Transgenic Rat and In-Vitro Studies of β-Amyloid Precursor Protein Processing

  • Kevin M. Felsenstein
  • Allison Treloar
  • Janet M. Roome
  • Lisa W. Hunihan
  • Kim M. Ingalls
  • Susan B. Roberts
Part of the Advances in Behavioral Biology book series (ABBI, volume 44)


The brains of individuals afflicted with Alzheimer’s Disease (AD) are characterized pathologically by cortical atrophy, deposition of senile plaques (i.e. ß-amyloid protein), and the formation of neurofibrillary tangles. The etiology of AD is complex and multifactorial; including evidence for genetic heterogeneity. However, genetic studies have clearly shown that several different mutations in the ß-APP gene on chromosome 21 are unambiguously pathogenic for AD in a subset of early-onset families.1–9 The mechanism by which ß-protein is generated and formed into amyloid in-vivo have yet to be defined. Aside from the genetic data, putative pathological mechanisms may include overexpression of ß-APP, as suggested by trisomy 21 or Down’s Syndrome individuals; or alterations in the proteolytic processing pathways, currently being defined in-vitro by a number of laboratories. To date no animal model exists that can recapitulate the pathological cascade of AD.


Amyloid Precursor Protein Mock Transfected Cell Alzheimer Amyloid Precursor Protein Carboxy Terminal Region Human Placental Alkaline Phosphatase 
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Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Kevin M. Felsenstein
    • 1
  • Allison Treloar
    • 1
  • Janet M. Roome
    • 1
  • Lisa W. Hunihan
    • 1
  • Kim M. Ingalls
    • 1
  • Susan B. Roberts
    • 1
  1. 1.Bristol-Myers Squibb Pharmaceutical Research InstituteCNS-Drug DiscoveryWallingfordUSA

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