Radish phospholipid hydroperoxide glutathione peroxidase provides protection against hydroperoxide-mediated injury in mouse 3T3 fibroblasts

Tian, Lei; Liu, Guan-Lan; Duan, Mingxing; Liu, Jinyuan

doi:10.5483/bmbrep.2009.42.10.648

Cited by 5 publications

(3 citation statements)

References 24 publications

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“…MDA content was measured using the thiobarbituric acid (TBA) assay [66]. Two-week-old rice seedlings were treated with or without H 2 O 2 (300 or 600 µM), then the roots (∼2 g per sample) were harvested and ground on ice with 0.4 g quartz sand, then extracted with 5 ml phosphate buffer (10 mM, pH 7.0).…”

Section: Methodsmentioning

confidence: 99%

Comparative Proteomics Analysis of the Root Apoplasts of Rice Seedlings in Response to Hydrogen Peroxide

et al. 2011

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BackgroundPlant apoplast is the prime site for signal perception and defense response, and of great importance in responding to environmental stresses. Hydrogen peroxide (H2O2) plays a pivotal role in determining the responsiveness of cells to stress. However, how the apoplast proteome changes under oxidative condition is largely unknown. In this study, we initiated a comparative proteomic analysis to explore H2O2-responsive proteins in the apoplast of rice seedling roots.Methodology/Principal Findings14-day-old rice seedlings were treated with low concentrations (300 and 600 µM) of H2O2 for 6 h and the levels of relative electrolyte leakage, malondialdehyde and H2O2 were assayed in roots. The modified vacuum infiltration method was used to extract apoplast proteins of rice seedling roots, and then two-dimensional electrophoresis gel analysis revealed 58 differentially expressed protein spots under low H2O2 conditions. Of these, 54 were successfully identified by PMF or MS/MS as matches to 35 different proteins including known and novel H2O2-responsive proteins. Almost all of these identities (98%) were indeed apoplast proteins confirmed either by previous experiments or through publicly available prediction programs. These proteins identified are involved in a variety of processes, including redox homeostasis, cell wall modification, signal transduction, cell defense and carbohydrate metabolism, indicating a complex regulative network in the apoplast of seedling roots under H2O2 stress.Conclusions/SignificanceThe present study is the first apoplast proteome investigation of plant seedlings in response to H2O2 and may be of paramount importance for the understanding of the plant network to environmental stresses. Based on the abundant changes in these proteins, together with their putative functions, we proposed a possible protein network that provides new insights into oxidative stress response in the rice root apoplast and clues for the further functional research of target proteins associated with H2O2 response.

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Section: Methodsmentioning

confidence: 99%

Comparative Proteomics Analysis of the Root Apoplasts of Rice Seedlings in Response to Hydrogen Peroxide

et al. 2011

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“…A point mutation converting S 284 (AGT) of AtYY1 to A (GCT) or D (GAT) was introduced using a PCR-mediated mutagenesis method (Li et al, 2009). Recombinant His-MBP, His-AtYY1, His-S284D, and His-S284A proteins were prepared as described previously (Li et al, 2016).…”

Section: Methodsmentioning

confidence: 99%

A Casein Kinase II Phosphorylation Site in AtYY1 Affects Its Activity, Stability, and Function in the ABA Response

2017

Front. Plant Sci.

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The phosphorylation and dephosphorylation of proteins are crucial in the regulation of protein activity and stability in various signaling pathways. In this study, we identified an ABA repressor, Arabidopsis Ying Yang 1 (AtYY1) as a potential target of casein kinase II (CKII). AtYY1 physically interacts with two regulatory subunits of CKII, CKB3, and CKB4. Moreover, AtYY1 can be phosphorylated by CKII in vitro, and the S284 site is the major CKII phosphorylation site. Further analyses indicated that S284 phosphorylation can enhance the transcriptional activity and protein stability of AtYY1 and hence strengthen the effect of AtYY1 as a negative regulator in the ABA response. Our study provides novel insights into the regulatory mechanism of AtYY1 mediated by CKII phosphorylation.

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“…Seiler et al (2008) report that knockout of GPX4 in MEFs leads to the death of mice. In mouse 3T3 fibroblasts, GPX4 also shows a antioxidative activity and protects against injury caused by hydroperoxide (T. Li et al, 2009). In addition, the inhibition of GPX4 blocks the cell proliferation and the EMT phenotype (Peng et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Function and regulation of GPX4 in the development and progression of fibrotic disease

Zhao-bing

Zhu

Liu

et al. 2022

Journal Cellular Physiology

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Fibrosis is a common feature of fibrotic diseases that poses a serious threat to global health due to high morbidity and mortality in developing countries. There exist some chemical compounds and biomolecules associated with the development of fibrosis, including cytokines, hormones, and enzymes. Among them, glutathione peroxidase 4 (GPX4), as a selenoprotein antioxidant enzyme, is widely found in the embryo, testis, brain, liver, heart, and photoreceptor cells. Moreover, it is shown that GPX4 elicits diverse biological functions by suppressing phospholipid hydroperoxide at the expense of decreased glutathione (GSH), including loss of neurons, autophagy, cell repair, inflammation, ferroptosis, apoptosis, and oxidative stress. Interestingly, these processes are intimately related to the occurrence of fibrotic disease. Recently, GPX4 has been reported to exhibit a decline in fibrotic disease and inhibit fibrosis, suggesting that alterations of GPX4 can change the course or dictate the outcome of fibrotic disease. In this review, we summarize the role and underlying mechanisms of GPX4 in fibrosis diseases such as lung fibrosis, liver fibrosis, kidney fibrosis, cardiac fibrosis, and myelofibrosis.

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Radish phospholipid hydroperoxide glutathione peroxidase provides protection against hydroperoxide-mediated injury in mouse 3T3 fibroblasts

Cited by 5 publications

References 24 publications

Comparative Proteomics Analysis of the Root Apoplasts of Rice Seedlings in Response to Hydrogen Peroxide

Comparative Proteomics Analysis of the Root Apoplasts of Rice Seedlings in Response to Hydrogen Peroxide

A Casein Kinase II Phosphorylation Site in AtYY1 Affects Its Activity, Stability, and Function in the ABA Response

Function and regulation of GPX4 in the development and progression of fibrotic disease

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