Adenanthin targets proteins involved in the regulation of disulphide bonds
Muchowicz, Angelika1; Firczuk, Malgorzata1; Chlebowska, Justyna1; Nowis, Dominika1,2; Stachura, Joanna1; Barankiewicz, Joanna1; Trzeciecka, Anna1; Klossowski, Szymon3; Ostaszewski, Ryszard3; Zagozdzon, Radoslaw1; Pu, Jian-Xin4; Sun, Han-Dong4; Golab, Jakub1,5
Corresponding AuthorGolab,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
Source PublicationBIOCHEMICAL PHARMACOLOGY
ISSN0006-2952
Volume89Issue:2Pages:210-216
AbstractAdenanthin 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.
KeywordAdenanthin Cancer Peroxiredoxin Protein Disulphide Isomerase Thioredoxin
Subject AreaPharmacology & Pharmacy
DOI10.1016/j.bcp.2014.02.022
Indexed BySCI
Language英语
WOS Research AreaPharmacology & Pharmacy
WOS SubjectPharmacology & Pharmacy
WOS IDWOS:000335428800006
Citation statistics
Document Type期刊论文
Identifierhttp://ir.kib.ac.cn/handle/151853/18118
Collection植物化学与西部植物资源持续利用国家重点实验室
Affiliation1.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
Recommended Citation
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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