β-amyloid peptide vaccination results in marked changes in serum and brain Aβ levels in APPswe/PS1ΔE9 mice, as detected by SELDI-TOF-based ProteinChip® technology

Anne K. Vehmas, Juan C. Troncoso, David R. Borchelt, Donald L. Price, Diane McCarthy, Marsha Wills-Karp, Marilyn J. Peper, Gay Rudow, Jackie Luyinbazi, Lawrence T. Siew

Research output: Contribution to journalArticle

Abstract

Although the pathogenesis of Alzheimer's disease (AD) is not fully understood, growing evidence indicates that the deposition of β-amyloid (Aβ) and the local reactions of various cell types to this protein play major roles in the development of the disease. Immunization with the Aβ 1-42 peptide has been reported to decrease Aβ deposits in the brains of mutant amyloid precursor protein (APP/V717F) transgenic (tg) mice (Schenk et al. Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 1999;400:173-177). We have replicated this finding in APPswe/PS1ΔE9 tg mice, which also develop Aβ deposits in the brain. The immunized animals developed high titers of antibodies against Aβ 1-42 in serum, and Aβ deposits in the brains were significantly reduced. Using surface-enhanced laser desorption/ionization (SELDI) mass spectrometry and ProteinChip® technology, we detected trends toward increased soluble Aβ peptide in the brain and a decrease in assayable Aβ peptide in the serum of immunized compared with control animals. This last finding raises the possibility that anti-Aβ antibodies in the periphery sequester Aβ peptides or target them for degradation and in this way contribute to the enhanced Aβ clearance from the brain in immunized animals.

Original languageEnglish (US)
Pages (from-to)713-721
Number of pages9
JournalDNA and Cell Biology
Volume20
Issue number11
DOIs
StatePublished - Nov 1 2001

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

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