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PMID: 16814100 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The various aggregation states of beta-amyloid 1-42 mediate different effects on oxidative stress, neurodegeneration, and BACE-1 expression.

Free radical biology & medicine ·Vol. 41 ·No. 2 ·2006-07-15 ·Pages 202-12

Tamagno E, Bardini P, Guglielmotto M, Danni O, Tabaton M

Abstract

The amyloid cascade hypothesis suggests that the insoluble and fibrillar form of beta-amyloid (A beta) may play a primary pathogenic role in Alzheimer disease at the molecular level. However, neither the rate of dementia nor the extent of neuronal change seems to correlate with the levels of amyloidotic plaques (i.e., aggregated/fibrillar A beta). Recent evidence suggests, however, that neurotoxicity may be exerted also by rather small soluble aggregates of A beta, including oligomers. To characterize the mechanisms underlying toxicity mediated by the various aggregation states of A beta peptides is then a major goal of research. In this work we investigated the effects of fibrillar, prefibrillar, and oligomeric A beta(1-42) on the induction of oxidative stress, cell death, and BACE-1 expression in NT2 neuronal cells. We found that prefibrillar and oligomeric A beta(1-42) resulted in a more dramatic increase in the oxidative stress markers 4-hydroxynonenal and hydrogen peroxide compared to fibrillar A beta(1-42). Moreover, increased oxidative stress levels also resulted in a more rapid and significant induction of both apoptotic and necrotic neuronal cell death. Accordingly, fibrillar A beta(1-42), but not the soluble nonfibrillar forms, was the only condition able to up-regulate BACE-1 expression and activity.

MeSH Terms
Amyloid Precursor Protein Secretases/metabolism Amyloid beta-Peptides/metabolism Aspartic Acid Endopeptidases/metabolism Base Sequence Cell Death Cell Line DNA Primers Humans Oxidative Stress Peptide Fragments/metabolism Protein Binding Reverse Transcriptase Polymerase Chain Reaction
Chemicals
Amyloid beta-Peptides DNA Primers Peptide Fragments amyloid beta-protein (1-42) Amyloid Precursor Protein Secretases Aspartic Acid Endopeptidases BACE1 protein, human
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Tamagno Elena
General Pathology Section, Department of Experimental Medicine and Oncology, University of Turin, Corso Raffaello 30, 10125 Turin, Italy. elena.tamagno@unito.it
Bardini Paola
Guglielmotto Michela
Danni Oliviero
Tabaton Massimo
Article Info
Journal
Free radical biology & medicine
Abbr.
Free Radic Biol Med
ISSN
0891-5849
Published
2006-07-15
Epub
2006-00-14
Pages
202-12
Language
English
Region
United States
NLM ID
8709159
Subset
IM
Corrections
CommentIn
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