Liangwei Zhong

ORCID: 0000-0003-4027-3516
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • Redox biology and oxidative stress
  • Glutathione Transferases and Polymorphisms
  • Selenium in Biological Systems
  • Genomics, phytochemicals, and oxidative stress
  • Sulfur Compounds in Biology
  • Free Radicals and Antioxidants
  • Heme Oxygenase-1 and Carbon Monoxide
  • Phytochemicals and Antioxidant Activities
  • Adipokines, Inflammation, and Metabolic Diseases
  • Adipose Tissue and Metabolism
  • Trace Elements in Health
  • Nitric Oxide and Endothelin Effects
  • Protein Tyrosine Phosphatases
  • Tea Polyphenols and Effects
  • Mast cells and histamine
  • Heat shock proteins research
  • Growth Hormone and Insulin-like Growth Factors
  • Endoplasmic Reticulum Stress and Disease
  • Microbial Metabolites in Food Biotechnology
  • Vitamin C and Antioxidants Research
  • Bone and Dental Protein Studies
  • Biochemical effects in animals
  • Peroxisome Proliferator-Activated Receptors
  • Vitamin D Research Studies
  • S100 Proteins and Annexins

University of Chinese Academy of Sciences
2010-2021

Chinese Academy of Sciences
2005-2014

National Natural Science Foundation of China
2013

Shanxi Medical University
2013

Karolinska Institutet
1998-2009

Beijing Proteome Research Center
2009

Svenska Örtmedicinska Institute
2009

Nobel Foundation
1998-2005

Augusta University
2001

Mammalian thioredoxin reductases (TrxR) are homodimers, homologous to glutathione reductase (GR), with an essential selenocysteine (SeCys) residue in extension containing the conserved C-terminal sequence -Gly-Cys-SeCys-Gly. In oxidized enzyme, we demonstrated two nonflavin redox centers by chemical modification and peptide sequencing: one was a disulfide within -Cys 59 -Val-Asn-Val-Gly-Cys 64 , identical active site of GR; other selenenylsulfide formed from Cys 497 -SeCys 498 confirmed mass...

10.1073/pnas.100114897 article EN Proceedings of the National Academy of Sciences 2000-05-09

Mammalian thioredoxin reductases (TrxR) are dimers homologous to glutathione reductase with a selenocysteine (SeCys) residue in the conserved C-terminal sequence -Gly-Cys-SeCys-Gly. We removed insertion rat gene, and we changed SeCys498 encoded by TGA Cys or Ser mutagenesis. The truncated protein having SeCys-Gly dipeptide deleted, expected selenium deficiency, was also engineered. All three mutant enzymes were overexpressed Escherichia coli purified homogeneity 1 mol of FAD per monomeric...

10.1074/jbc.m000690200 article EN cc-by Journal of Biological Chemistry 2000-06-01

Thioredoxin reductases (TrxRs) from mammalian cells contain an essential selenocysteine residue in the conserved C-terminal sequence Gly-Cys-SeCys-Gly forming a selenenylsulfide oxidized enzyme. Reduction by NADPH generates selenolthiol, which is active site reduction of Trx. The three-dimensional structure SeCys498Cys mutant rat TrxR complex with NADP + has been determined to 3.0-Å resolution x-ray crystallography. overall similar that glutathione reductase (GR), including amino acid...

10.1073/pnas.171178698 article EN Proceedings of the National Academy of Sciences 2001-07-31

10.1016/s0076-6879(99)00129-9 article EN Methods in enzymology on CD-ROM/Methods in enzymology 1999-01-01

We have determined the sequence of 23 peptides from bovine thioredoxin reductase covering 364 amino acid residues. The result was used to identify a rat cDNA clone (2.19 kilobase pairs), which contained an open reading frame 1496 base pairs encoding protein with 498 and sequences revealed close homology glutathione including conserved active site (Cys-Val-Asn-Val-Gly-Cys). This also confirmed identity previously published putative human clone. Moreover, one peptide enzyme selenocysteine...

10.1074/jbc.273.15.8581 article EN cc-by Journal of Biological Chemistry 1998-04-01

The immunostimulatory dinitrohalobenzene compound 1-chloro-2, 4-dinitrobenzene (DNCB) irreversibly inhibits mammalian thioredoxin reductase (TrxR) in the presence of NADPH, inducing an NADPH oxidase activity modified enzyme (Arnér, E. S. J., Björnstedt, M., and Holmgren, A. (1995) J. Biol. Chem. 270, 3479-3482). Here we have further analyzed reactivity with DNCB analogues varying immunomodulatory properties. We also identified reactive residues bovine reductase, recently discovered to be a...

10.1074/jbc.273.18.10835 article EN cc-by Journal of Biological Chemistry 1998-05-01

Selenium is an essential micronutrient for humans and animals, its deficiency can predispose to the development of pathological conditions. This study evaluates effect selenium on thioredoxin system, consisting NADPH, selenoprotein reductase (TrxR), (Trx); glutathione including reductase, glutathione, glutaredoxin coupled with peroxidase (GPx). We particularly investigate whether inactive truncated TrxR present under selenium-starvation conditions due reading UGA codon as stop. Feeding rats...

10.1096/fj.08-127662 article EN The FASEB Journal 2009-04-07

Background and Purpose Insulin‐sensitizing drugs are currently limited, identifying new candidates is a challenge. Protein tyrosine phosphatase 1B (PTP1B) negatively regulates insulin signalling, its inhibition anticipated to improve resistance. Here, the pharmacological properties of CX08005, novel PTP1B inhibitor, were investigated. Experimental Approach Recombinant hPTP1B protein was used study enzyme activity mode inhibition. Docking simulation explored interactions between CX08005...

10.1111/bph.13483 article EN British Journal of Pharmacology 2016-03-19

Abstract (−)‐Epigallocatechin gallate (EGCG) is a major bioactive component in leaves of green tea, and has been widely investigated for its anti‐tumor activity. The interaction between EGCG the key peptides or proteins (e.g. glutathione, enzymes) vivo thought to be involved toxicity anti‐cancer mechanism EGCG. However, true not clear, few studies have focused on reactivity toward under physiological conditions (pH 7.4, 37°C). In this work, covalent interactions model containing one more...

10.1002/rcm.3985 article EN Rapid Communications in Mass Spectrometry 2009-03-12

High‐fat diet (HFD) can induce oxidative stress. Thioredoxin (Trx) and thioredoxin reductase (TrxR) are critical antioxidant proteins but how they affected by HFD remains unclear. Using HFD‐induced insulin‐resistant mouse model, we show here that liver Trx TrxR significantly decreased, but, remarkably, the degree of their S‐acylation is increased after consuming HFD. These changes in Trx/TrxR may reflect abnormalities lipid metabolism insulin signaling transduction. HFD‐driven accumulation...

10.1016/j.fob.2014.10.015 article EN cc-by-nc-nd FEBS Open Bio 2014-01-01

Epigallocatechin 3-gallate (EGCG) is the most abundant catechin in green tea and may combat bacteria with few side-effects. Its selectivity for different bacterial infections remains unclear, hence identification of underlying mechanism practical importance. Both thioredoxin (Trx) system glutathione/glutaredoxin (Grx) support growth. Some pathogenic are naturally deficient Grx system. We analyzed effect extract (GTE) EGCG on wild-type null mutants Escherichia coli either Trx or deficiency...

10.1111/febs.13587 article EN FEBS Journal 2015-11-07

Abstract Intracellular Ca 2+ signaling controls many cellular functions. Understanding its regulation by selenoproteins is essential for understanding the role of in regulating cell The activity thioredoxin reductase (TrxR), (Trx) content, and glutathione peroxidase (GPx) human endothelial cells cultured selenium‐supplemented medium (refer as Se + cells) was found 70%, 40%, 20% higher, respectively than those normal 0 cells). intracellular initiated inositol 1,4,5‐trisphosphate (IP 3 ),...

10.1002/jcp.20378 article EN Journal of Cellular Physiology 2005-05-05

10.1016/s0076-6879(02)47023-1 article EN Methods in enzymology on CD-ROM/Methods in enzymology 2002-01-01

10.1016/j.bbrc.2015.03.132 article EN Biochemical and Biophysical Research Communications 2015-04-06

10.1016/j.bbagen.2019.03.007 article EN Biochimica et Biophysica Acta (BBA) - General Subjects 2019-03-07

Acute exacerbation of chronic obstructive pulmonary disease (AECOPD) is a global problem with high mortality. Its pathogenesis not fully understood. To reveal new serum feature AECOPD and their potential implications, we have analyzed 180 samples, found that in the patients, 4-hydroxy-2-nonenal (4HNE)-protein adducts are dynamically increased as partial pressure oxygen (PaO 2 ) drops, which accompanied by progressively decreasing thioredoxin reductase (TrxR1) (Trx1), compared those healthy...

10.1371/journal.pone.0245810 article EN cc-by PLoS ONE 2021-01-25
Coming Soon ...