Adenanthin targets proteins involved in the regulation of disulphide bonds

doi:10.1016/j.bcp.2014.02.022

	Adenanthin targets proteins involved in the regulation of disulphide bonds
	Muchowicz, Angelika 1; Firczuk, Malgorzata 1; Chlebowska, Justyna 1; Nowis, Dominika 1,2; Stachura, Joanna 1; Barankiewicz, Joanna 1; Trzeciecka, Anna 1; Klossowski, Szymon 3; Ostaszewski, Ryszard 3; Zagozdzon, Radoslaw 1; Pu, Jian-Xin4 ; Sun, Han-Dong4 ; Golab, Jakub 1,5
通讯作者	Golab,J (reprint author),Med Univ Warsaw,Dept Immunol,Ctr Biostruct Res,1a Banacha Str,F Bldg,PL-02097 Warsaw,Poland. ; hdsun@mail.kib.ac.cn ; jakub.golab@wum.edu.pl
	2014-05-15
发表期刊	BIOCHEMICAL PHARMACOLOGY
ISSN	0006-2952
卷号	89 期号:2 页码:210-216
摘要	Adenanthin has been recently shown to inhibit the enzymatic activities of peroxiredoxins (Prdx) land II through its functional alpha,beta-unsaturated ketone group serving as a Michael acceptor. A similar group is found in SK053, a compound recently developed by our group to target the thioredoxin-thioredoxin reductase (Trx-TrxR) system. This work provides evidence that next to Prdx I and II adenanthin targets additional proteins including thioredoxin-thioredoxin reductase system as well as protein disulfide isomerase (PDI) that contain a characteristic structural motif, referred to as a thioredoxin fold. Adenanthin inhibits the activity of Trx-TR system and PDI in vitro in the insulin reduction assay and decreases the activity of Trx in cultured cells. Moreover, we identified Trx-1 as an adenanthin binding protein in cells incubated with biotinylated adenanthin as an affinity probe. The results of our studies indicate that adenanthin is a mechanism-selective, rather than an enzyme-specific inhibitor of enzymes containing readily accessible, nucleophilic cysteines. This observation might be of importance in considering potential therapeutic applications of adenanthin to include a range of diseases, where aberrant activity of Prdx, Trx-TrxR and PDI is involved in their pathogenesis. (C) 2014 Elsevier Inc. All rights reserved.
关键词	Adenanthin Cancer Peroxiredoxin Protein Disulphide Isomerase Thioredoxin
学科领域	Pharmacology & Pharmacy
DOI	10.1016/j.bcp.2014.02.022
收录类别	SCI
语种	英语
WOS记录号	WOS:000335428800006
引用统计
文献类型	期刊论文
条目标识符	http://ir.kib.ac.cn/handle/151853/18118
专题	植物化学与西部植物资源持续利用国家重点实验室
作者单位	1.Med Univ Warsaw, Dept Immunol, Ctr Biostruct Res, PL-02097 Warsaw, Poland 2.Med Univ Warsaw, Dept Gen Transplant & Liver Surg, PL-02097 Warsaw, Poland 3.Polish Acad Sci, Inst Organ Chem, PL-01224 Warsaw, Poland 4.Chinese Acad Sci, Kunming Inst Bot, Kunming, Peoples R China 5.Polish Acad Sci, Inst Phys Chem, Dept 3, Warsaw, Poland
推荐引用方式 GB/T 7714	Muchowicz, Angelika,Firczuk, Malgorzata,Chlebowska, Justyna,et al. Adenanthin targets proteins involved in the regulation of disulphide bonds[J]. BIOCHEMICAL PHARMACOLOGY,2014,89(2):210-216.
APA	Muchowicz, Angelika.,Firczuk, Malgorzata.,Chlebowska, Justyna.,Nowis, Dominika.,Stachura, Joanna.,...&Golab, Jakub.(2014).Adenanthin targets proteins involved in the regulation of disulphide bonds.BIOCHEMICAL PHARMACOLOGY,89(2),210-216.
MLA	Muchowicz, Angelika,et al."Adenanthin targets proteins involved in the regulation of disulphide bonds".BIOCHEMICAL PHARMACOLOGY 89.2(2014):210-216.

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