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Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson's disease patients.

Araki K, Yagi N, Ikemoto Y, Yagi H, Choong CJ, Hayakawa H, Beck G, Sumi H, Fujimura H, Moriwaki T, Nagai Y, Goto Y, Mochizuki H - Sci Rep (2015)

Bottom Line: Thus, we used synchrotron Fourier transform infrared micro-spectroscopy (FTIRM) to analyse the fine structure of LBs in the brain of PD patients.Our results showed a shift in the infrared spectrum that indicates abundance of a β-sheet-rich structure in LBs.Also, 2D infrared mapping of LBs revealed that the content of the β-sheet structure is higher in the halo than in the core, and the core contains a large amount of proteins and lipids.

View Article: PubMed Central - PubMed

Affiliation: Department of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.

ABSTRACT
Lewy bodies (LBs), which mainly consist of α-synuclein (α-syn), are neuropathological hallmarks of patients with Parkinson's disease (PD). The fine structure of LBs is unknown, and LBs cannot be made artificially. Nevertheless, many studies have described fibrillisation using recombinant α-syn purified from E. coli. An extremely fundamental problem is whether the structure of LBs is the same as that of recombinant amyloid fibrils. Thus, we used synchrotron Fourier transform infrared micro-spectroscopy (FTIRM) to analyse the fine structure of LBs in the brain of PD patients. Our results showed a shift in the infrared spectrum that indicates abundance of a β-sheet-rich structure in LBs. Also, 2D infrared mapping of LBs revealed that the content of the β-sheet structure is higher in the halo than in the core, and the core contains a large amount of proteins and lipids.

No MeSH data available.


Related in: MedlinePlus

Typical visible and FTIR images of an SP in brain tissue derived from the patient who had AD pathology.Shown from left to right are a microscope image, the amount of total proteins, the proportion of β-sheet structures, and the amount of lipids. The colour bar indicates low (blue) to high (red) contents. The area in the visible image was scanned with 5-μm steps (16 × 8 pixels = 80 × 40 μm2). Scale bar, 10 μm. Protein-rich regions correspond well to the regions stained with Congo red. The proportion of β-sheet structures is high in the core of the plaque. Lipids exist around the core of the plaque.
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f4: Typical visible and FTIR images of an SP in brain tissue derived from the patient who had AD pathology.Shown from left to right are a microscope image, the amount of total proteins, the proportion of β-sheet structures, and the amount of lipids. The colour bar indicates low (blue) to high (red) contents. The area in the visible image was scanned with 5-μm steps (16 × 8 pixels = 80 × 40 μm2). Scale bar, 10 μm. Protein-rich regions correspond well to the regions stained with Congo red. The proportion of β-sheet structures is high in the core of the plaque. Lipids exist around the core of the plaque.

Mentions: Figure 4 shows 2D mapping of components in the FTIRM spectrum for a section of an SP that was analysed using the method of Liao et al.31 and Bousset et al.12. The protein map was obtained by the sum of the absorbance at 1540 cm−1 and 1640 cm−1, whereas that of the β-sheet was obtained by the proportion of the fitted peaks at 1628 cm−1 and 1680 cm−1 and lipids by the 2850 cm−1 peak. The amount of total proteins was high in the centre of the core of SPs (Fig. 4, Protein), and the proportion of β-sheet structures was also high in the centre of the core of SPs (Fig. 4, β-sheet). On the other hand, the amount of lipids was high around the core (Fig. 4, Lipid). The result of the distribution of lipids was consistent with a previous report31, which used a frozen section. Because the present study used a deparaffinised section, the result shows that the lipids in an SP were not lost during the deparaffinising process.


Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson's disease patients.

Araki K, Yagi N, Ikemoto Y, Yagi H, Choong CJ, Hayakawa H, Beck G, Sumi H, Fujimura H, Moriwaki T, Nagai Y, Goto Y, Mochizuki H - Sci Rep (2015)

Typical visible and FTIR images of an SP in brain tissue derived from the patient who had AD pathology.Shown from left to right are a microscope image, the amount of total proteins, the proportion of β-sheet structures, and the amount of lipids. The colour bar indicates low (blue) to high (red) contents. The area in the visible image was scanned with 5-μm steps (16 × 8 pixels = 80 × 40 μm2). Scale bar, 10 μm. Protein-rich regions correspond well to the regions stained with Congo red. The proportion of β-sheet structures is high in the core of the plaque. Lipids exist around the core of the plaque.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4664933&req=5

f4: Typical visible and FTIR images of an SP in brain tissue derived from the patient who had AD pathology.Shown from left to right are a microscope image, the amount of total proteins, the proportion of β-sheet structures, and the amount of lipids. The colour bar indicates low (blue) to high (red) contents. The area in the visible image was scanned with 5-μm steps (16 × 8 pixels = 80 × 40 μm2). Scale bar, 10 μm. Protein-rich regions correspond well to the regions stained with Congo red. The proportion of β-sheet structures is high in the core of the plaque. Lipids exist around the core of the plaque.
Mentions: Figure 4 shows 2D mapping of components in the FTIRM spectrum for a section of an SP that was analysed using the method of Liao et al.31 and Bousset et al.12. The protein map was obtained by the sum of the absorbance at 1540 cm−1 and 1640 cm−1, whereas that of the β-sheet was obtained by the proportion of the fitted peaks at 1628 cm−1 and 1680 cm−1 and lipids by the 2850 cm−1 peak. The amount of total proteins was high in the centre of the core of SPs (Fig. 4, Protein), and the proportion of β-sheet structures was also high in the centre of the core of SPs (Fig. 4, β-sheet). On the other hand, the amount of lipids was high around the core (Fig. 4, Lipid). The result of the distribution of lipids was consistent with a previous report31, which used a frozen section. Because the present study used a deparaffinised section, the result shows that the lipids in an SP were not lost during the deparaffinising process.

Bottom Line: Thus, we used synchrotron Fourier transform infrared micro-spectroscopy (FTIRM) to analyse the fine structure of LBs in the brain of PD patients.Our results showed a shift in the infrared spectrum that indicates abundance of a β-sheet-rich structure in LBs.Also, 2D infrared mapping of LBs revealed that the content of the β-sheet structure is higher in the halo than in the core, and the core contains a large amount of proteins and lipids.

View Article: PubMed Central - PubMed

Affiliation: Department of Neurology, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.

ABSTRACT
Lewy bodies (LBs), which mainly consist of α-synuclein (α-syn), are neuropathological hallmarks of patients with Parkinson's disease (PD). The fine structure of LBs is unknown, and LBs cannot be made artificially. Nevertheless, many studies have described fibrillisation using recombinant α-syn purified from E. coli. An extremely fundamental problem is whether the structure of LBs is the same as that of recombinant amyloid fibrils. Thus, we used synchrotron Fourier transform infrared micro-spectroscopy (FTIRM) to analyse the fine structure of LBs in the brain of PD patients. Our results showed a shift in the infrared spectrum that indicates abundance of a β-sheet-rich structure in LBs. Also, 2D infrared mapping of LBs revealed that the content of the β-sheet structure is higher in the halo than in the core, and the core contains a large amount of proteins and lipids.

No MeSH data available.


Related in: MedlinePlus