Full Text:   <2365>

Summary:  <1648>

CLC number: R392.11

On-line Access: 2017-09-05

Received: 2016-05-03

Revision Accepted: 2016-10-07

Crosschecked: 2017-08-25

Cited: 0

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Citations:  Bibtex RefMan EndNote GB/T7714


Yan-ting Gu


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Journal of Zhejiang University SCIENCE B 2017 Vol.18 No.9 P.770-777


Protective effect of dihydropteridine reductase against oxidative stress is abolished with A278C mutation

Author(s):  Yan-ting Gu, Yan-chun Wang, Hao-jun Zhang, Ting-ting Zhao, Si-fan Sun, Hua Wang, Bin Zhu, Ping Li

Affiliation(s):  Beijing Key Lab for Immune-Mediated Inflammatory Diseases, Institute of Clinical Medical Sciences, China-Japan Friendship Hospital, Beijing 100029, China; more

Corresponding email(s):   lp8675@163.com

Key Words:  Dihydropteridine reductase, Transforming growth factor β, 1 (TGF-β, 1), Nicotinamide adenine dinucleotide phosphate oxidase 4 (NOX4), Superoxide dismutase 1 (SOD1), Glutathione peroxidase 3 (GPX3), Oxidative stress

Yan-ting Gu, Yan-chun Wang, Hao-jun Zhang, Ting-ting Zhao, Si-fan Sun, Hua Wang, Bin Zhu, Ping Li. Protective effect of dihydropteridine reductase against oxidative stress is abolished with A278C mutation[J]. Journal of Zhejiang University Science B, 2017, 18(9): 770-777.

@article{title="Protective effect of dihydropteridine reductase against oxidative stress is abolished with A278C mutation",
author="Yan-ting Gu, Yan-chun Wang, Hao-jun Zhang, Ting-ting Zhao, Si-fan Sun, Hua Wang, Bin Zhu, Ping Li",
journal="Journal of Zhejiang University Science B",
publisher="Zhejiang University Press & Springer",

%0 Journal Article
%T Protective effect of dihydropteridine reductase against oxidative stress is abolished with A278C mutation
%A Yan-ting Gu
%A Yan-chun Wang
%A Hao-jun Zhang
%A Ting-ting Zhao
%A Si-fan Sun
%A Hua Wang
%A Bin Zhu
%A Ping Li
%J Journal of Zhejiang University SCIENCE B
%V 18
%N 9
%P 770-777
%@ 1673-1581
%D 2017
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B1600123

T1 - Protective effect of dihydropteridine reductase against oxidative stress is abolished with A278C mutation
A1 - Yan-ting Gu
A1 - Yan-chun Wang
A1 - Hao-jun Zhang
A1 - Ting-ting Zhao
A1 - Si-fan Sun
A1 - Hua Wang
A1 - Bin Zhu
A1 - Ping Li
J0 - Journal of Zhejiang University Science B
VL - 18
IS - 9
SP - 770
EP - 777
%@ 1673-1581
Y1 - 2017
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B1600123

Objective: To evaluate the antioxidation of dihydrobiopterin reductase and to explore the effect of A278C mutation of the quinoid dihydropteridine reductase (QDPR) gene on its antioxidant activity. Methods: First, plasmids with different genes (wild and mutant QDPR) were constructed. After gene sequencing, they were transfected into human kidney cells (HEK293T). Then, the intracellular production of reactive oxygen species (ROS) and tetrahydrobiopterin (BH4) was detected after cells were harvested. Activations of nicotinamide adenine dinucleotide phosphate oxidase 4 (NOX4), glutathione peroxidase 3 (GPX3), and superoxide dismutase 1 (SOD1) were analyzed to observe the oxidative stress after transfection. The expression of the neuronal nitric oxide synthase (nNOS) gene was analyzed by semiquantitative reverse-transcription polymerase chain reaction (RT-PCR). We also detected the activation of transforming growth factor β;1 (TGF-β;1) by enzyme-linked immunosorbent assay (ELISA) to observe the connection of TGF-β1 and oxidative stress. Results: The exogenous wild-type QDPR significantly decreased the expression of nNOS, NOX4, and TGF-β1 and induced the expression of SOD1 and GPX3, but the mutated QDPR lost this function and resulted in excessive ROS production. Our data also suggested that the influence on the level of BH4 had no significant difference between mutated and the wild-type QDPR transfection. Conclusions: Wild-type QDPR played an important role in protecting against oxidative stress, but mutant QDPR failed to have these beneficial effects.




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