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Volumn 51, Issue 18, 2012, Pages 3759-3766

A mass spectrometric approach for characterization of amyloid-β aggregates and identification of their post-translational modifications

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER'S DISEASE; DIAGNOSTIC TOOLS; IMMUNOAFFINITY CHROMATOGRAPHY; IN-VIVO; ION MAPPING; LOW LEVEL; POST-TRANSLATIONAL MODIFICATIONS; PRECURSOR IONS; STRUCTURAL CHARACTERIZATION; THERAPEUTIC DRUGS; TOXIC AGENTS; TRANSGLUTAMINASES;

EID: 84860782237     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300316d     Document Type: Article
Times cited : (10)

References (45)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy, J. and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 297, 353-356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 3
    • 33750841488 scopus 로고    scopus 로고
    • Neuronal neprilysin overexpression is associated with attenuation of Aβ-related spatial memory deficit
    • DOI 10.1016/j.nbd.2006.08.003, PII S0969996106001999
    • Poirier, R., Wolfer, D., Welzl, H., Tracy, J., Galsworthy, M., Nitsch, R., and Mohajeri, M. (2006) Neuronal neprilysin overexpression is associated with attenuation of Aβ-related spatial memory deficit Neurobiol. Dis. 24, 475-483 (Pubitemid 44716677)
    • (2006) Neurobiology of Disease , vol.24 , Issue.3 , pp. 475-483
    • Poirier, R.1    Wolfer, D.P.2    Welzl, H.3    Tracy, J.4    Galsworthy, M.J.5    Nitsch, R.M.6    Mohajeri, M.H.7
  • 4
    • 0037462769 scopus 로고    scopus 로고
    • Alzheimer's disease β-amyloid peptide is increased in mice deficient in endothelin-converting enzyme
    • DOI 10.1074/jbc.C200642200
    • Eckman, E. A. (2002) Alzheimer's disease beta-amyloid peptide is increased in mice deficient in endothelin-converting enzyme J. Biol. Chem. 278, 2081-2084 (Pubitemid 36801269)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.4 , pp. 2081-2084
    • Eckman, E.A.1    Watson, M.2    Marlow, L.3    Sambamurti, K.4    Eckman, C.B.5
  • 10
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • DOI 10.1038/416535a
    • Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., and Selkoe, D. J. (2002) Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo Nature 416, 535-539 (Pubitemid 34288854)
    • (2002) Nature , vol.416 , Issue.6880 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 12
    • 71549121663 scopus 로고    scopus 로고
    • Biophysical analyses of synthetic amyloid-β(1-42) aggregates before and after covalent cross-linking. Implications for deducing the structure of endogenous amyloid-β oligomers
    • Moore, B. D., Rangachari, V., Tay, W. M., Milkovic, N. M., and Rosenberry, T. L. (2009) Biophysical analyses of synthetic amyloid-β(1-42) aggregates before and after covalent cross-linking. Implications for deducing the structure of endogenous amyloid-β oligomers Biochemistry 48, 11796-11806
    • (2009) Biochemistry , vol.48 , pp. 11796-11806
    • Moore, B.D.1    Rangachari, V.2    Tay, W.M.3    Milkovic, N.M.4    Rosenberry, T.L.5
  • 13
    • 0033551440 scopus 로고    scopus 로고
    • Assembly of Aβ amyloid peptides: An in vitro model for a possible early event in Alzheimer's disease
    • Harper, J. D., Wong, S. S., Lieber, C. M., and Lansbury, P. T., Jr. (1999) Assembly of Aβ amyloid peptides: an in vitro model for a possible early event in Alzheimer's disease Biochemistry 38, 8972-8980
    • (1999) Biochemistry , vol.38 , pp. 8972-8980
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury Jr., P.T.4
  • 14
    • 0037076539 scopus 로고    scopus 로고
    • Growth of β-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy
    • DOI 10.1021/bi015985r
    • Nichols, M. R., Moss, M. A., Reed, D. K., Lin, W.-L., Mukhopadhyay, R., Hoh, J. H., and Rosenberry, T. L. (2002) Growth of β-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy Biochemistry 41, 6115-6127 (Pubitemid 34498918)
    • (2002) Biochemistry , vol.41 , Issue.19 , pp. 6115-6127
    • Nichols, M.R.1    Moss, M.A.2    Reed, D.K.3    Lin, W.-L.4    Mukhopadhyay, R.5    Hoh, J.H.6    Rosenberry, T.L.7
  • 20
    • 33746095813 scopus 로고    scopus 로고
    • Secondary structure and interfacial aggregation of amyloid-β(1-40) on sodium dodecyl sulfate micelles
    • DOI 10.1021/bi060323t
    • Rangachari, V., Reed, D. K., Moore, B. D., and Rosenberry, T. L. (2006) Secondary structure and interfacial aggregation of amyloid-β(1-40) on sodium dodecylsulfate micelles Biochemistry 45, 8639-8648 (Pubitemid 44078884)
    • (2006) Biochemistry , vol.45 , Issue.28 , pp. 8639-8648
    • Rangachari, V.1    Reed, D.K.2    Moore, B.D.3    Rosenberry, T.L.4
  • 21
    • 35648986681 scopus 로고    scopus 로고
    • Amyloid-β(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate
    • DOI 10.1021/bi701213s
    • Rangachari, V., Moore, B. D., Reed, D. K., Sonoda, L. K., Bridges, A. W., Conboy, E., Hartigan, D., and Rosenberry, T. L. (2007) Amyloid-β(1-42) rapidly forms protofibrils and oligomers by distinct pathways in low concentrations of sodium dodecylsulfate Biochemistry 46, 12451-12462 (Pubitemid 350027406)
    • (2007) Biochemistry , vol.46 , Issue.43 , pp. 12451-12462
    • Rangachari, V.1    Moore, B.D.2    Reed, D.K.3    Sonoda, L.K.4    Bridges, A.W.5    Conboy, E.6    Hartigan, D.7    Rosenberry, T.L.8
  • 25
    • 0033373675 scopus 로고    scopus 로고
    • Elevated transglutaminase-induced bonds in PHF tau in Alzheimer's disease
    • DOI 10.1016/S0006-8993(99)02179-4, PII S0006899399021794
    • Norlund, M. A., Lee, J. M., Zainelli, G. M., and Muma, N. A. (1999) Elevated transglutaminase-induced bonds in PHF tau in Alzheimer's disease Brain Res. 851, 154-163 (Pubitemid 30038140)
    • (1999) Brain Research , vol.851 , Issue.1-2 , pp. 154-163
    • Norlund, M.A.1    Lee, J.M.2    Zainelli, G.M.3    Muma, N.A.4
  • 26
    • 0030998670 scopus 로고    scopus 로고
    • Transglutaminase activity is increased in Alzheimer's disease brain
    • DOI 10.1016/S0006-8993(96)01431-X, PII S000689939601431X
    • Johnson, G. V. W., Cox, T. M., Lockhart, J. P., Zinnerman, M. D., Miller, M. L., and Powers, R. E. (1997) Transglutaminase activity is increased in Alzheimer's disease brain Brain Res. 751, 323-329 (Pubitemid 27132565)
    • (1997) Brain Research , vol.751 , Issue.2 , pp. 323-329
    • Johnson, G.V.W.1    Cox, T.M.2    Lockhart, J.P.3    Zinnerman, M.D.4    Miller, M.L.5    Powers, R.E.6
  • 27
    • 62849088434 scopus 로고    scopus 로고
    • MALDI, AP/MALDI and ESI techniques for the MS detection of amyloid β-peptides
    • Grasso, G., Mineo, P., Rizzarelli, E., and Spoto, G. (2009) MALDI, AP/MALDI and ESI techniques for the MS detection of amyloid β-peptides Int. J. Mass Spectrom. 282, 50-55
    • (2009) Int. J. Mass Spectrom. , vol.282 , pp. 50-55
    • Grasso, G.1    Mineo, P.2    Rizzarelli, E.3    Spoto, G.4
  • 29
    • 55249111076 scopus 로고    scopus 로고
    • A tandem MS precursor-ion scan approach to identify variable covalent modification of albumin Cys34: A new tool for studying vascular carbonylation
    • Aldini, G., Regazzoni, L., Orioli, M., Rimoldi, I., Facino, R. M., and Carini, M. (2008) A tandem MS precursor-ion scan approach to identify variable covalent modification of albumin Cys34: a new tool for studying vascular carbonylation J. Mass Spectrom. 43, 1470-1481
    • (2008) J. Mass Spectrom. , vol.43 , pp. 1470-1481
    • Aldini, G.1    Regazzoni, L.2    Orioli, M.3    Rimoldi, I.4    Facino, R.M.5    Carini, M.6
  • 30
    • 0035298820 scopus 로고    scopus 로고
    • Detection of tyrosine phosphorylated peptides by precursor ion scanning quadrupole TOF mass spectrometry in positive ion mode
    • DOI 10.1021/ac001318c
    • Steen, H., Kuster, B., Fernandez, M., Pandey, A., and Mann, M. (2001) Detection of tyrosine phosphorylated peptides by precursor ion scanning quadrupole TOF mass spectrometry in positive ion mode Anal. Chem. 73, 1440-1448 (Pubitemid 32896198)
    • (2001) Analytical Chemistry , vol.73 , Issue.7 , pp. 1440-1448
    • Steen, H.1    Kuster, B.2    Fernandez, M.3    Pandey, A.4    Mann, M.5
  • 31
    • 0027586797 scopus 로고
    • Collisional fragmentation of glycopeptides by electrospray ionization LC/MS and LC/MS/MS: Methods for selective detection of glycopeptides in protein digests
    • Huddleston, M. J., Bean, M. F., and Carr, S. A. (1993) Collisional fragmentation of glycopeptides by electrospray ionization LC/MS and LC/MS/MS: methods for selective detection of glycopeptides in protein digests Anal. Chem. 65, 877-884
    • (1993) Anal. Chem. , vol.65 , pp. 877-884
    • Huddleston, M.J.1    Bean, M.F.2    Carr, S.A.3
  • 32
    • 81855176005 scopus 로고    scopus 로고
    • Identification of oxidized phospholipids by electrospray ionization mass spectrometry and LC-MS using a QQLIT instrument
    • Spickett, C. M., Reis, A., and Pitt, A. R. (2011) Identification of oxidized phospholipids by electrospray ionization mass spectrometry and LC-MS using a QQLIT instrument Free Radical Biol. Med. 51, 2133-2149
    • (2011) Free Radical Biol. Med. , vol.51 , pp. 2133-2149
    • Spickett, C.M.1    Reis, A.2    Pitt, A.R.3
  • 33
    • 69949125668 scopus 로고    scopus 로고
    • Transglutaminases and transglutaminase-catalyzed cross-links colocalize with the pathological lesions in Alzheimer's disease brain
    • Wilhelmus, M. M., Grunberg, S. C., Bol, J. G., van Dam, A. M., Hoozemans, J. J., Rozemuller, A. J., and Drukarch, B. (2009) Transglutaminases and transglutaminase-catalyzed cross-links colocalize with the pathological lesions in Alzheimer's disease brain Brain Pathol. 19, 612-622
    • (2009) Brain Pathol. , vol.19 , pp. 612-622
    • Wilhelmus, M.M.1    Grunberg, S.C.2    Bol, J.G.3    Van Dam, A.M.4    Hoozemans, J.J.5    Rozemuller, A.J.6    Drukarch, B.7
  • 34
    • 0026338017 scopus 로고
    • Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg, C. S., Birckbichler, P. J., and Rice, R. H. (1991) Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues FASEB J. 5, 3071-3077 (Pubitemid 21892867)
    • (1991) FASEB Journal , vol.5 , Issue.15 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 35
    • 0028298620 scopus 로고
    • Transglutaminase facilitates the formation of polymers of the β-amyloid peptide
    • DOI 10.1016/0006-8993(94)90688-2
    • Dudek, S. M. and Johnson, G. V. (1994) Transglutaminase facilitates the formation of polymers of the β-amyloid peptide Brain Res. 651, 129-133 (Pubitemid 24222858)
    • (1994) Brain Research , vol.651 , Issue.1-2 , pp. 129-133
    • Dudek, S.M.1    Johnson, G.V.W.2
  • 36
    • 0027289153 scopus 로고
    • Cross-linking of a synthetic partial-length (1-28) peptide of the Alzheimer β/A4 amyloid protein by transglutaminase
    • DOI 10.1016/0014-5793(93)81772-R
    • Ikura, K., Takahata, K., and Sasaki, R. (1993) Cross-linking of a synthetic partial-length (1-28) peptide of the Alzheimer beta/A4 amyloid protein by transglutaminase FEBS Lett. 326, 109-111 (Pubitemid 23200258)
    • (1993) FEBS Letters , vol.326 , Issue.1-3 , pp. 109-111
    • Ikura, K.1    Takahata, K.2    Sasaki, R.3
  • 37
    • 0028144630 scopus 로고
    • 2M receptor
    • DOI 10.1016/0014-5793(94)80356-0
    • Rasmussen, L. K., Sorensen, E. S., Petersen, T. E., Gliemann, J., and Jensen, P. H. (1994) Identification of glutamine and lysine residues in Alzheimer amyloid beta A4 peptide responsible for transglutaminase-catalysed homopolymerization and cross-linking to alpha 2M receptor FEBS Lett. 338, 161-166 (Pubitemid 24064957)
    • (1994) FEBS Letters , vol.338 , Issue.2 , pp. 161-166
    • Rasmussen, L.K.1
  • 38
    • 0028177277 scopus 로고
    • Cross-linking of β-amyloid protein precursor catalyzed by tissue transglutaminase
    • Ho, G. J., Gregory, E. J., Smirnova, I. V., Zoubine, M. N., and Festoff, B. W. (1994) Cross-linking of β-amyloid protein precursor catalyzed by tissue transglutaminase FEBS Lett. 349, 151-154
    • (1994) FEBS Lett. , vol.349 , pp. 151-154
    • Ho, G.J.1    Gregory, E.J.2    Smirnova, I.V.3    Zoubine, M.N.4    Festoff, B.W.5
  • 39
    • 33846458989 scopus 로고    scopus 로고
    • A Triaxial Probe for On-line Proteolysis Coupled with Hydrogen/Deuterium Exchange-Electrospray Mass Spectrometry
    • DOI 10.1016/j.jasms.2006.09.011, PII S1044030506008282
    • Chen, M., Cook, K. D., Kheterpal, I., and Wetzel, R. (2007) A triaxial probe for on-line proteolysis coupled with hydrogen/deuterium exchange-electrospray mass spectrometry J. Am. Soc. Mass Spectrom. 18, 208-217 (Pubitemid 46150090)
    • (2007) Journal of the American Society for Mass Spectrometry , vol.18 , Issue.2 , pp. 208-217
    • Chen, M.1    Cook, K.D.2    Kheterpal, I.3    Wetzel, R.4
  • 40
    • 76149098520 scopus 로고    scopus 로고
    • Identification of cross-linked peptides by high-resolution precursor ion scan
    • Iglesias, A. H., Santos, L. F. A., and Gozzo, F. (2010) Identification of cross-linked peptides by high-resolution precursor ion scan Anal. Chem. 82, 909-916
    • (2010) Anal. Chem. , vol.82 , pp. 909-916
    • Iglesias, A.H.1    Santos, L.F.A.2    Gozzo, F.3
  • 41
    • 33645505550 scopus 로고    scopus 로고
    • Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: A potent role for trimers
    • Townsend, M., Shankar, G. M., Mehta, T., Walsh, D. M., and Selkoe, D. J. (2006) Effects of secreted oligomers of amyloid β-protein on hippocampal synaptic plasticity: a potent role for trimers J. Physiol. 572, 477-492
    • (2006) J. Physiol. , vol.572 , pp. 477-492
    • Townsend, M.1    Shankar, G.M.2    Mehta, T.3    Walsh, D.M.4    Selkoe, D.J.5
  • 42
    • 0033860372 scopus 로고    scopus 로고
    • Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity
    • Varadarajan, S., Yatin, S., Aksenova, M., and Butterfield, D. A. (2000) Review: Alzheimer's amyloid beta-peptide-associated free radical oxidative stress and neurotoxicity J. Struct. Biol. 130, 184-208
    • (2000) J. Struct. Biol. , vol.130 , pp. 184-208
    • Varadarajan, S.1    Yatin, S.2    Aksenova, M.3    Butterfield, D.A.4
  • 45
    • 0029752755 scopus 로고    scopus 로고
    • The profile of soluble amyloid β protein in cultured cell media. Detection and quantification of amyloid β protein and variants by immunoprecipitation-mass spectrometry
    • DOI 10.1074/jbc.271.50.31894
    • Wang, R., Sweeney, D., Gandy, S. E., and Sisodia, S. S. (1996) The profile of soluble amyloid beta protein in cultured cell media. Detection and quantification of amyloid beta protein and variants by immunoprecipitation-mass spectrometry J. Biol. Chem. 271, 31894-31902 (Pubitemid 26422211)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.50 , pp. 31894-31902
    • Wang, R.1    Sweeney, D.2    Gandy, S.E.3    Sisodia, S.S.4


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