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ABSTRACT: Background
A role for neutrophils in the pathogenesis of Alzheimer's disease (AD) is emerging. We previously showed that the neutrophil granule proteins cationic antimicrobial protein of 37 kDa (CAP37), cathepsin G (CG), and neutrophil elastase (NE) directly bind the amyloid-beta peptide Aβ1-42, a central player in AD pathogenesis. CAP37, CG, and NE are serine proteases that can cleave Aβ1-42 at different sites and with different catalytic activities.Objective
In this study, we compared the effects of these three proteins on Aβ1-42 fibrillation and neurotoxicity.Methods
Using mass spectrometry and in vitro aggregation assay, we found that NE and CG efficiently cleave Aβ1-42. This cleavage correlates well with the inhibitio
SUBMITTER: Kasus-Jacobi A
PROVIDER: S-EPMC9791948 | biostudies-literature | 2021
REPOSITORIES: biostudies-literature