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Protease Nexin 1 Immunoreactivity in Senile Plaques in Alzheimer Disease and Aged Brain

  • Yoshio Namba
  • Kazuhiko Ikeda
  • Masanori Tomonaga
Part of the Advances in Behavioral Biology book series (ABBI, volume 38A)

Abstract

Amyloid ß -protein is deposited in senile plaques of Alzheimer and Down syndrome patient1. This ß -protein is now known to be derived from a larger precursor protein (APP) 2. However, the mechanism whereby the amyloid proteins are deposited is thus far not clarified. The recent finding that the APP contains a new domain with structural similarity to the Kunitz family of protease inhibitor3–5 has raised the possibility that an imbalance of protease-protease inhibitor interaction is involved in the aberrant degradation of APP, which may lead to formation of amyloid ß -protein. In fact, this domain does have protease inhibitor activity3, and the amount of two larger versions of APP with a protease inhibitor domain appears to be elevated in Alzheimer brain. Recently, another completely unrelated protease inhibitor, al-antichymotrypsin, was demonstrated to be closely associated with amyloid fibrils6. This fact also supports the possibility that the imbalance between protease and protease inhibitor brings about the anomalous degradation of the APP7.

Keywords

Down Syndrome Alzheimer Brain Senile Plaque Aged Brain Amyloid Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Yoshio Namba
    • 1
  • Kazuhiko Ikeda
    • 1
  • Masanori Tomonaga
    • 1
  1. 1.Department of Neuropathology Institute of Brain Research Faculty of MedicineUniversity of TokyoBunkyo-ku Tokyo 113Japan

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