Protein Folding in the Presence of Water-Soluble Cyclic Diselenides with Novel Oxidoreductase and Isomerase Activities

被引：36

作者：

Arai, Kenta ^{[1
]}

Ueno, Haruhito ^{[1
]}

Asano, Yuki ^{[1
]}

Chakrabarty, Gaurango ^{[2
]}

Shimodaira, Shingo ^{[1
]}

Mugesh, Govindasamy ^{[2
]}

Iwaoka, Michio ^{[1
]}

机构：

[1] Tokai Univ, Dept Chem, Sch Sci, Hiratsuka, Kanagawa 2591292, Japan

[2] Indian Inst Sci, Dept Inorgan & Phys Chem, Bangalore 560012, Karnataka, India

来源：

CHEMBIOCHEM | 2018年 / 19卷 / 03期

关键词：

diselenides; enzyme models; isomerases; protein folding; selenium; DISULFIDE BOND FORMATION; SMALL-MOLECULE DISELENIDES; ENDOPLASMIC-RETICULUM; RIBONUCLEASE-A; GLUTATHIONE-PEROXIDASE; SELENOXIDE REAGENT; CATALYSTS; STRESS; ER; SELENOGLUTATHIONE;

D O I：

10.1002/cbic.201700624

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The protein disulfide isomerase (PDI) family, found in the endoplasmic reticulum (ER) of the eukaryotic cell, catalyzes the formation and cleavage of disulfide bonds and thereby helps in protein folding. A decrease in PDI activity under ER stress conditions leads to protein misfolding, which is responsible for the progression of various human diseases, such as Alzheimer's, Parkinson's, diabetes mellitus, and atherosclerosis. Here we report that water-soluble cyclic diselenides mimic the multifunctional activity of the PDI family by facilitating oxidative folding, disulfide formation/reduction, and repair of the scrambled disulfide bonds in misfolded proteins.

引用

页码：207 / 211

页数：5

共 45 条

[1] An Amphiphilic Selenide Catalyst Behaves Like a Hybrid Mimic of Protein Disulfide Isomerase and Glutathione Peroxidase 7 [J].

Arai, Kenta ;

Moriai, Kenji ;

Ogawa, Akinobu ;

Iwaoka, Michio .

CHEMISTRY-AN ASIAN JOURNAL, 2014, 9 (12) :3464-3471

[2] Kinetic and thermodynamic analysis of the conformational folding process of SS-reduced bovine pancreatic ribonuclease A using a selenoxide reagent with high oxidizing ability [J].

Arai, Kenta ;

Kumakura, Fumio ;

Iwaoka, Michio .

FEBS OPEN BIO, 2012, 2 :60-70

[3] Characterization of Kinetic and Thermodynamic Phases in the Prefolding Process of Bovine Pancreatic Ribonuclease A Coupled with Fast SS Formation and SS Reshuffling [J].

Arai, Kenta ;

Kumakura, Fumio ;

Iwaoka, Michio .

BIOCHEMISTRY, 2010, 49 (49) :10535-10542

[4] Catalysis of oxidative protein folding by small-molecule diselenides [J].

Beld, Joris ;

Woycechowsky, Kenneth J. ;

Hilvert, Donald .

BIOCHEMISTRY, 2008, 47 (27) :6985-6987

[5] Selenoglutathione: Efficient oxidative protein folding by a diselenide [J].

Beld, Joris ;

Woycechowsky, Kenneth J. ;

Hilvert, Donald .

BIOCHEMISTRY, 2007, 46 (18) :5382-5390

[6] Diselenides as universal oxidative folding catalysts of diverse proteins [J].

Beld, Joris ;

Woycechowsky, Kenneth J. ;

Hilvert, Donald .

JOURNAL OF BIOTECHNOLOGY, 2010, 150 (04) :481-489

[7] Small-Molecule Diselenides Catalyze Oxidative Protein Folding in Vivo [J].

Beld, Joris ;

Woycechowsky, Kenneth J. ;

Hilvert, Donald .

ACS CHEMICAL BIOLOGY, 2010, 5 (02) :177-182

[8]

Bhowmick D., 2015, ANGEW CHEM, V127, P8569

[9] Highly Efficient Glutathione Peroxidase and Peroxiredoxin Mimetics Protect Mammalian Cells against Oxidative Damage [J].

Bhowmick, Debasish ;

Srivastava, Shubhi ;

D'Silva, Patrick ;

Mugesh, Govindasamy .

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2015, 54 (29) :8449-8453

[10] The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress [J].

Chakravarthi, S ;

Jessop, CE ;

Bulleid, NJ .

EMBO REPORTS, 2006, 7 (03) :271-275

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