Quantitative analysis of amyloid-β peptides in cerebrospinal fluid using immunoprecipitation and MALDI-Tof mass spectrometry

Valentina Gelfanova, Richard E. Higgs, Robert A. Dean, David M. Holtzman, Martin R. Farlow, Eric R. Siemers, Amechand Boodhoo, Yue Wei Qian, Xiaohua He, Zhaoyan Jin, Deborah I. Fisher, Karen I. Cox, John E. Hale

Research output: Contribution to journalArticle

30 Scopus citations

Abstract

Immunoprecipitation (IP) combined with matrix-assisted laser desorption ionization (MALDI) time of flight (Tof) mass spectrometry has been used to develop quantitative assays for amyloid-β (Aβ) peptides in cerebrospinal fluid (CSF). Inclusion of 15N labelled standard peptides allows for absolute quantification of multiple Aβ isoforms in individual samples. Characterization of variability associated with all steps of the assay indicated that the IP step is the single largest contributor to overall variability. Optimization of the assay resulted in overall coefficient of variation ≤8% with high agreement to an Aβ1-40 and Aβ1-42 ELISA assay. Application of the MALDI-Tof assay to CSF obtained from healthy volunteers and Alzheimer's disease patients indicated statistically significant 43% lower levels of Aβ1-42 in the AD group (P = 0.0025).

Original languageEnglish
Pages (from-to)149-158
Number of pages10
JournalBriefings in Functional Genomics and Proteomics
Volume6
Issue number2
DOIs
StatePublished - Jun 1 2007

Keywords

  • Alzheimers disease
  • Amyloid-β peptide
  • MALDI-Tof mass spectrometry
  • multiplexed analysis

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    Gelfanova, V., Higgs, R. E., Dean, R. A., Holtzman, D. M., Farlow, M. R., Siemers, E. R., Boodhoo, A., Qian, Y. W., He, X., Jin, Z., Fisher, D. I., Cox, K. I., & Hale, J. E. (2007). Quantitative analysis of amyloid-β peptides in cerebrospinal fluid using immunoprecipitation and MALDI-Tof mass spectrometry. Briefings in Functional Genomics and Proteomics, 6(2), 149-158. https://doi.org/10.1093/bfgp/elm010