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Volumn 15, Issue 2-3, 2015, Pages 508-519

Quantitative phosphoproteomics of Alzheimer's disease reveals cross-talk between kinases and small heat shock proteins

Author keywords

IMAC; MS; Neurodegeneration; Proteostasis; Systems biology

Indexed keywords

ALPHA CRYSTALLIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 27; PHOSPHOPEPTIDE; PROTEIN KINASE; SMALL HEAT SHOCK PROTEIN; TAU PROTEIN;

EID: 84921366995     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201400189     Document Type: Article
Times cited : (64)

References (45)
  • 1
    • 0020617012 scopus 로고
    • Protein phosphorylation in the brain
    • Nestler, E. J., Greengard, P., Protein phosphorylation in the brain. Nature 1983, 305, 583-588.
    • (1983) Nature , vol.305 , pp. 583-588
    • Nestler, E.J.1    Greengard, P.2
  • 2
    • 0034797512 scopus 로고    scopus 로고
    • The role of protein phosphorylation in human health and disease
    • Cohen, P., The role of protein phosphorylation in human health and disease. Eur. J. Biochem. 2001, 268, 5001-5010.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5001-5010
    • Cohen, P.1
  • 5
    • 0036434880 scopus 로고    scopus 로고
    • Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer's disease
    • Ghoshal, N., García-Sierra, F., Wuu, J., Leurgans, S. et al., Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer's disease. Exp. Neurol. 2002, 177, 475-493.
    • (2002) Exp. Neurol. , vol.177 , pp. 475-493
    • Ghoshal, N.1    García-Sierra, F.2    Wuu, J.3    Leurgans, S.4
  • 6
    • 34548036227 scopus 로고    scopus 로고
    • Tau-mediated neurodegeneration in Alzheimer's disease and related disorders
    • Ballatore, C., Lee, V. M. Y., Trojanowski, J. Q., Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat. Rev. Neurosci. 2007, 8, 663-672.
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 663-672
    • Ballatore, C.1    Lee, V.M.Y.2    Trojanowski, J.Q.3
  • 8
    • 0028003725 scopus 로고
    • Microtubule-associated protein MAP1B showing a fetal phosphorylation pattern is present in sites of neurofibrillary degeneration in brains of Alzheimer's disease patients
    • Ulloa, L., Montejo de Garcini, E., Gomez-Ramos, P., Moran, M. A., Avila, J., Microtubule-associated protein MAP1B showing a fetal phosphorylation pattern is present in sites of neurofibrillary degeneration in brains of Alzheimer's disease patients. Brain Res. 1994, 26, 113-122.
    • (1994) Brain Res. , vol.26 , pp. 113-122
    • Ulloa, L.1    Montejo de Garcini, E.2    Gomez-Ramos, P.3    Moran, M.A.4    Avila, J.5
  • 9
    • 35248821113 scopus 로고    scopus 로고
    • Collapsin response mediator protein-2 hyperphosphorylation is an early event in Alzheimer's disease progression
    • Cole, A. R., Noble, W., Aalten, L. V., Plattner, F. et al., Collapsin response mediator protein-2 hyperphosphorylation is an early event in Alzheimer's disease progression. J. Neurochem. 2007, 103, 1132-1144.
    • (2007) J. Neurochem. , vol.103 , pp. 1132-1144
    • Cole, A.R.1    Noble, W.2    Aalten, L.V.3    Plattner, F.4
  • 10
    • 84889049013 scopus 로고    scopus 로고
    • Pharmacologic inhibition of ROCK2 suppresses amyloid-beta production in an Alzheimer's disease mouse model
    • Herskowitz, J. H., Feng, Y., Mattheyses, A. L., Hales, C. M. et al., Pharmacologic inhibition of ROCK2 suppresses amyloid-beta production in an Alzheimer's disease mouse model. J. Neurosci. 2013, 33, 19086-19098.
    • (2013) J. Neurosci. , vol.33 , pp. 19086-19098
    • Herskowitz, J.H.1    Feng, Y.2    Mattheyses, A.L.3    Hales, C.M.4
  • 11
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localisation of the kinase
    • Hanger, D. P., Hughes, K., Woodgett, J. R., Brion, J.-P., Anderton, B. H., Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localisation of the kinase. Neurosc. Lett. 1992, 147, 58-62.
    • (1992) Neurosc. Lett. , vol.147 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.-P.4    Anderton, B.H.5
  • 12
    • 0038689162 scopus 로고    scopus 로고
    • Cdk5 is a key factor in tau aggregation and tangle formation in vivo
    • Noble, W., Olm, V., Takata, K., Casey, E. et al., Cdk5 is a key factor in tau aggregation and tangle formation in vivo. Neuron. 2003, 38, 555-565.
    • (2003) Neuron , vol.38 , pp. 555-565
    • Noble, W.1    Olm, V.2    Takata, K.3    Casey, E.4
  • 13
  • 14
    • 0033758105 scopus 로고    scopus 로고
    • Microtubule-affinity regulating kinase (MARK) is tightly associated with neurofibrillary tangles in Alzheimer brain: a fluorescence resonance energy transfer study
    • Chin, J. Y., Knowles, R. B., Schneider, A., Drewes, G. et al., Microtubule-affinity regulating kinase (MARK) is tightly associated with neurofibrillary tangles in Alzheimer brain: a fluorescence resonance energy transfer study. J. Neuropathol. Exp. Neurol. 2000, 59, 966-971.
    • (2000) J. Neuropathol. Exp. Neurol. , vol.59 , pp. 966-971
    • Chin, J.Y.1    Knowles, R.B.2    Schneider, A.3    Drewes, G.4
  • 15
    • 0027214404 scopus 로고
    • Phosphoprotein phosphatase activities in Alzheimer disease brain
    • Gong, C. X., Singh, T. J., Grundke-Iqbal, I., Iqbal, K., Phosphoprotein phosphatase activities in Alzheimer disease brain. J. Neurochem. 1993, 61, 921-927.
    • (1993) J. Neurochem. , vol.61 , pp. 921-927
    • Gong, C.X.1    Singh, T.J.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 16
    • 84855572697 scopus 로고    scopus 로고
    • Mapping in vivo signal transduction defects by phosphoproteomics
    • Stasyk, T., Huber, L. A., Mapping in vivo signal transduction defects by phosphoproteomics. Trends Mol. Med. 2012, 18, 43-51.
    • (2012) Trends Mol. Med. , vol.18 , pp. 43-51
    • Stasyk, T.1    Huber, L.A.2
  • 17
    • 51649095905 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of human brain by calcium phosphate precipitation and mass spectrometry
    • Xia, Q., Cheng, D., Duong, D. M., Gearing, M. et al., Phosphoproteomic analysis of human brain by calcium phosphate precipitation and mass spectrometry. J. Proteome Res. 2008, 7, 2845-2851.
    • (2008) J. Proteome Res. , vol.7 , pp. 2845-2851
    • Xia, Q.1    Cheng, D.2    Duong, D.M.3    Gearing, M.4
  • 18
    • 78649865461 scopus 로고    scopus 로고
    • Phosphoproteomic analysis reveals site-specific changes in GFAP and NDRG2 phosphorylation in frontotemporal lobar degeneration
    • Herskowitz, J. H., Seyfried, N. T., Duong, D. M., Xia, Q. et al., Phosphoproteomic analysis reveals site-specific changes in GFAP and NDRG2 phosphorylation in frontotemporal lobar degeneration. J. Proteome Res. 2010, 9, 6368-6379.
    • (2010) J. Proteome Res. , vol.9 , pp. 6368-6379
    • Herskowitz, J.H.1    Seyfried, N.T.2    Duong, D.M.3    Xia, Q.4
  • 19
    • 70450030926 scopus 로고    scopus 로고
    • The consequences of sample pooling in proteomics: an empirical study
    • Diz, A. P., Truebano, M., Skibinski, D. O., The consequences of sample pooling in proteomics: an empirical study. Electrophoresis 2009, 30, 2967-2975.
    • (2009) Electrophoresis , vol.30 , pp. 2967-2975
    • Diz, A.P.1    Truebano, M.2    Skibinski, D.O.3
  • 20
    • 84879962116 scopus 로고    scopus 로고
    • Neuron enriched nuclear proteome isolated from human brain
    • Dammer, E. B., Duong, D. M., Diner, I., Gearing, M. et al., Neuron enriched nuclear proteome isolated from human brain. J. Proteome Res. 2013, 12, 3193-3206.
    • (2013) J. Proteome Res. , vol.12 , pp. 3193-3206
    • Dammer, E.B.1    Duong, D.M.2    Diner, I.3    Gearing, M.4
  • 21
    • 70449436388 scopus 로고    scopus 로고
    • Proteomics analysis reveals novel components in the detergent-insoluble subproteome in Alzheimers disease
    • Gozal, Y. M., Duong, D. M., Gearing, M., Cheng, D. et al., Proteomics analysis reveals novel components in the detergent-insoluble subproteome in Alzheimers disease. J. Proteome Res. 2009, 8, 5069-5079.
    • (2009) J. Proteome Res. , vol.8 , pp. 5069-5079
    • Gozal, Y.M.1    Duong, D.M.2    Gearing, M.3    Cheng, D.4
  • 22
    • 84882245417 scopus 로고    scopus 로고
    • Exploring the potential of the platelet membrane proteome as a source of peripheral biomarkers for Alzheimer's disease
    • Donovan, L. E., Dammer, E. B., Duong, D. M., Hanfelt, J. J. et al., Exploring the potential of the platelet membrane proteome as a source of peripheral biomarkers for Alzheimer's disease. Alzheimers Res. Ther. 2013, 5, 32.
    • (2013) Alzheimers Res. Ther. , vol.5 , pp. 32
    • Donovan, L.E.1    Dammer, E.B.2    Duong, D.M.3    Hanfelt, J.J.4
  • 24
    • 78649894034 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of neuronal intermediate filament proteins (NF-M/H) in Alzheimer's disease by iTRAQ
    • Rudrabhatla, P., Grant, P., Jaffe, H., Strong, M. J., Pant, H. C., Quantitative phosphoproteomic analysis of neuronal intermediate filament proteins (NF-M/H) in Alzheimer's disease by iTRAQ. FASEB J. 2010, 24, 4396-4407.
    • (2010) FASEB J. , vol.24 , pp. 4396-4407
    • Rudrabhatla, P.1    Grant, P.2    Jaffe, H.3    Strong, M.J.4    Pant, H.C.5
  • 25
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias, J. E., Gygi, S. P., Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Meth. 2007, 4, 207-214.
    • (2007) Nat. Meth. , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 26
    • 33749853607 scopus 로고    scopus 로고
    • A probability-based approach for high-throughput protein phosphorylation analysis and site localization
    • Beausoleil, S. A., Villen, J., Gerber, S. A., Rush, J., Gygi, S. P., A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat. Biotechnol. 2006, 24, 1285-1292.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1285-1292
    • Beausoleil, S.A.1    Villen, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 27
    • 84860617820 scopus 로고    scopus 로고
    • Quantitative analysis of the detergent-insoluble brain proteome in frontotemporal lobar degeneration using SILAC internal standards
    • Seyfried, N. T., Gozal, Y. M., Donovan, L. E., Herskowitz, J. H. et al., Quantitative analysis of the detergent-insoluble brain proteome in frontotemporal lobar degeneration using SILAC internal standards. J. Proteome. Res. 2012, 11, 2721-2738.
    • (2012) J. Proteome. Res. , vol.11 , pp. 2721-2738
    • Seyfried, N.T.1    Gozal, Y.M.2    Donovan, L.E.3    Herskowitz, J.H.4
  • 28
    • 84863935926 scopus 로고    scopus 로고
    • Tissue-type plasminogen activator regulates the neuronal uptake of glucose in the Ischemic Brain
    • Wu, F., Wu, J., Nicholson, A. D., Echeverry, R. et al., Tissue-type plasminogen activator regulates the neuronal uptake of glucose in the Ischemic Brain. J. Neurosci. 2012, 32, 9848-9858.
    • (2012) J. Neurosci. , vol.32 , pp. 9848-9858
    • Wu, F.1    Wu, J.2    Nicholson, A.D.3    Echeverry, R.4
  • 29
    • 38449085131 scopus 로고    scopus 로고
    • Clinical proteomics in neurodegenerative diseases
    • Zhou, J. Y., Hanfelt, J., Peng, J., Clinical proteomics in neurodegenerative diseases. Proteomics Clin. Appl. 2007, 1, 1342-1350.
    • (2007) Proteomics Clin. Appl. , vol.1 , pp. 1342-1350
    • Zhou, J.Y.1    Hanfelt, J.2    Peng, J.3
  • 30
    • 60549111634 scopus 로고    scopus 로고
    • WGCNA: an R package for weighted correlation network analysis
    • Langfelder, P., Horvath, S., WGCNA: an R package for weighted correlation network analysis. BMC Bioinformatics 2008, 9, 559.
    • (2008) BMC Bioinformatics , vol.9 , pp. 559
    • Langfelder, P.1    Horvath, S.2
  • 31
    • 77950658888 scopus 로고    scopus 로고
    • Multiplex SILAC analysis of a cellular TDP-43 proteinopathy model reveals protein inclusions associated with SUMOylation and diverse polyUb chains
    • Seyfried, N. T., Gozal, Y. M., Dammer, E. B., Xia, Q. et al., Multiplex SILAC analysis of a cellular TDP-43 proteinopathy model reveals protein inclusions associated with SUMOylation and diverse polyUb chains. Mol. Cell. Proteomics 2010, 9, 705-718.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 705-718
    • Seyfried, N.T.1    Gozal, Y.M.2    Dammer, E.B.3    Xia, Q.4
  • 32
    • 66349093926 scopus 로고    scopus 로고
    • Magnetic bead processor for rapid evaluation and optimization of parameters for phosphopeptide enrichment
    • Ficarro, S. B., Adelmant, G., Tomar, M. N., Zhang, Y. et al., Magnetic bead processor for rapid evaluation and optimization of parameters for phosphopeptide enrichment. Anal. Chem. 2009, 81, 4566-4575.
    • (2009) Anal. Chem. , vol.81 , pp. 4566-4575
    • Ficarro, S.B.1    Adelmant, G.2    Tomar, M.N.3    Zhang, Y.4
  • 33
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da, W., Sherman, B. T., Lempicki, R. A., Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protocols 2009, 4, 44-57.
    • (2009) Nat. Protocols , vol.4 , pp. 44-57
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 34
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists
    • Huang da, W., Sherman, B. T., Lempicki, R. A., Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res. 2009, 37, 1-13.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1-13
    • Huang da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 35
    • 82955249335 scopus 로고    scopus 로고
    • Exploiting the diversity of the heat-shock protein family for primary and secondary tauopathy therapeutics
    • Abisambra, J. F., Jinwal, U. K., Jones, J. R., Blair, L. J. et al., Exploiting the diversity of the heat-shock protein family for primary and secondary tauopathy therapeutics. Curr. Neuropharmacol. 2011, 9, 623-631.
    • (2011) Curr. Neuropharmacol. , vol.9 , pp. 623-631
    • Abisambra, J.F.1    Jinwal, U.K.2    Jones, J.R.3    Blair, L.J.4
  • 36
    • 0028263008 scopus 로고
    • The serum-induced phosphorylation of mammalian hsp27 correlates with changes in its intracellular localization and levels of oligomerization
    • Mehlen, P., Arrigo, A.-P., The serum-induced phosphorylation of mammalian hsp27 correlates with changes in its intracellular localization and levels of oligomerization. Eur. J. Biochem. 1994, 221, 327-334.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 327-334
    • Mehlen, P.1    Arrigo, A.-P.2
  • 37
    • 37349032463 scopus 로고    scopus 로고
    • Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant
    • Ahmad, M. F., Raman, B., Ramakrishna, T., Rao Ch, M., Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant. J. Mol. Biol. 2008, 375, 1040-1051.
    • (2008) J. Mol. Biol. , vol.375 , pp. 1040-1051
    • Ahmad, M.F.1    Raman, B.2    Ramakrishna, T.3    Rao Ch, M.4
  • 38
    • 0027330972 scopus 로고
    • αB crystallin and HSP28 are enhanced in the cerebral cortex of patients with Alzheimer's disease
    • Shinohara, H., Inaguma, Y., Goto, S., Inagaki, T., Kato, K., αB crystallin and HSP28 are enhanced in the cerebral cortex of patients with Alzheimer's disease. J. Neurol. Sci. 1993, 119, 203-208.
    • (1993) J. Neurol. Sci. , vol.119 , pp. 203-208
    • Shinohara, H.1    Inaguma, Y.2    Goto, S.3    Inagaki, T.4    Kato, K.5
  • 39
    • 13644267037 scopus 로고    scopus 로고
    • Mammalian SAD kinases are required for neuronal polarization
    • Kishi, M., Pan, Y. A., Crump, J. G., Sanes, J. R., Mammalian SAD kinases are required for neuronal polarization. Science 2005, 307, 929-932.
    • (2005) Science , vol.307 , pp. 929-932
    • Kishi, M.1    Pan, Y.A.2    Crump, J.G.3    Sanes, J.R.4
  • 40
    • 33644994653 scopus 로고    scopus 로고
    • The ubiquitin-associated domain of AMPK-related kinases regulates conformation and LKB1-mediated phosphorylation and activation
    • Jaleel, M., Villa, F., Deak, M., Toth, R. et al., The ubiquitin-associated domain of AMPK-related kinases regulates conformation and LKB1-mediated phosphorylation and activation. Biochem. J. 2006, 394, 545-555.
    • (2006) Biochem. J. , vol.394 , pp. 545-555
    • Jaleel, M.1    Villa, F.2    Deak, M.3    Toth, R.4
  • 41
    • 83155185539 scopus 로고    scopus 로고
    • Emerging role of p62/sequestosome-1 in the pathogenesis of Alzheimer's disease
    • Salminen, A., Kaarniranta, K., Haapasalo, A., Hiltunen, M. et al., Emerging role of p62/sequestosome-1 in the pathogenesis of Alzheimer's disease. Progress Neurobiol. 2012, 96, 87-95.
    • (2012) Progress Neurobiol. , vol.96 , pp. 87-95
    • Salminen, A.1    Kaarniranta, K.2    Haapasalo, A.3    Hiltunen, M.4
  • 42
    • 82455172117 scopus 로고    scopus 로고
    • Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins
    • Matsumoto, G., Wada, K., Okuno, M., Kurosawa, M., Nukina, N., Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic clearance of ubiquitinated proteins. Mol. Cell 2011, 44, 279-289.
    • (2011) Mol. Cell , vol.44 , pp. 279-289
    • Matsumoto, G.1    Wada, K.2    Okuno, M.3    Kurosawa, M.4    Nukina, N.5
  • 43
    • 79953197650 scopus 로고    scopus 로고
    • Polyubiquitin linkage profiles in three models of proteolytic stress suggest the etiology of Alzheimer disease
    • Dammer, E. B., Na, C. H., Xu, P., Seyfried, N. T. et al., Polyubiquitin linkage profiles in three models of proteolytic stress suggest the etiology of Alzheimer disease. J. Biol. Chem. 2011, 286, 10457-10465.
    • (2011) J. Biol. Chem. , vol.286 , pp. 10457-10465
    • Dammer, E.B.1    Na, C.H.2    Xu, P.3    Seyfried, N.T.4
  • 44
    • 1342294313 scopus 로고    scopus 로고
    • The Hsp90 Cochaperone p23 is the limiting component of the multiprotein Hsp90/Hsp70-based chaperone system in vivo where it acts to stabilize the client protein·Hsp90 complex
    • Morishima, Y., Kanelakis, K. C., Murphy, P. J. M., Lowe, E. R. et al., The Hsp90 Cochaperone p23 is the limiting component of the multiprotein Hsp90/Hsp70-based chaperone system in vivo where it acts to stabilize the client protein·Hsp90 complex. J. Biol. Chem. 2003, 278, 48754-48763.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48754-48763
    • Morishima, Y.1    Kanelakis, K.C.2    Murphy, P.J.M.3    Lowe, E.R.4
  • 45
    • 63349087295 scopus 로고    scopus 로고
    • Cytosolic prostaglandin E synthase: expression patterns in control and Alzheimer's disease brains
    • Chaudhry, U. A., Dore, S., Cytosolic prostaglandin E synthase: expression patterns in control and Alzheimer's disease brains. Am. J. Alzheimer's Dis. Other Dementias 2009, 24, 46-51.
    • (2009) Am. J. Alzheimer's Dis. Other Dementias , vol.24 , pp. 46-51
    • Chaudhry, U.A.1    Dore, S.2


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