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  1. 学術雑誌掲載済論文
  2. 洋雑誌

Free tyrosine and tyrosine-rich peptide-dependent superoxide generation catalyzed by a copper-binding, threonine-rich neurotoxic peptide derived from prion protein

https://kitami-it.repo.nii.ac.jp/records/8868
f4597088-4385-478f-b28a-b14f21b62e33
名前 / ファイル ライセンス アクション
Int Int J Biol Sci 2009, 5(1).53-63 (421.9 kB)
license.icon
Item type 学術雑誌論文 / Journal Article(1)
公開日 2019-12-17
タイトル
言語 en
タイトル Free tyrosine and tyrosine-rich peptide-dependent superoxide generation catalyzed by a copper-binding, threonine-rich neurotoxic peptide derived from prion protein
言語
言語 eng
キーワード
言語 en
主題Scheme Other
主題 Prion protein
キーワード
言語 en
主題Scheme Other
主題 Tyrosine
キーワード
言語 en
主題Scheme Other
主題 Superoxide
キーワード
言語 en
主題Scheme Other
主題 Redox
キーワード
言語 en
主題Scheme Other
主題 Copper
資源タイプ
資源 http://purl.org/coar/resource_type/c_6501
タイプ journal article
アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
著者 Yokawa, Ken

× Yokawa, Ken

WEKO 90255

en Yokawa, Ken

Search repository
Kagenishi, Tomoko

× Kagenishi, Tomoko

WEKO 90256

en Kagenishi, Tomoko

Search repository
Goto, Kaishi

× Goto, Kaishi

WEKO 90322

en Goto, Kaishi

Search repository
Kawano, Tomonori

× Kawano, Tomonori

WEKO 90323

en Kawano, Tomonori

Search repository
著者別名
姓名
姓名 陽川, 憲
言語 ja
著者別名
姓名
姓名 蔭西, 知子
言語 ja
著者別名
姓名
姓名 河野, 智謙
言語 ja
抄録
内容記述タイプ Abstract
内容記述 Previously, generation of superoxide anion (O2•-) catalyzed by Cu-binding peptides derived from human prion protein (model sequence for helical Cu-binding motif VNITKQHTVTTTT was most active) in the presence of catecholamines and related aromatic monoamines such as phenylethylamine and tyramine, has been reported [Kawano, T., Int J Biol Sci 2007; 3: 57-63]. The peptide sequence (corresponding to helix 2) tested here is known as threonine-rich neurotoxic peptide. In the present article, the redox behaviors of aromatic monoamines, 20 amino acids and prion-derived tyrosine-rich peptide sequences were compared as putative targets of the oxidative reactions mediated with the threonine-rich prion-peptide. For detection of O2•-, an O2•--specific chemiluminescence probe, Cypridina luciferin analog was used. We found that an aromatic amino acid, tyrosine (structurally similar to tyramine) behaves as one of the best substrates for the O2•- generating reaction (conversion from hydrogen peroxide) catalyzed by Cu-bound prion helical peptide. Data suggested that phenolic moiety is required to be an active substrate while the presence of neither carboxyl group nor amino group was necessarily required. In addition to the action of free tyrosine, effect of two tyrosine-rich peptide sequences YYR and DYEDRYYRENMHR found in human prion corresponding to the tyrosine-rich region was tested as putative substrates for the threonine-rich neurotoxic peptide. YYR motif (found twice in the Y-rich region) showed 2- to 3-fold higher activity compared to free tyrosine. Comparison of Y-rich sequence consisted of 13 amino acids and its Y-to-F substitution mutant sequence revealed that the tyrosine-residues on Y-rich peptide derived from prion may contribute to the higher production of O2•-. These data suggest that the tyrosine residues on prion molecules could be additional targets of the prion-mediated reactions through intra- or inter-molecular interactions. Lastly, possible mechanism of O2•- generation and the impacts of such self-redox events on the conformational changes in prion are discussed.
書誌情報 en : International Journal of Biological Sciences

巻 5, 号 1, p. 53-63, 発行日 2009
ISSN
収録物識別子タイプ ISSN
収録物識別子 1449-2288
DOI
関連識別子
識別子タイプ DOI
関連識別子 https://doi.org/10.7150/ijbs.5.53
権利
権利情報 c Ivyspring International Publisher. All rights reserved
出版者
出版者 Ivyspring International Publisher
著者版フラグ
値 publisher
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
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