Preserved structural property after amplification of alpha-synuclein aggregates from brains of synucleinopathies
神経変性疾患で蓄積する異常タンパク質の1つであるα-synは、PD、DLBおよびMSAの脳内に主に蓄積する。DLBやMSAの患者脳から解析可能な量のα-syn凝集体の増幅に成功した。増幅前後の凝集体のプロテイナーゼKコアのMS分析結果から、増幅による変化はないもののマウスとヒトのα-syn凝集体で切断パターンが異なることがわかった。これらの結果から、この方法が神経変性疾患の異常タンパク質研究の発展に貢献できることを示唆した。 === Pathological proteins related to neurodegenerative diseases are misfolded, aggreg...
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ndltd-doshisha.ac.jp-oai-doshisha.repo.nii.ac.jp-000016242021-11-23T05:06:09Z Preserved structural property after amplification of alpha-synuclein aggregates from brains of synucleinopathies en alpha-synuclein synucleinopathy seeding reaction protein misfolding cyclic amplification(PMCA) mass spectrometry https://doshisha.repo.nii.ac.jp/?action=repository_uri&item_id=1624 http://id.nii.ac.jp/1707/00001616/ Thesis or Dissertation シヌクレイノパチー脳におけるα-シヌクレイン凝集体の増幅と増幅後の構造特性 シヌクレイノパチー ノウ ニオケル α-シヌクレイン ギョウシュウタイ ノ ゾウフク ト ゾウフクゴ ノ コウゾウ トクセイ 吉永 早希 Saki Yoshinaga 脳科学研究科 Graduate School of Brain Science 神経変性疾患で蓄積する異常タンパク質の1つであるα-synは、PD、DLBおよびMSAの脳内に主に蓄積する。DLBやMSAの患者脳から解析可能な量のα-syn凝集体の増幅に成功した。増幅前後の凝集体のプロテイナーゼKコアのMS分析結果から、増幅による変化はないもののマウスとヒトのα-syn凝集体で切断パターンが異なることがわかった。これらの結果から、この方法が神経変性疾患の異常タンパク質研究の発展に貢献できることを示唆した。 Pathological proteins related to neurodegenerative diseases are misfolded, aggregating to form amyloid fibrils. One of the pathological proteins, α-syn, accumulates in the brains of PD, DLB and MSA. We first performed amplification of α-syn aggregates. We successfully amplified enough α-syn aggregates derived from α-syncleinopathies. We found that the MS analysis results of proteinase K-resistant cores of the aggregates before and after the amplification differ between mouse and human α-syn aggregates. The results suggest that structural properties of amplified α-syn fibrils are preserved and these methods can be applicable in the study of pathological proteins of the neurodegenerative disorders. BC02444353 https://doors.doshisha.ac.jp/opac/opac_link/bibid/BB13127448/?lang=0 application/pdf https://doshisha.repo.nii.ac.jp/?action=repository_action_common_download&item_id=1624&item_no=1&attribute_id=21&file_no=1 https://doshisha.repo.nii.ac.jp/?action=repository_action_common_download&item_id=1624&item_no=1&attribute_id=21&file_no=2 博士(理学) Doctor of Philosophy in Science 同志社大学 Doshisha University 2020-03-22 34310甲第1095号 |
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alpha-synuclein synucleinopathy seeding reaction protein misfolding cyclic amplification(PMCA) mass spectrometry |
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alpha-synuclein synucleinopathy seeding reaction protein misfolding cyclic amplification(PMCA) mass spectrometry 吉永 早希 Saki Yoshinaga Preserved structural property after amplification of alpha-synuclein aggregates from brains of synucleinopathies |
description |
神経変性疾患で蓄積する異常タンパク質の1つであるα-synは、PD、DLBおよびMSAの脳内に主に蓄積する。DLBやMSAの患者脳から解析可能な量のα-syn凝集体の増幅に成功した。増幅前後の凝集体のプロテイナーゼKコアのMS分析結果から、増幅による変化はないもののマウスとヒトのα-syn凝集体で切断パターンが異なることがわかった。これらの結果から、この方法が神経変性疾患の異常タンパク質研究の発展に貢献できることを示唆した。 === Pathological proteins related to neurodegenerative diseases are misfolded, aggregating to form amyloid fibrils. One of the pathological proteins, α-syn, accumulates in the brains of PD, DLB and MSA. We first performed amplification of α-syn aggregates. We successfully amplified enough α-syn aggregates derived from α-syncleinopathies. We found that the MS analysis results of proteinase K-resistant cores of the aggregates before and after the amplification differ between mouse and human α-syn aggregates. The results suggest that structural properties of amplified α-syn fibrils are preserved and these methods can be applicable in the study of pathological proteins of the neurodegenerative disorders. === 博士(理学) === Doctor of Philosophy in Science === 同志社大学 === Doshisha University |
author |
吉永 早希 Saki Yoshinaga |
author_facet |
吉永 早希 Saki Yoshinaga |
author_sort |
吉永 早希 |
title |
Preserved structural property after amplification of alpha-synuclein aggregates from brains of synucleinopathies |
title_short |
Preserved structural property after amplification of alpha-synuclein aggregates from brains of synucleinopathies |
title_full |
Preserved structural property after amplification of alpha-synuclein aggregates from brains of synucleinopathies |
title_fullStr |
Preserved structural property after amplification of alpha-synuclein aggregates from brains of synucleinopathies |
title_full_unstemmed |
Preserved structural property after amplification of alpha-synuclein aggregates from brains of synucleinopathies |
title_sort |
preserved structural property after amplification of alpha-synuclein aggregates from brains of synucleinopathies |
publishDate |
2020 |
url |
https://doshisha.repo.nii.ac.jp/?action=repository_uri&item_id=1624 http://id.nii.ac.jp/1707/00001616/ https://doshisha.repo.nii.ac.jp/?action=repository_action_common_download&item_id=1624&item_no=1&attribute_id=21&file_no=1 https://doshisha.repo.nii.ac.jp/?action=repository_action_common_download&item_id=1624&item_no=1&attribute_id=21&file_no=2 |
work_keys_str_mv |
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