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Unraveling amyloid toxicity pathway in NIH3T3 cells by a combined proteomic and1H-NMR metabonomic approach
- Source :
- Journal of cellular physiology, 228 (2013): 1359–1367. doi:10.1002/jcp.24294, info:cnr-pdr/source/autori:Vilasi A; Vilasi S; Romano R; Acernese F; Barone F; Balestrieri ML; Maritato R; Irace G; Sirangelo I/titolo:Unraveling amyloid toxicity pathway in NIH3T3 cells by a combined proteomic and 1H-NMR metabonomic approach/doi:10.1002%2Fjcp.24294/rivista:Journal of cellular physiology (Print)/anno:2013/pagina_da:1359/pagina_a:1367/intervallo_pagine:1359–1367/volume:228
- Publication Year :
- 2013
- Publisher :
- Wiley, 2013.
-
Abstract
- A range of debilitating human diseases is known to be associated with the formation of stable highly organized protein aggregates known as amyloid fibrils. The early prefibrillar aggregates behave as cytotoxic agents and their toxicity appears to result from an intrinsic ability to impair fundamental cellular processes by interacting with cellular membranes, causing oxidative stress and increase in free Ca2+ that lead to apoptotic or necrotic cell death. However, specific signaling pathways that underlie amyloid pathogenicity remain still unclear. This work aimed to clarify cell impairment induced by amyloid aggregated. To this end, we used a combined proteomic and one-dimensional 1H-NMR approach on NIH-3T3 cells exposed to prefibrillar aggregates from the amyloidogenic apomyoglobin mutant W7FW14F. The results indicated that cell exposure to prefibrillar aggregates induces changes of the expression level of proteins and metabolites involved in stress response. The majority of the proteins and metabolites detected are reported to be related to oxidative stress, perturbation of calcium homeostasis, apoptotic and survival pathways, and membrane damage. In conclusion, the combined proteomic and 1H-NMR metabonomic approach, described in this study, contributes to unveil novel proteins and metabolites that could take part to the general framework of the toxicity induced by amyloid aggregates. These findings offer new insights in therapeutic and diagnostic opportunities. J. Cell. Physiol. 228: 1359–1367, 2013. © 2012 Wiley Periodicals, Inc.
- Subjects :
- Proteomics
Amyloid
Magnetic Resonance Spectroscopy
Physiology
Blotting, Western
Clinical Biochemistry
Cell
Protein aggregation
Biology
medicine.disease_cause
Mice
medicine
Animals
Metabolomics
metabonomics
Electrophoresis, Gel, Two-Dimensional
Cytotoxicity
apoptosis
Reproducibility of Results
Cell Biology
Fibroblasts
amyloid toxicity
proteomics
Cell biology
medicine.anatomical_structure
Biochemistry
Apoptosis
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Toxicity
NIH 3T3 Cells
Signal transduction
Oxidative stress
Signal Transduction
Subjects
Details
- ISSN :
- 00219541
- Volume :
- 228
- Database :
- OpenAIRE
- Journal :
- Journal of Cellular Physiology
- Accession number :
- edsair.doi.dedup.....8ade2068e787c5a2cb7f2fc0dfa383cc