Isolation and characterization of mammalian D-aspartyl endopeptidase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2006-10-06

AUTHORS

T. Kinouchi, H. Nishio, Y. Nishiuchi, M. Tsunemi, K. Takada, T. Hamamoto, Y. Kagawa, N. Fujii

ABSTRACT

Summary.The accumulation of D-isomers of aspartic acid (D-Asp) in proteins during aging has been implicated in the pathogenesis of Alzheimer’s disease (AD), cataracts and arteriosclerosis. Here, we identified a specific lactacystin-sensitive endopeptidase that cleaves the D-Asp-containing protein and named it D-aspartyl endopeptidase (DAEP). DAEP has a multi-complex structure (MW: 600 kDa) and is localized in the inner mitochondrial membrane. However, DAEP activity was not detected in E. coli, S. cerevisiae, and C. elegans. A specific inhibitor for DAEP, i-DAEP: (benzoyl-L-Arg-L-His-[D-Asp]-CH2Cl; MW: 563.01), was newly synthesized and inhibited DAEP activity (IC50, 3 µM), a factor of ten greater than lactacystin on DAEP. On the other hand, i-DAEP did not inhibit either the 20S or 26S proteasome. And we identified succinate dehydrogenase and glutamate dehydrogenase 1 as components of DAEP by affinity label using biotinylated i-DAEP. In the long life span of mammals, DAEP may serve as a scavenger against accumulation of racemized proteins in aging. Insights into DAEP will provide the foundation for developing treatments of diseases, such as AD, in which accumulation of D-Asp-containing proteins are implicated. More... »

PAGES

79-85

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00726-006-0348-4

DOI

http://dx.doi.org/10.1007/s00726-006-0348-4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1033714499

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17021656


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