Molecular imaging of amyloid beta peptides in mouse brain sections using mass spectrometry

Anal Biochem. 2002 Dec 1;311(1):33-9. doi: 10.1016/s0003-2697(02)00386-x.

Abstract

A method is presented for direct spatial analysis of amyloid beta peptides in biological tissue sections. The technique takes advantage of the very high sensitivity of matrix-assisted laser desorption/ionization mass spectrometry and is implemented on a commercial instrument with modifications to only a few components and the software. With this setup, hundreds of molecular images can be generated simultaneously and within just a few minutes. The current features are an instrumental resolution of 50 microm and a sensitivity down to the attomol range. This new technology is applied to the study of amyloid beta peptide distribution in brain sections from mice, showing features reminiscent of Alzheimer's disease.

MeSH terms

  • Alzheimer Disease / genetics
  • Alzheimer Disease / metabolism
  • Amino Acid Sequence
  • Amyloid Neuropathies, Familial / genetics
  • Amyloid Neuropathies, Familial / metabolism
  • Amyloid beta-Peptides / analysis*
  • Amyloid beta-Peptides / metabolism
  • Amyloid beta-Peptides / ultrastructure
  • Amyloid beta-Protein Precursor / genetics
  • Amyloid beta-Protein Precursor / metabolism
  • Animals
  • Benzothiazoles
  • Blotting, Western
  • Brain / metabolism*
  • Brain Chemistry
  • Frozen Sections
  • Humans
  • Image Processing, Computer-Assisted / methods*
  • Mice
  • Mice, Transgenic
  • Molecular Sequence Data
  • Reproducibility of Results
  • Sensitivity and Specificity
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods*
  • Thiazoles / chemistry
  • Thiazoles / metabolism
  • Tissue Distribution

Substances

  • Amyloid beta-Peptides
  • Amyloid beta-Protein Precursor
  • Benzothiazoles
  • Thiazoles
  • thioflavin T