Ontology highlight
ABSTRACT:
SUBMITTER: Wang YP
PROVIDER: S-EPMC1891218 | biostudies-literature | 2007 Jun
REPOSITORIES: biostudies-literature
Wang Y P YP Biernat J J Pickhardt M M Mandelkow E E Mandelkow E-M EM
Proceedings of the National Academy of Sciences of the United States of America 20070529 24
Tau is a highly soluble protein, yet it aggregates abnormally in Alzheimer's disease. Here, we address the question of proteolytic processing of tau and the nucleation of aggregates by tau fragments. We show in neuronal cell models that fragments of the repeat domain of tau containing mutations of FTDP17 (frontotemporal dementia with parkinsonism linked to chromosome 17), produced by endogenous proteases, can induce the aggregation of full-length tau. Fragments are generated by successive cleava ...[more]