Preparing your results

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Abeta42 is essential for parenchymal and vascular amyloid deposition in mice.

Considerable circumstantial evidence suggests that Abeta42 is the initiating molecule in Alzheimer's disease (AD) pathogenesis. However, the absolute requirement for Abeta42 for amyloid deposition has never been demonstrated in vivo. We have addressed this by developing transgenic models that express Abeta1-40 or Abeta1-42 in the absence of human amyloid beta protein precursor (APP) overexpression. Mice expressing high levels of Abeta1-40 do not develop overt amyloid pathology. In contrast, mice expressing lower levels of Abeta1-42 accumulate insoluble Abeta1-42 and develop compact amyloid plaques, congophilic amyloid angiopathy (CAA), and diffuse Abeta deposits. When mice expressing Abeta1-42 are crossed with mutant APP (Tg2576) mice, there is also a massive increase in amyloid deposition. These data establish that Abeta1-42 is essential for amyloid deposition in the parenchyma and also in vessels.

Pubmed ID: 16039562


  • McGowan E
  • Pickford F
  • Kim J
  • Onstead L
  • Eriksen J
  • Yu C
  • Skipper L
  • Murphy MP
  • Beard J
  • Das P
  • Jansen K
  • Delucia M
  • Lin WL
  • Dolios G
  • Wang R
  • Eckman CB
  • Dickson DW
  • Hutton M
  • Hardy J
  • Golde T



Publication Data

July 21, 2005

Associated Grants

  • Agency: NCI NIH HHS, Id: CA88325
  • Agency: NIA NIH HHS, Id: R01 AG022595-01
  • Agency: NIA NIH HHS, Id: R01 AG022595-02

Mesh Terms

  • Age Factors
  • Amyloid beta-Peptides
  • Amyloid beta-Protein Precursor
  • Animals
  • Blood Vessels
  • Blotting, Northern
  • Blotting, Western
  • Brain
  • Cerebral Amyloid Angiopathy
  • Enzyme-Linked Immunosorbent Assay
  • Female
  • Glial Fibrillary Acidic Protein
  • Humans
  • Immunohistochemistry
  • Immunoprecipitation
  • In Situ Hybridization
  • Male
  • Mass Spectrometry
  • Mice
  • Mice, Transgenic
  • Microscopy, Electron, Transmission
  • Mutation
  • Peptide Fragments
  • Pia Mater
  • Plaque, Amyloid
  • Thiazoles