메뉴 건너뛰기




Volumn 6, Issue 11, 2007, Pages 4433-4439

Characterization of amyloid β peptides in cerebrospinal fluid by an automated immunoprecipitation procedure followed by mass spectrometry

Author keywords

amyloid; Alzheimer's disease; Cerebrospinal fluid; Immunoprecipitation; LC MS MS; LTQ FT; MALDI TOF MS

Indexed keywords

AMYLOID BETA PROTEIN;

EID: 36348970121     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr0703627     Document Type: Article
Times cited : (139)

References (36)
  • 1
  • 2
    • 7944233158 scopus 로고    scopus 로고
    • Selkoe, D. J. Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases. Nat. Cell Biol. 2004, 6 (11), 1054-1061.
    • Selkoe, D. J. Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases. Nat. Cell Biol. 2004, 6 (11), 1054-1061.
  • 4
    • 0038343343 scopus 로고    scopus 로고
    • Amyloid precursor protein (APP) and the biology of proteolytic processing: Relevance to Alzheimer's disease
    • Ling, Y.; Morgan, K.; Kalsheker, N. Amyloid precursor protein (APP) and the biology of proteolytic processing: relevance to Alzheimer's disease. Int. J. Biochem. Cell Biol. 2003, 35 (11), 1505-1535.
    • (2003) Int. J. Biochem. Cell Biol , vol.35 , Issue.11 , pp. 1505-1535
    • Ling, Y.1    Morgan, K.2    Kalsheker, N.3
  • 5
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe, D. J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 2001, 81 (2), 741-766.
    • (2001) Physiol. Rev , vol.81 , Issue.2 , pp. 741-766
    • Selkoe, D.J.1
  • 6
    • 26244462301 scopus 로고    scopus 로고
    • Proteolytic mechanisms in amyloid-beta metabolism: Therapeutic implications for Alzheimer's disease
    • Vardy, E. R.; Catto, A. J.; Hooper, N. M. Proteolytic mechanisms in amyloid-beta metabolism: therapeutic implications for Alzheimer's disease. Trends Mol. Med. 2005, 11 (10), 464-472.
    • (2005) Trends Mol. Med , vol.11 , Issue.10 , pp. 464-472
    • Vardy, E.R.1    Catto, A.J.2    Hooper, N.M.3
  • 8
    • 0027535111 scopus 로고
    • J. beta-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms
    • Haass, C.; Hung, A. Y.; Schlossmacher, M. G.; Teplow, D. B.; Selkoe, D. J. beta-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms. J. Biol. Chem. 1993, 268 (5), 3021-3024.
    • (1993) J. Biol. Chem , vol.268 , Issue.5 , pp. 3021-3024
    • Haass, C.1    Hung, A.Y.2    Schlossmacher, M.G.3    Teplow, D.B.4    Selkoe, D.5
  • 10
    • 0031698581 scopus 로고    scopus 로고
    • ADAMs: Focus on the protease domain
    • Black, R. A.; White, J. M. ADAMs: focus on the protease domain. Curr. Opin. Cell Biol. 1998, 10 (5), 654-659.
    • (1998) Curr. Opin. Cell Biol , vol.10 , Issue.5 , pp. 654-659
    • Black, R.A.1    White, J.M.2
  • 11
    • 33747341626 scopus 로고    scopus 로고
    • The ADAMs family: Coordinators of nervous system development, plasticity and repair
    • Yang, P.; Baker, K. A.; Hagg, T. The ADAMs family: coordinators of nervous system development, plasticity and repair. Prog. Neurobiol. 2006, 79 (2), 73-94.
    • (2006) Prog. Neurobiol , vol.79 , Issue.2 , pp. 73-94
    • Yang, P.1    Baker, K.A.2    Hagg, T.3
  • 12
    • 0242330374 scopus 로고    scopus 로고
    • ADAMs family members as amyloid precursor protein alpha-secretases
    • Allinson, T. M.; Parkin, E. T.; Turner, A. J.; Hooper, N. M. ADAMs family members as amyloid precursor protein alpha-secretases. J. Neurosci. Res. 2003, 74 (3), 342-352.
    • (2003) J. Neurosci. Res , vol.74 , Issue.3 , pp. 342-352
    • Allinson, T.M.1    Parkin, E.T.2    Turner, A.J.3    Hooper, N.M.4
  • 13
    • 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.; Ball, M. J. Chemical characterization of A beta 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease. J. Biol. Chem. 1994, 269 (15), 10987-10990.
    • (1994) J. Biol. Chem , vol.269 , Issue.15 , pp. 10987-10990
    • 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
  • 14
    • 0030300022 scopus 로고    scopus 로고
    • The " nonamyloidogenic" p3 fragment (amyloid beta17-42) is a major constituent of Down's syndrome cerebellar preamyloid
    • Lalowski, M.; Golabek, A.; Lemere, C. A.; Selkoe, D. J.; Wisniewski, H. M.; Beavis, R. C.; Frangione, B.; Wisniewski, T. The " nonamyloidogenic" p3 fragment (amyloid beta17-42) is a major constituent of Down's syndrome cerebellar preamyloid. J. Biol. Chem. 1996, 271 (52), 33623-33631.
    • (1996) J. Biol. Chem , vol.271 , Issue.52 , pp. 33623-33631
    • Lalowski, M.1    Golabek, A.2    Lemere, C.A.3    Selkoe, D.J.4    Wisniewski, H.M.5    Beavis, R.C.6    Frangione, B.7    Wisniewski, T.8
  • 18
    • 11844260044 scopus 로고    scopus 로고
    • Structure and function of amyloid in Alzheimer's disease
    • Morgan, C.; Colombres, M.; Nunez, M. T.; Inestrosa, N. C. Structure and function of amyloid in Alzheimer's disease. Prog. Neurobiol. 2004, 74 (6), 323-349.
    • (2004) Prog. Neurobiol , vol.74 , Issue.6 , pp. 323-349
    • Morgan, C.1    Colombres, M.2    Nunez, M.T.3    Inestrosa, N.C.4
  • 19
    • 0037026929 scopus 로고    scopus 로고
    • Development of a novel diffusion-based method to estimate the size of the aggregated Abeta species responsible for neurotoxicity
    • Wang, S. S.; Becerra-Arteaga, A.; Good, T. A. Development of a novel diffusion-based method to estimate the size of the aggregated Abeta species responsible for neurotoxicity. Biotechnol. Bioeng. 2002, 80 (1), 50-59.
    • (2002) Biotechnol. Bioeng , vol.80 , Issue.1 , pp. 50-59
    • Wang, S.S.1    Becerra-Arteaga, A.2    Good, T.A.3
  • 20
    • 0028169925 scopus 로고
    • Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: Evidence that an initially deposited species is A beta 42(43)
    • Iwatsubo, T.; Odaka, A.; Suzuki, N.; Mizusawa, H.; Nukina, N.; Ihara, Y. Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is A beta 42(43). Neuron 1994, 13 (1), 45-53.
    • (1994) Neuron , vol.13 , Issue.1 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 21
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett, J. T.; Berger, E. P.; Lansbury, P. T., Jr. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 1993, 32 (18), 4693-4697.
    • (1993) Biochemistry , vol.32 , Issue.18 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 22
    • 0033061647 scopus 로고    scopus 로고
    • Andreasen, N.; Hesse, C.; Davidsson, P.; Minthon, L.; Wallin, A.; Winblad, B.; Vanderstichele, H.; Vanmechelen, E.; Blennow, K. Cerebrospinal fluid beta-amyloid(1-42) in Alzheimer disease: differences between early- and late-onset Alzheimer disease and stability during the course of disease. Arch. Neurol. 1999, 56 (6), 673-680.
    • Andreasen, N.; Hesse, C.; Davidsson, P.; Minthon, L.; Wallin, A.; Winblad, B.; Vanderstichele, H.; Vanmechelen, E.; Blennow, K. Cerebrospinal fluid beta-amyloid(1-42) in Alzheimer disease: differences between early- and late-onset Alzheimer disease and stability during the course of disease. Arch. Neurol. 1999, 56 (6), 673-680.
  • 24
    • 12144290725 scopus 로고    scopus 로고
    • Plasma levels of beta-amyloid(1-40), beta-amyloid(1-42), and total beta-amyloid remain unaffected in adult patients with hypercholesterolemia after treatment with statins
    • Hoglund, K.; Wiklund, O.; Vanderstichele, H.; Eikenberg, O.; Vanmechelen, E.; Blennow, K. Plasma levels of beta-amyloid(1-40), beta-amyloid(1-42), and total beta-amyloid remain unaffected in adult patients with hypercholesterolemia after treatment with statins. Arch. Neurol. 2004, 61 (3), 333-337.
    • (2004) Arch. Neurol , vol.61 , Issue.3 , pp. 333-337
    • Hoglund, K.1    Wiklund, O.2    Vanderstichele, H.3    Eikenberg, O.4    Vanmechelen, E.5    Blennow, K.6
  • 25
    • 33645775230 scopus 로고    scopus 로고
    • Determination of beta-Amyloid Peptide Signatures in Cerebrospinal Fluid Using Immunoprecipitation-Mass Spectrometry
    • Portelius, E.; Westman-Brinkmalm, A.; Zetterberg, H.; Blennow, K. Determination of beta-Amyloid Peptide Signatures in Cerebrospinal Fluid Using Immunoprecipitation-Mass Spectrometry. J. Proteome Res. 2006, 5 (4), 1010-1016.
    • (2006) J. Proteome Res , vol.5 , Issue.4 , pp. 1010-1016
    • Portelius, E.1    Westman-Brinkmalm, A.2    Zetterberg, H.3    Blennow, K.4
  • 26
    • 4644364868 scopus 로고    scopus 로고
    • Cerebrospinal fluid amyloid beta peptide patterns in Alzheimer's disease patients and nondemented controls depend on sample pretreatment: Indication of carrier-mediated epitope masking of amyloid beta peptides
    • Bibl, M.; Esselmann, H.; Otto, M.; Lewczuk, P.; Cepek, L.; Ruther, E.; Kornhuber, J.; Wiltfang, J. Cerebrospinal fluid amyloid beta peptide patterns in Alzheimer's disease patients and nondemented controls depend on sample pretreatment: indication of carrier-mediated epitope masking of amyloid beta peptides. Electrophoresis 2004, 25 (17), 2912-2918.
    • (2004) Electrophoresis , vol.25 , Issue.17 , pp. 2912-2918
    • Bibl, M.1    Esselmann, H.2    Otto, M.3    Lewczuk, P.4    Cepek, L.5    Ruther, E.6    Kornhuber, J.7    Wiltfang, J.8
  • 28
    • 18444393054 scopus 로고    scopus 로고
    • Highly conserved and disease-specific patterns of carboxyterminally truncated Abeta peptides 1-37/38/39 in addition to 1-40/42 in Alzheimer's disease and in patients with chronic neuroinflammation
    • Wiltfang, J.; Esselmann, H.; Bibl, M.; Smirnov, A.; Otto, M.; Paul, S.; Schmidt, B.; Klafki, H. W.; Maler, M.; Dyrks, T.; Bienert, M.; Beyermann, M.; Ruther, E.; Kornhuber, J. Highly conserved and disease-specific patterns of carboxyterminally truncated Abeta peptides 1-37/38/39 in addition to 1-40/42 in Alzheimer's disease and in patients with chronic neuroinflammation. J. Neurochem. 2002, 81 (3), 481-496.
    • (2002) J. Neurochem , vol.81 , Issue.3 , pp. 481-496
    • Wiltfang, J.1    Esselmann, H.2    Bibl, M.3    Smirnov, A.4    Otto, M.5    Paul, S.6    Schmidt, B.7    Klafki, H.W.8    Maler, M.9    Dyrks, T.10    Bienert, M.11    Beyermann, M.12    Ruther, E.13    Kornhuber, J.14
  • 30
    • 26844536197 scopus 로고    scopus 로고
    • Simple and robust two-layer matrix/sample preparation method for MALDI MS/MS analysis of peptides
    • Zheng, J.; Li, N.; Ridyard, M.; Dai, H.; Robbins, S. M.; Li, L. Simple and robust two-layer matrix/sample preparation method for MALDI MS/MS analysis of peptides. J. Proteome Res. 2005, 4 (5), 1709-1716.
    • (2005) J. Proteome Res , vol.4 , Issue.5 , pp. 1709-1716
    • Zheng, J.1    Li, N.2    Ridyard, M.3    Dai, H.4    Robbins, S.M.5    Li, L.6
  • 31
    • 0035816707 scopus 로고    scopus 로고
    • Degradation of the Alzheimer's amyloid beta peptide by endothelin-converting enzyme
    • Eckman, E. A.; Reed, D. K.; Eckman, C. B. Degradation of the Alzheimer's amyloid beta peptide by endothelin-converting enzyme. J. Biol. Chem. 2001, 276 (27), 24540-24548.
    • (2001) J. Biol. Chem , vol.276 , Issue.27 , pp. 24540-24548
    • Eckman, E.A.1    Reed, D.K.2    Eckman, C.B.3
  • 32
    • 0029061685 scopus 로고
    • Neutral endopeptidase can hydrolyze beta-amyloid(1-40) but shows no effect on beta-amyloid precursor protein metabolism
    • Howell, S.; Nalbantoglu, J.; Crine, P. Neutral endopeptidase can hydrolyze beta-amyloid(1-40) but shows no effect on beta-amyloid precursor protein metabolism. Peptides 1995, 16 (4), 647-652.
    • (1995) Peptides , vol.16 , Issue.4 , pp. 647-652
    • Howell, S.1    Nalbantoglu, J.2    Crine, P.3
  • 34
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced proteolysis of beta-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death
    • Leissring, M. A.; Farris, W.; Chang, A. Y.; Walsh, D. M.; Wu, X.; Sun, X.; Frosch, M. P.; Selkoe, D. J. Enhanced proteolysis of beta-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death. Neuron 2003, 40 (6), 1087-1093.
    • (2003) Neuron , vol.40 , Issue.6 , pp. 1087-1093
    • Leissring, M.A.1    Farris, W.2    Chang, A.Y.3    Walsh, D.M.4    Wu, X.5    Sun, X.6    Frosch, M.P.7    Selkoe, D.J.8
  • 35
    • 33845591072 scopus 로고    scopus 로고
    • Quantitative analysis of amyloid beta peptides in cerebrospinal fluid of Alzheimer's disease patients by immunoaffinity purification and stable isotope dilution liquid chromatography/negative electrospray ionization tandem mass spectrometry
    • Oe, T.; Ackermann, B. L.; Inoue, K.; Berna, M. J.; Garner, C. O.; Gelfanova, V.; Dean, R. A.; Siemers, E. R.; Holtzman, D. M.; Farlow, M. R.; Blair, I. A. Quantitative analysis of amyloid beta peptides in cerebrospinal fluid of Alzheimer's disease patients by immunoaffinity purification and stable isotope dilution liquid chromatography/negative electrospray ionization tandem mass spectrometry. Rapid Commun. Mass Spectrom. 2006, 20 (24), 3723-3735.
    • (2006) Rapid Commun. Mass Spectrom , vol.20 , Issue.24 , pp. 3723-3735
    • Oe, T.1    Ackermann, B.L.2    Inoue, K.3    Berna, M.J.4    Garner, C.O.5    Gelfanova, V.6    Dean, R.A.7    Siemers, E.R.8    Holtzman, D.M.9    Farlow, M.R.10    Blair, I.A.11
  • 36
    • 84987419408 scopus 로고
    • Proposal for a common nomenclature for sequence ions in mass spectra of peptides
    • Roepstorff, P.; Fohlman, J. Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed. Mass. Spectrom. 1984, 11 (11), 601.
    • (1984) Biomed. Mass. Spectrom , vol.11 , Issue.11 , pp. 601
    • Roepstorff, P.1    Fohlman, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.