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Title 

Inactivation of human DGAT2 by oxidative stress on cysteine residues

 

ROS에 의한 DGAT2 효소활성 조절

Authors 

Sunhee JungMiri ChoiKwangman ChoiEun Bin KwonMingu KangDong-eun KimHyejeong JeongJanghwan KimJ H KimMun-Ock KimS B HanSungchan Cho

Publisher 

Public Library of Science

Issue Date 

2017

Citation 

Plos One

Abstract 

Diacylglycerol acyltransferases (DGATs) have a crucial role in the biosynthesis of triacylglycerol (TG), the major storage form of metabolic energy in eukaryotic organisms. Even though DGAT2, one of two distinct DGATs, has a vital role in TG biosynthesis, little is known about the regulation of DGAT2 activity. In this study, we examined the role of cysteine and its oxidation in the enzymatic activity of human DGAT2 in vitro. Human DGAT2 activity was considerably inhibited not only by thiol-modifying reagents (NEM and IA) but also by ROSrelated chemicals (H2O2 and β-lapachone), while human DGAT1 and GPAT1 were little affected. Particularly, ROS-related chemicals concomitantly induced intermolecular disulfide crosslinking of human DGAT2. Both the oxidative inactivation and disulfide crosslinking were almost completely reversed by the treatment with DTT, a disulfide-reducing agent. These results clearly demonstrated the significant role of ROS-induced intermolecular crosslinking in the inactivation of human DGAT2 and also suggested DGAT2 as a redox-sensitive regulator in TG biosynthesis

ISSN 

1932-6203

Link 

http://dx.doi.org/10.1371/journal.pone.0181076

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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