Wild-type and mutated nicastrins do not display aminopeptidase M- and B-like activities

Anissa Fergani, G. Yu, Peter St. George-Hyslop, Frédéric Checler

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Nicastrin is a recently discovered protein interacting with presenilins and the β-amyloid precursor protein, the proteins playing key roles in Alzheimer's disease and which, when mutated, appear responsible for early-onset familial forms of Alzheimer's disease. Nicastrin was reported to modulate β-amyloid production, a phenotype affected differently by missense mutations or deletions of a conserved hydrophilic domain. In addition to such a function, nicastrin was recently suggested to possess putative catalytic activity based on its sequence homology with enzymes of the aminopeptidase family. We set up stably transfected human HEK293 cells expressing either wild-type or mutated nicastrins and we show that these proteins do not exhibit aminopeptidase M- and B-like activities.

Original languageEnglish (US)
Pages (from-to)678-680
Number of pages3
JournalBiochemical and Biophysical Research Communications
Volume289
Issue number3
DOIs
StatePublished - Dec 7 2001

Keywords

  • Alzheimer's disease
  • Aminopeptidases
  • Mutant proteins
  • Nicastrin
  • Presenilins
  • Transfectants

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Wild-type and mutated nicastrins do not display aminopeptidase M- and B-like activities'. Together they form a unique fingerprint.

  • Cite this