Dipeptidyl peptidase 4 contributes to Alzheimer's disease-like defects in a mouse model and is increased in sporadic Alzheimer's disease brains.

ABSTRACT: The amyloid cascade hypothesis, which proposes a prominent role for full-length amyloid β peptides in Alzheimer's disease, is currently being questioned. In addition to full-length amyloid β peptide, several N-terminally truncated fragments of amyloid β peptide could well contribute to Alzheimer's disease setting and/or progression. Among them, pyroGlu3-amyloid β peptide appears to be one of the main components of early anatomical lesions in Alzheimer's disease-affected brains. Little is known about the proteolytic activities that could account for the N-terminal truncations of full-length amyloid β, but they appear as the rate-limiting enzymes yielding the Glu3-amyloid β peptide sequence that undergoes subsequent cyclization by glutaminyl cyclase, thereby yielding pyroGlu3-amyloid β. Here

SUBMITTER: Valverde A 

PROVIDER: S-EPMC8334387 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature