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Amyloid peptides in different assembly states and related effects on isolated and cellular proteasomes.
Brain Res. 2008 May 13; 1209:8-18.BR

Abstract

The role of amyloid-beta protein (Abeta) in the pathogenesis of Alzheimer's disease (AD) has been widely investigated and amyloid aggregates are considered a major cause of neuronal dysfunction. Increasing evidence has identified a correlation between this protein and the proteasome, the cellular proteolytic machinery, in particular the ubiquitin-proteasome system. The 20S proteasome is the catalytic core of a complex, known as 26S proteasome, and is the main responsible for the clearance of misfolded and oxidized proteins. In this work we have investigated the effects of different assembly states of two major amyloid peptides, Abeta (1-40) and Abeta (1-42) on the 20S proteasome functionality and on the ubiquitin-dependent pathway of protein degradation. In particular, we have tested proteasome activities after Abeta treatment on purified 20S complexes and on lysates of a human neuroblastoma cell line. Our findings show a significant decrease in proteasome activity, more evident in cell lysates than in isolated complexes, and an increased amount of ubiquitin-protein conjugates and of a known proteasome substrate (p27). Furthermore, the altered proteasome functionality is not associated with a decrease in cell viability, but is linked with increased levels of protein oxidation.

Authors+Show Affiliations

Department of Molecular, Cellular and Animal Biology, University of Camerino, 62032 Camerino (MC), Italy. valentina.cecarini@unicam.itNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18400214

Citation

Cecarini, Valentina, et al. "Amyloid Peptides in Different Assembly States and Related Effects On Isolated and Cellular Proteasomes." Brain Research, vol. 1209, 2008, pp. 8-18.
Cecarini V, Bonfili L, Amici M, et al. Amyloid peptides in different assembly states and related effects on isolated and cellular proteasomes. Brain Res. 2008;1209:8-18.
Cecarini, V., Bonfili, L., Amici, M., Angeletti, M., Keller, J. N., & Eleuteri, A. M. (2008). Amyloid peptides in different assembly states and related effects on isolated and cellular proteasomes. Brain Research, 1209, 8-18. https://doi.org/10.1016/j.brainres.2008.03.003
Cecarini V, et al. Amyloid Peptides in Different Assembly States and Related Effects On Isolated and Cellular Proteasomes. Brain Res. 2008 May 13;1209:8-18. PubMed PMID: 18400214.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Amyloid peptides in different assembly states and related effects on isolated and cellular proteasomes. AU - Cecarini,Valentina, AU - Bonfili,Laura, AU - Amici,Manila, AU - Angeletti,Mauro, AU - Keller,Jeffrey N, AU - Eleuteri,Anna Maria, Y1 - 2008/03/18/ PY - 2007/12/06/received PY - 2008/02/25/revised PY - 2008/03/03/accepted PY - 2008/4/11/pubmed PY - 2008/8/12/medline PY - 2008/4/11/entrez SP - 8 EP - 18 JF - Brain research JO - Brain Res. VL - 1209 N2 - The role of amyloid-beta protein (Abeta) in the pathogenesis of Alzheimer's disease (AD) has been widely investigated and amyloid aggregates are considered a major cause of neuronal dysfunction. Increasing evidence has identified a correlation between this protein and the proteasome, the cellular proteolytic machinery, in particular the ubiquitin-proteasome system. The 20S proteasome is the catalytic core of a complex, known as 26S proteasome, and is the main responsible for the clearance of misfolded and oxidized proteins. In this work we have investigated the effects of different assembly states of two major amyloid peptides, Abeta (1-40) and Abeta (1-42) on the 20S proteasome functionality and on the ubiquitin-dependent pathway of protein degradation. In particular, we have tested proteasome activities after Abeta treatment on purified 20S complexes and on lysates of a human neuroblastoma cell line. Our findings show a significant decrease in proteasome activity, more evident in cell lysates than in isolated complexes, and an increased amount of ubiquitin-protein conjugates and of a known proteasome substrate (p27). Furthermore, the altered proteasome functionality is not associated with a decrease in cell viability, but is linked with increased levels of protein oxidation. SN - 0006-8993 UR - https://www.unboundmedicine.com/medline/citation/18400214/Amyloid_peptides_in_different_assembly_states_and_related_effects_on_isolated_and_cellular_proteasomes_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-8993(08)00613-6 DB - PRIME DP - Unbound Medicine ER -