APP processing and the APP-KPI domain involvement in the amyloid cascade

M. Menéndez-González, P. Pérez-Pinera, M. Martínez-Rivera, M. T. Calatayud, B. Blázquez Menes

Research output: Contribution to journalShort surveypeer-review

Abstract

Alternative APP mRNA splicing can generate isoforms of APP containing a Kunitz protease inhibitor (KPI) domain. KPI is one of the main serine protease inhibitors. Protein and mRNA KPI(+)APP levels are elevated in Alzheimer's disease (AD) brain and are associated with increased amyloid beta deposition. In the last years increasing evidence on multiple points in the amyloid cascade where KPI(+)APP is involved has been accumulated, admitting an outstanding position in the pathogenesis of AD to the KPI domain. This review focuses on the APP processing, the molecular activity of KPI and its physiological and pathological roles and the KPI involvement in the amyloid cascade through the nerve growth factor, the lipoprotein receptor-related protein, the tumor necrosis factor-alpha converting enzyme and the Notch1 protein.

Original languageEnglish (US)
Pages (from-to)277-283
Number of pages7
JournalNeurodegenerative Diseases
Volume2
Issue number6
DOIs
StatePublished - May 1 2006
Externally publishedYes

Keywords

  • Amyloid beta precursor protein
  • Kunitz protease inhibitor
  • Lipoprotein receptor-related protein
  • Nerve growth factor
  • Notch1
  • Tumor necrosis factor-alpha- converting enzyme

ASJC Scopus subject areas

  • Clinical Neurology
  • Neurology

Fingerprint Dive into the research topics of 'APP processing and the APP-KPI domain involvement in the amyloid cascade'. Together they form a unique fingerprint.

Cite this