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Volumn 90, Issue 3, 2014, Pages 104-117

Identification and quantification of amyloid beta-related peptides in human plasma using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

Author keywords

Alzheimer's disease; Amyloid precursor protein; Amyloid ; Immunoprecipitation; Matrix assisted laser desorption ionization time of flight mass spectrometry; Plasma

Indexed keywords

AMYLOID BETA PROTEIN;

EID: 84896836139     PISSN: 03862208     EISSN: 13492896     Source Type: Journal    
DOI: 10.2183/pjab.90.104     Document Type: Article
Times cited : (57)

References (41)
  • 2
    • 0026597063 scopus 로고
    • Alzheimer's disease: the amyloid cascade hypothesis
    • Hardy, J.A. and Higgins, G.A. (1992) Alzheimer's disease: the amyloid cascade hypothesis. Science 256, 184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 4
    • 7944233158 scopus 로고    scopus 로고
    • Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases
    • Selkoe, D.J. (2004) Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases. Nat. Cell Biol. 6, 1054-1061.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1054-1061
    • Selkoe, D.J.1
  • 5
    • 0028179341 scopus 로고
    • Chemical characterization of A beta 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease
    • Gowing, E., Roher, A.E., Woods, A.S., Cotter, R.J., Chaney, M., Little, S.P. and Ball, M.J. (1994) Chemical characterization of A beta 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease. J. Biol. Chem. 269, 10987- 10990.
    • (1994) J. Biol. Chem. , vol.269
    • Gowing, E.1    Roher, A.E.2    Woods, A.S.3    Cotter, R.J.4    Chaney, M.5    Little, S.P.6    Ball, M.J.7
  • 7
    • 57649221135 scopus 로고    scopus 로고
    • Amyloid precursor protein trafficking, processing, and function
    • Thinakaran, G. and Koo, E.H. (2008) Amyloid precursor protein trafficking, processing, and function. J. Biol. Chem. 283, 29615-29619.
    • (2008) J. Biol. Chem. , vol.283 , pp. 29615-29619
    • Thinakaran, G.1    Koo, E.H.2
  • 9
    • 84867028097 scopus 로고    scopus 로고
    • Lysosomal fusion dysfunction as a unifying hypothesis for Alzheimer's disease pathology
    • Funk, K.E. and Kuret, J. (2012) Lysosomal fusion dysfunction as a unifying hypothesis for Alzheimer's disease pathology. Int. J. Alzheimers Dis. 2012, 752894.
    • (2012) Int. J. Alzheimers Dis. , vol.2012 , pp. 752894
    • Funk, K.E.1    Kuret, J.2
  • 10
    • 0034667518 scopus 로고    scopus 로고
    • Purified recombinant insulindegrading enzyme degrades amyloid beta-protein but does not promote its oligomerization
    • Chesneau, V., Vekrellis, K., Rosner, M.R. and Selkoe, D.J. (2000) Purified recombinant insulindegrading enzyme degrades amyloid beta-protein but does not promote its oligomerization. Biochem. J. 351 (Pt 2), 509-516.
    • (2000) Biochem. J. , vol.351 , Issue.PART 2 , pp. 509-516
    • Chesneau, V.1    Vekrellis, K.2    Rosner, M.R.3    Selkoe, D.J.4
  • 11
    • 0034551718 scopus 로고    scopus 로고
    • Insulysin hydrolyzes amyloid beta peptides to products that are neither neurotoxic nor deposit on amyloid plaques
    • Mukherjee, A., Song, E., Kihiko-Ehmann, M., Goodman, J.P., Pyrek, J.S., Estus, S. and Hersh, L.B. (2000) Insulysin hydrolyzes amyloid beta peptides to products that are neither neurotoxic nor deposit on amyloid plaques. J. Neurosci. 20, 8745-8749.
    • (2000) J. Neurosci. , vol.20 , pp. 8745-8749
    • Mukherjee, A.1    Song, E.2    Kihiko-Ehmann, M.3    Goodman, J.P.4    Pyrek, J.S.5    Estus, S.6    Hersh, L.B.7
  • 12
    • 27344441173 scopus 로고    scopus 로고
    • Metabolism of amyloid-beta peptide and Alzheimer's disease
    • Iwata, N., Higuchi, M. and Saido, T.C. (2005) Metabolism of amyloid-beta peptide and Alzheimer's disease. Pharmacol. Ther. 108, 129-148.
    • (2005) Pharmacol. Ther. , vol.108 , pp. 129-148
    • Iwata, N.1    Higuchi, M.2    Saido, T.C.3
  • 18
    • 0027379395 scopus 로고
    • Characterization of betaamyloid peptide from human cerebrospinal fluid
    • Vigo-Pelfrey, C., Lee, D., Keim, P., Lieberburg, I. and Schenk, D.B. (1993) Characterization of betaamyloid peptide from human cerebrospinal fluid. J. Neurochem. 61, 1965-1968.
    • (1993) J. Neurochem. , vol.61 , pp. 1965-1968
    • Vigo-Pelfrey, C.1    Lee, D.2    Keim, P.3    Lieberburg, I.4    Schenk, D.B.5
  • 19
    • 0029752755 scopus 로고    scopus 로고
    • The profile of soluble amyloid beta protein in cultured cell media. Detection and quantification of amyloid beta protein and variants by immunoprecipitation-mass spectrometry
    • 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.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31894-31902
    • Wang, R.1    Sweeney, D.2    Gandy, S.E.3    Sisodia, S.S.4
  • 20
    • 33645775230 scopus 로고    scopus 로고
    • Determination of betaamyloid peptide signatures in cerebrospinal fluid using immunoprecipitation-mass spectrometry
    • Portelius, E., Westman-Brinkmalm, A., Zetterberg, H. and Blennow, K. (2006) Determination of betaamyloid peptide signatures in cerebrospinal fluid using immunoprecipitation-mass spectrometry. J. Proteome Res. 5, 1010-1016.
    • (2006) J. Proteome Res. , vol.5 , pp. 1010-1016
    • Portelius, E.1    Westman-Brinkmalm, A.2    Zetterberg, H.3    Blennow, K.4
  • 21
    • 36348970121 scopus 로고    scopus 로고
    • Characterization of amyloid beta peptides in cerebrospinal fluid by an automated immunoprecipitation procedure followed by mass spectrometry
    • Portelius, E., Tran, A.J., Andreasson, U., Persson, R., Brinkmalm, G., Zetterberg, H., Blennow, K. and Westman-Brinkmalm, A. (2007) Characterization of amyloid beta peptides in cerebrospinal fluid by an automated immunoprecipitation procedure followed by mass spectrometry. J. Proteome Res. 6, 4433-4439.
    • (2007) J. Proteome Res. , vol.6 , pp. 4433-4439
    • Portelius, E.1    Tran, A.J.2    Andreasson, U.3    Persson, R.4    Brinkmalm, G.5    Zetterberg, H.6    Blennow, K.7    Westman-Brinkmalm, A.8
  • 25
    • 29744444606 scopus 로고    scopus 로고
    • Effects of total plasma protein concentration on plasma sodium, potassium and chloride measurements by an indirect ion selective electrode measuring system
    • Dimeski, G. and Barnett, R.J. (2005) Effects of total plasma protein concentration on plasma sodium, potassium and chloride measurements by an indirect ion selective electrode measuring system. Crit. Care Resusc. 7, 12-15.
    • (2005) Crit. Care Resusc. , vol.7 , pp. 12-15
    • Dimeski, G.1    Barnett, R.J.2
  • 26
    • 33845572150 scopus 로고    scopus 로고
    • Human body fluid proteome analysis
    • Hu, S., Loo, J.A. and Wong, D.T. (2006) Human body fluid proteome analysis. Proteomics 6, 6326- 6353.
    • (2006) Proteomics , vol.6
    • Hu, S.1    Loo, J.A.2    Wong, D.T.3
  • 28
    • 76149083562 scopus 로고    scopus 로고
    • Analysis of large peptides by MALDI using a linear quadrupole ion trap with mass range extension
    • Magparangalan, D.P., Garrett, T.J., Drexler, D.M. and Yost, R.A. (2010) Analysis of large peptides by MALDI using a linear quadrupole ion trap with mass range extension. Anal. Chem. 82, 930-934.
    • (2010) Anal. Chem. , vol.82 , pp. 930-934
    • Magparangalan, D.P.1    Garrett, T.J.2    Drexler, D.M.3    Yost, R.A.4
  • 29
    • 14744281153 scopus 로고    scopus 로고
    • Quantification of the A beta peptide in Alzheimer's plaques by laser dissection microscopy combined with mass spectrometry
    • Rüfenacht, P., Güntert, A., Bohrmann, B., Ducret, A. and Döbeli, H. (2005) Quantification of the A beta peptide in Alzheimer's plaques by laser dissection microscopy combined with mass spectrometry. J. Mass Spectrom. 40, 193-201.
    • (2005) J. Mass Spectrom. , vol.40 , pp. 193-201
    • Rüfenacht, P.1    Güntert, A.2    Bohrmann, B.3    Ducret, A.4    Döbeli, H.5
  • 31
    • 84857504095 scopus 로고    scopus 로고
    • A novel study on amyloid O peptide 40, 42 and 40/42 ratio in Saudi autistics
    • Al-Ayadhi, L.Y., Ben Bacha, A.G., Kotb, M. and El- Ansary, A.K. (2012) A novel study on amyloid O peptide 40, 42 and 40/42 ratio in Saudi autistics. Behav. Brain Funct. 8, 4.
    • (2012) Behav. Brain Funct. , vol.8 , pp. 4
    • Al-Ayadhi, L.Y.1    Ben Bacha, A.G.2    Kotb, M.3    El-Ansary, A.K.4
  • 33
    • 0033597105 scopus 로고    scopus 로고
    • gamma- Secretase, evidence for multiple proteolytic activities and influence of membrane positioning of substrate on generation of amyloid beta peptides of varying length
    • Murphy, M.P., Hickman, L.J., Eckman, C.B., Uljon, S.N., Wang, R. and Golde, T.E. (1999) gamma- Secretase, evidence for multiple proteolytic activities and influence of membrane positioning of substrate on generation of amyloid beta peptides of varying length. J. Biol. Chem. 274, 11914-11923.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11914-11923
    • Murphy, M.P.1    Hickman, L.J.2    Eckman, C.B.3    Uljon, S.N.4    Wang, R.5    Golde, T.E.6
  • 34
    • 0036322138 scopus 로고    scopus 로고
    • Generation of C-terminally truncated amyloid-beta peptides is dependent on gamma-secretase activity
    • Beher, D., Wrigley, J.D.J., Owens, A.P. and Shearman, M.S. (2002) Generation of C-terminally truncated amyloid-beta peptides is dependent on gamma-secretase activity. J. Neurochem. 82, 563- 575.
    • (2002) J. Neurochem. , vol.82
    • Beher, D.1    Wrigley, J.D.J.2    Owens, A.P.3    Shearman, M.S.4
  • 36
    • 0036077536 scopus 로고    scopus 로고
    • Beta-amyloid catabolism: roles for neprilysin (NEP) and other metallopeptidases?
    • Carson, J.A. and Turner, A.J. (2002) Beta-amyloid catabolism: roles for neprilysin (NEP) and other metallopeptidases? J. Neurochem. 81, 1-8.
    • (2002) J Neurochem. , vol.81 , pp. 1-8
    • Carson, J.A.1    Turner, A.J.2
  • 37
    • 0033623415 scopus 로고    scopus 로고
    • Abeta-generating enzymes: recent advances in beta- and gammasecretase research
    • Vassar, R. and Citron, M. (2000) Abeta-generating enzymes: recent advances in beta- and gammasecretase research. Neuron 27, 419-422.
    • (2000) Neuron , vol.27 , pp. 419-422
    • Vassar, R.1    Citron, M.2
  • 39
    • 4344673143 scopus 로고    scopus 로고
    • Biomarkers of Alzheimer disease in plasma
    • Irizarry, M.C. (2004) Biomarkers of Alzheimer disease in plasma. NeuroRx 1, 226-234.
    • (2004) NeuroRx , vol.1 , pp. 226-234
    • Irizarry, M.C.1
  • 40
    • 0034027642 scopus 로고    scopus 로고
    • Agedependent change in the levels of Abeta40 and Abeta42 in cerebrospinal fluid from control subjects, and a decrease in the ratio of Abeta42 to Abeta40 level in cerebrospinal fluid from Alzheimer's disease patients
    • Fukuyama, R., Mizuno, T., Mori, S., Nakajima, K., Fushiki, S. and Yanagisawa, K. (2000) Agedependent change in the levels of Abeta40 and Abeta42 in cerebrospinal fluid from control subjects, and a decrease in the ratio of Abeta42 to Abeta40 level in cerebrospinal fluid from Alzheimer's disease patients. Eur. Neurol. 43, 155-160.
    • (2000) Eur. Neurol. , vol.43 , pp. 155-160
    • Fukuyama, R.1    Mizuno, T.2    Mori, S.3    Nakajima, K.4    Fushiki, S.5    Yanagisawa, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.