule-associated proteins tau, MAP2, and MAP5 in the rat
    • Irving EA, McCulloch J and Dewar D. The effect of postmortem delay on the distribution of microtubule-associated proteins tau, MAP2, and MAP5 in the rat. Mol Chem Neuropathol 30: 253-271 (1997).
    • (1997) Mol Chem Neuropathol , vol.30 , pp. 253-271
    • Irving, E.A.1    McCulloch, J.2    Dewar, D.3
  • 14
    • 0030586896 scopus 로고    scopus 로고
    • Involvement of calpain in postmortem proteolysis in the rat brain
    • Sorimachi Y, Harada K and Yoshida K. Involvement of calpain in postmortem proteolysis in the rat brain. Forensic Sci Int 81: 165-174 (1996).
    • (1996) Forensic Sci Int , vol.81 , pp. 165-174
    • Sorimachi, Y.1    Harada, K.2    Yoshida, K.3
  • 15
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak H and Braak E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol 82: 239-259 (1991).
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 16
    • 0025908356 scopus 로고
    • The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease
    • Mirra SS, Heyman A, McKeel D, Sumi SM, Crain BJ, Brownlee LM, et al. The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease. Neurology 41: 479-486 (1991).
    • (1991) Neurology , vol.41 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3    Sumi, S.M.4    Crain, B.J.5    Brownlee, L.M.6
  • 17
    • 0029020259 scopus 로고
    • Two-dimensional electrophoresis of proteins: An updated protocol and implications for a functional analysis of the genome
    • Klose J and Kobalz U. Two-dimensional electrophoresis of proteins: an updated protocol and implications for a functional analysis of the genome. Electrophoresis 16: 1034-1059 (1995).
    • (1995) Electrophoresis , vol.16 , pp. 1034-1059
    • Klose, J.1    Kobalz, U.2
  • 18
    • 33749239065 scopus 로고    scopus 로고
    • Pilot study of the human proteome organisation brain proteome project: Applying different 2-DE techniques to monitor proteomic changes during murine brain development
    • Stuhler K, Pfeiffer K, Joppich C, Stephan C, Jung K, Muller M, et al. Pilot study of the human proteome organisation brain proteome project: Applying different 2-DE techniques to monitor proteomic changes during murine brain development. Proteomics 6: 4899-4913 (2006).
    • (2006) Proteomics , vol.6 , pp. 4899-4913
    • Stuhler, K.1    Pfeiffer, K.2    Joppich, C.3    Stephan, C.4    Jung, K.5    Muller, M.6
  • 19
    • 0021988172 scopus 로고
    • Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining
    • Heukeshoven J and Dernick R. Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining. Electrophoresis 6: 103-112 (1985).
    • (1985) Electrophoresis , vol.6 , pp. 103-112
    • Heukeshoven, J.1    Dernick, R.2
  • 21
    • 0345822598 scopus 로고    scopus 로고
    • The positive false discovery rate: A bayesian interpretation and the q-value
    • Storey JD. The positive false discovery rate: a bayesian interpretation and the q-value. Ann Appl Stat 31: 2013-2035 (2003).
    • (2003) Ann Appl Stat , vol.31 , pp. 2013-2035
    • Storey, J.D.1
  • 22
    • 0033847019 scopus 로고    scopus 로고
    • Identification of platelet proteins separated by two-dimensional gel electrophoresis and analyzed by matrix assisted laser desorption/ionization-time of flight-mass spectrometry and detection of tyrosine-phosphorylated proteins
    • Marcus K, Immler D, Sternberger J and Meyer HE. Identification of platelet proteins separated by two-dimensional gel electrophoresis and analyzed by matrix assisted laser desorption/ionization-time of flight-mass spectrometry and detection of tyrosine-phosphorylated proteins. Electrophoresis 21: 2622-2636 (2000).
    • (2000) Electrophoresis , vol.21 , pp. 2622-2636
    • Marcus, K.1    Immler, D.2    Sternberger, J.3    Meyer, H.E.4
  • 23
    • 33846590619 scopus 로고    scopus 로고
    • Multidimensional chromatography: A powerful tool for the analysis of membrane proteins in mouse brain
    • Lohaus C, Nolte A, Bluggel M, Scheer C, Klose J, Gobom J, et al. Multidimensional chromatography: a powerful tool for the analysis of membrane proteins in mouse brain. J Proteome Res 6: 105-113 (2007).
    • (2007) J Proteome Res , vol.6 , pp. 105-113
    • Lohaus, C.1    Nolte, A.2    Bluggel, M.3    Scheer, C.4    Klose, J.5    Gobom, J.6
  • 24
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data 1
    • Perkins DN, Pappin DJ, Creasy DM and Cottrell JS. Probability-based protein identification by searching sequence databases using mass spectrometry data 1. Electrophoresis 20: 3551-3567 (1999).
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 25
    • 0037459791 scopus 로고    scopus 로고
    • Association of ATP synthase alpha-chain with neurofibrillary degeneration in Alzheimer's disease
    • Sergeant N, Wattez A, Galvan-valencia M, Ghestem A, David JP, Lemoine J, et al. Association of ATP synthase alpha-chain with neurofibrillary degeneration in Alzheimer's disease. Neuroscience 117: 293-303 (2003).
    • (2003) Neuroscience , vol.117 , pp. 293-303
    • Sergeant, N.1    Wattez, A.2    Galvan-valencia, M.3    Ghestem, A.4    David, J.P.5    Lemoine, J.6
  • 27
    • 41949104908 scopus 로고    scopus 로고
    • Cholinergic neuronal and axonal abnormalities are present early in aging and in Alzheimer disease
    • Geula C, Nagykery N, Nicholas A and Wu CK. Cholinergic neuronal and axonal abnormalities are present early in aging and in Alzheimer disease. J Neuropathol Exp Neurol 67: 309-18 (2008).
    • (2008) J Neuropathol Exp Neurol , vol.67 , pp. 309-318
    • Geula, C.1    Nagykery, N.2    Nicholas, A.3    Wu, C.K.4
  • 28
    • 0027511796 scopus 로고
    • Heterogeneity and selectivity of the degeneration of cholinergic neurons in the basal forebrain of patients with Alzheimer's disease
    • Lehericy S, Hirsch EC, Cervera-Pierot P, Hersh LB, Bakchine S, Piette F, et al. Heterogeneity and selectivity of the degeneration of cholinergic neurons in the basal forebrain of patients with Alzheimer's disease. J Comp Neurol 330: 15-31 (1993).
    • (1993) J Comp Neurol , vol.330 , pp. 15-31
    • Lehericy, S.1    Hirsch, E.C.2    Cervera-Pierot, P.3    Hersh, L.B.4    Bakchine, S.5    Piette, F.6
  • 29
    • 0035704857 scopus 로고    scopus 로고
    • Selective loss of KGDHC-enriched neurons in Alzheimer temporal cortex: Does mitochondrial variation contribute to selective vulnerability?
    • Ko LW, Sheu KF, Thaler HT, Markesbery WR and Blass JP. Selective loss of KGDHC-enriched neurons in Alzheimer temporal cortex: does mitochondrial variation contribute to selective vulnerability? J Mol Neurosci 17: 361-369 (2001).
    • (2001) J Mol Neurosci , vol.17 , pp. 361-369
    • Ko, L.W.1    Sheu, K.F.2    Thaler, H.T.3    Markesbery, W.R.4    Blass, J.P.5
  • 30
    • 0034074582 scopus 로고    scopus 로고
    • Effects of aluminum on activity of krebs cycle enzymes and glutamate dehydrogenase in rat brain homogenate
    • Zatta P, Lain E and Cagnolini C. Effects of aluminum on activity of krebs cycle enzymes and glutamate dehydrogenase in rat brain homogenate. Eur J Biochem 267: 3049-3055 (2000).
    • (2000) Eur J Biochem , vol.267 , pp. 3049-3055
    • Zatta, P.1    Lain, E.2    Cagnolini, C.3
  • 32
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: Dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71
    • Castegna A, Aksenov M, Thongboonkerd V, Klein JB, Pierce WM, Booze R, et al. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71. J Neurochem 82: 1524-1532 (2002).
    • (2002) J Neurochem , vol.82 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3    Klein, J.B.4    Pierce, W.M.5    Booze, R.6
  • 33
    • 36849001303 scopus 로고    scopus 로고
    • The role of ubiquitin C-terminal hydrolase L1 in neurodegenerative disorders 1
    • Gong B and Leznik E. The role of ubiquitin C-terminal hydrolase L1 in neurodegenerative disorders 1. Drug News Perspect 20: 365-370 (2007).
    • (2007) Drug News Perspect , vol.20 , pp. 365-370
    • Gong, B.1    Leznik, E.2
  • 34
    • 0030976363 scopus 로고    scopus 로고
    • Risk of Alzheimer's disease among elderly patients with anemia: Population-based investigations in Olmsted County, Minnesota
    • Beard CM, Kokmen E, O'Brien PC, Ania BJ and Melton LJ, III. Risk of Alzheimer's disease among elderly patients with anemia: population-based investigations in Olmsted County, Minnesota. Ann Epidemiol 7: 219-224 (1997).
    • (1997) Ann Epidemiol , vol.7 , pp. 219-224
    • Beard, C.M.1    Kokmen, E.2    O'Brien, P.C.3    Ania, B.J.4    Melton III, L.J.5
  • 37
    • 0032585829 scopus 로고    scopus 로고
    • Heat-shock protein 70 levels in brain of patients with down syndrome and Alzheimer's disease
    • Yoo BC, Seidl R, Cairns N and Lubec G. Heat-shock protein 70 levels in brain of patients with down syndrome and Alzheimer's disease. J Neural Transm Suppl 57: 315-322 (1999).
    • (1999) J Neural Transm , Issue.SUPPL. 57 , pp. 315-322
    • Yoo, B.C.1    Seidl, R.2    Cairns, N.3    Lubec, G.4
  • 38
    • 3142718813 scopus 로고    scopus 로고
    • Gene expression profiling in fetal, aged, and Alzheimer hippocampus: A continuum of stress-related signaling
    • Lukiw WJ. Gene expression profiling in fetal, aged, and Alzheimer hippocampus: a continuum of stress-related signaling. Neurochem Res 29: 1287-1297 (2004).
    • (2004) Neurochem Res , vol.29 , pp. 1287-1297
    • Lukiw, W.J.1
  • 39
    • 0028819856 scopus 로고
    • Heat shock protein 70 mRNA levels in mononuclear blood cells from patients with dementia of the Alzheimer type
    • Wakutani Y, Urakami K, Shimomura T and Takahashi K. Heat shock protein 70 mRNA levels in mononuclear blood cells from patients with dementia of the Alzheimer type. Dementia 6: 301-305 (1995).
    • (1995) Dementia , vol.6 , pp. 301-305
    • Wakutani, Y.1    Urakami, K.2    Shimomura, T.3    Takahashi, K.4
  • 40
    • 0038644221 scopus 로고    scopus 로고
    • The regulation of glucose metabolism by HIF-1 mediates a neuroprotective response to amyloid beta peptide
    • Soucek T, Cumming R, Dargusch R, Maher P and Schubert D. The regulation of glucose metabolism by HIF-1 mediates a neuroprotective response to amyloid beta peptide. Neuron 39: 43-56 (2003).
    • (2003) Neuron , vol.39 , pp. 43-56
    • Soucek, T.1    Cumming, R.2    Dargusch, R.3    Maher, P.4    Schubert, D.5
  • 41
    • 33947521347 scopus 로고    scopus 로고
    • In vitro assay of neurofilament light chain self-assembly using truncated mutants
    • Kim SK, Cho SM, Lee IB, Lee YH, Kang JH, Choi JH, et al. In vitro assay of neurofilament light chain self-assembly using truncated mutants. J Neurosci Methods 161: 199-204 (2007).
    • (2007) J Neurosci Methods , vol.161 , pp. 199-204
    • Kim, S.K.1    Cho, S.M.2    Lee, I.B.3    Lee, Y.H.4    Kang, J.H.5    Choi, J.H.6
  • 42
    • 0035914046 scopus 로고    scopus 로고
    • Hyperphosphorylation and accumulation of neurofilament proteins in Alzheimer disease brain and in okadaic acid-treated SY5Y cells
    • Wang J, Tung YC, Wang Y, Li XT, Iqbal K, Grundke-Iqbal I, et al. Hyperphosphorylation and accumulation of neurofilament proteins in Alzheimer disease brain and in okadaic acid-treated SY5Y cells. FEBS Lett 507: 81-87 (2001).
    • (2001) FEBS Lett , vol.507 , pp. 81-87
    • Wang, J.1    Tung, Y.C.2    Wang, Y.3    Li, X.T.4    Iqbal, K.5    Grundke-Iqbal, I.6


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