Ontology highlight
ABSTRACT:
SUBMITTER: Lanchec E
PROVIDER: S-EPMC5733603 | biostudies-literature | 2017 Dec
REPOSITORIES: biostudies-literature
Lanchec Erwan E Désilets Antoine A Béliveau François F Flamier Anthony A Mahmoud Shaimaa S Bernier Gilbert G Gris Denis D Leduc Richard R Lavoie Christine C
The Journal of biological chemistry 20171020 50
Recent studies have reported that many proteases, besides the canonical α-, β-, and γ-secretases, cleave the amyloid precursor protein (APP) and modulate β-amyloid (Aβ) peptide production. Moreover, specific APP isoforms contain Kunitz protease-inhibitory domains, which regulate the proteolytic activity of serine proteases. This prompted us to investigate the role of matriptase, a member of the type II transmembrane serine protease family, in APP processing. Using quantitative RT-PCR, we detecte ...[more]