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Microspectroscopy (μFTIR) reveals co-localization of lipid oxidation and amyloid plaques in human Alzheimer disease brains

Benseny-Cases, Núria; Klementieva, Oxana LU ; Cotte, Marine; Ferrer, Isidre and Cladera, Josep (2014) In Analytical Chemistry1949-01-01+01:00 86(24). p.54-12047
Abstract

Amyloid peptides are the main component of one of the characteristic pathological hallmarks of Alzheimer's disease (AD): senile plaques. According to the amyloid cascade hypothesis, amyloid peptides may play a central role in the sequence of events that leads to neurodegeneration. However, there are other factors, such as oxidative stress, that may be crucial for the development of the disease. In the present paper, we show that it is possible, by using Fourier tranform infrared (FTIR) microscopy, to co-localize amyloid deposits and lipid peroxidation in tissue slides from patients affected by Alzheimer's disease. Plaques and lipids can be analyzed in the same sample, making use of the characteristic infrared bands for peptide... (More)

Amyloid peptides are the main component of one of the characteristic pathological hallmarks of Alzheimer's disease (AD): senile plaques. According to the amyloid cascade hypothesis, amyloid peptides may play a central role in the sequence of events that leads to neurodegeneration. However, there are other factors, such as oxidative stress, that may be crucial for the development of the disease. In the present paper, we show that it is possible, by using Fourier tranform infrared (FTIR) microscopy, to co-localize amyloid deposits and lipid peroxidation in tissue slides from patients affected by Alzheimer's disease. Plaques and lipids can be analyzed in the same sample, making use of the characteristic infrared bands for peptide aggregation and lipid oxidation. The results show that, in samples from patients diagnosed with AD, the plaques and their immediate surroundings are always characterized by the presence of oxidized lipids. As for samples from non-AD individuals, those without amyloid plaques show a lower level of lipid oxidation than AD individuals. However, it is known that plaques can be detected in the brains of some non-AD individuals. Our results show that, in such cases, the lipid in the plaques and their surroundings display oxidation levels that are similar to those of tissues with no plaques. These results point to lipid oxidation as a possible key factor in the path that goes from showing the typical neurophatological hallmarks to suffering from dementia. In this process, the oxidative power of the amyloid peptide, possibly in the form of nonfibrillar aggregates, could play a central role.

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author
publishing date
type
Contribution to journal
publication status
published
keywords
Alzheimer Disease/pathology, Brain Chemistry, Humans, Immunohistochemistry/instrumentation, Lipids/chemistry, Oxidation-Reduction, Plaque, Amyloid/chemistry, Spectroscopy, Fourier Transform Infrared
in
Analytical Chemistry1949-01-01+01:00
volume
86
issue
24
pages
54 - 12047
publisher
The American Chemical Society
external identifiers
  • scopus:84918511645
ISSN
0003-2700
DOI
10.1021/ac502667b
language
English
LU publication?
no
id
f5737afa-b6b8-407c-899f-0d83a35f0413
date added to LUP
2018-11-01 13:15:12
date last changed
2019-07-09 04:36:00
@article{f5737afa-b6b8-407c-899f-0d83a35f0413,
  abstract     = {<p>Amyloid peptides are the main component of one of the characteristic pathological hallmarks of Alzheimer's disease (AD): senile plaques. According to the amyloid cascade hypothesis, amyloid peptides may play a central role in the sequence of events that leads to neurodegeneration. However, there are other factors, such as oxidative stress, that may be crucial for the development of the disease. In the present paper, we show that it is possible, by using Fourier tranform infrared (FTIR) microscopy, to co-localize amyloid deposits and lipid peroxidation in tissue slides from patients affected by Alzheimer's disease. Plaques and lipids can be analyzed in the same sample, making use of the characteristic infrared bands for peptide aggregation and lipid oxidation. The results show that, in samples from patients diagnosed with AD, the plaques and their immediate surroundings are always characterized by the presence of oxidized lipids. As for samples from non-AD individuals, those without amyloid plaques show a lower level of lipid oxidation than AD individuals. However, it is known that plaques can be detected in the brains of some non-AD individuals. Our results show that, in such cases, the lipid in the plaques and their surroundings display oxidation levels that are similar to those of tissues with no plaques. These results point to lipid oxidation as a possible key factor in the path that goes from showing the typical neurophatological hallmarks to suffering from dementia. In this process, the oxidative power of the amyloid peptide, possibly in the form of nonfibrillar aggregates, could play a central role. </p>},
  author       = {Benseny-Cases, Núria and Klementieva, Oxana and Cotte, Marine and Ferrer, Isidre and Cladera, Josep},
  issn         = {0003-2700},
  keyword      = {Alzheimer Disease/pathology,Brain Chemistry,Humans,Immunohistochemistry/instrumentation,Lipids/chemistry,Oxidation-Reduction,Plaque, Amyloid/chemistry,Spectroscopy, Fourier Transform Infrared},
  language     = {eng},
  month        = {12},
  number       = {24},
  pages        = {54--12047},
  publisher    = {The American Chemical Society},
  series       = {Analytical Chemistry1949-01-01+01:00},
  title        = {Microspectroscopy (μFTIR) reveals co-localization of lipid oxidation and amyloid plaques in human Alzheimer disease brains},
  url          = {http://dx.doi.org/10.1021/ac502667b},
  volume       = {86},
  year         = {2014},
}