Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Mass-spectroscopic quantification of CHAC1-regulated protein cysteine S-glutathionylation

ABSTRACT: S-glutathionylation is an important post-translational modification of a cysteine residue of target protein. We applied a quantitative redox proteomics approach to identify the specific cysteine residues as targets of S-glutathionylation. Using this approach, we profiled CHAC1-associated changes in glutathionylome in APAP-induced hepatoxicity and ferroptosis. Primary mouse hepatocytes (PMHs) were infected with Ad-GFP or Ad-CHAC1 for 36 h, and then challenged with 20 mM APAP for 3 h followed by the enrichment and quantitative analysis of glutathionylated proteins.

ORGANISM(S): Mus Musculus

SUBMITTER: Xiaobo Li

PROVIDER: PXD050569 | iProX | Tue Mar 12 00:00:00 GMT 2024

REPOSITORIES: iProX

ACCESS DATA

Json Xml

Publications

Protein S-glutathionylation confers cellular resistance to ferroptosis induced by glutathione depletion.

Ju Yi Y Zhang Yuting Y Tian Xiaolin X Zhu Nanbin N Zheng Yufan Y Qiao Yiming Y Yang Tao T Niu Baolin B Li Xiaoyun X Yu Liu L Liu Zhuolin Z Wu Yixuan Y Zhi Yang Y Dong Yinuo Y Xu Qingling Q Yang Xiaoming X Wang Xuening X Wang Xiaokai X Deng Haiteng H Mao Yimin Y Li Xiaobo X

Redox biology 20250506

Ferroptosis is one of the most critical biological consequences of glutathione depletion. Excessive oxidative stress, indicated by an elevated oxidized glutathione (GSSG)/reduced glutathione (GSH) ratio, is recognized as a key driver of ferroptosis. However, in glutathione depletion-induced ferroptosis, a marked decrease in total glutathione levels (including both GSH and GSSG) is frequently observed, yet its significance remains understudied. Protein S-glutathionylation (protein-SSG) levels are ...[more]

PMID: 40354766

Similar Datasets

Non-canonical BIM-regulated energy metabolism determines drug-induced liver necrosis

Project description:Paracetamol (acetaminophen, APAP) overdose severely damages mitochondria and triggers several apoptotic processes in hepatocytes, but the final outcome is fulminant necrotic cell death, resulting in acute liver failure and mortality. Here, we studied this switch of cell death modes and demonstrate a non-canonical role of the apoptosis-regulating BCL-2 homolog BIM/Bcl2l11 in promoting necrosis by regulating cellular bioenergetics. BIM deficiency enhanced total ATP production and shifted the bioenergetic profile towards glycolysis, resulting in persistent protection from APAP-induced liver injury. Modulation of glucose levels and deletion of mitofusins confirmed that severe APAP toxicity occurs only in cells dependent on oxidative phosphorylation. Glycolytic hepatocytes maintained elevated ATP levels and reduced ROS, which enabled lysosomal recycling of damaged mitochondria by mitophagy. The present study highlights how metabolism and bioenergetics affect drug-induced liver toxicity, and identifies BIM as important regulator of glycolysis, mitochondrial respiration, and oxidative stress signaling.

2024-09-24 | PXD045034 | Pride

Non-canonical BIM-regulated energy metabolism determines drug-induced liver necrosis.

2023-09-08 | GSE242368 | GEO

DrugMap: A quantitative pan-cancer analysis of cysteine ligandability

Project description:DrugMap: A quantitative pan-cancer analysis of cysteine ligandability

| PRJNA1079738 | ENA

Hypoxia-induced cysteine metabolism reprogramming are crucial for the tumorigenesis of colorectal cancer [HCT116]

Project description:Metabolic reprogramming is a hallmark of human cancer and cancer-specific metabolism provide opportunities for cancer diagnosis, prognosis, and treatment. However, how metabolic pathways affect the initiation and progression of colorectal cancer remain largely unknown. Here, we showed cysteine is highly enriched in colorectal tumors compared with adjacent non-tumor tissues to promote tumorigenesis of CRC. Both cystine and cysteine imports are essential to maintain intracellular cysteine level and promote tumor growth and survival. Transporter genes of cystine and cysteine are all upregulated in colorectal cancer by tumor microenvironment induced ROS through transcription factor ATF4. Glutathione synthetase GSS is upregulated and increases cysteine to reduced glutathione flux to support tumor growth and survival in colorectal cancer. Depletion of cystine and cysteine by a recombinant cyst(e)inase effectively reduced the growth of colorectal tumors. Moreover, scavenging cystine and cysteine induces autophagy of colorectal cancer cells through mTOR-ULK signaling axis. With this study, we demonstrate that cysteine metabolism is a key signature of CRC metabolic reprogramming and targeting cysteine metabolism might be an effective approach to treat colon cancer.

2023-01-21 | GSE223118 | GEO

Hypoxia-induced cysteine metabolism reprogramming are crucial for the tumorigenesis of colorectal cancer [tissue pair]

2023-01-21 | GSE223119 | GEO

Cysteine deprivation in liver cell line

2007-12-13 | GSE9517 | GEO

Transcription profiling of human liver cell line after cysteine deprivation

Project description:First experiment: Cells were cultured in sulfur amino acid-free DMEM supplemented with 0.1 mM methionine + 0.1 mM cysteine (complete) or supplemented only with 0.1 mM methionine (cysteine-free). Cells were cultured in either medium for 42 h (Long + Cys; Long -Cys) or in cysteine-free medium for 36 h followed by 6 h in complete medium (Short +Cys); Second experiment: C3A/HepG2 cells were cultured in sulfur amino acid-free DMEM supplemented with 0.1 mM Met and 0.1 mM Cys (complete) or supplemented only with 0.1 mM Met (cysteine-devoid). Cells were cultured in complete medium for 42 h (Long +Cys) or in complete medium for 36 h followed by cysteine-devoid medium for 6 h (Short -Cys). Experiment Overall Design: First experiment: Three plates of cells were cultured under each condition. Cells were cultured in sulfur amino acid-free DMEM supplemented with 0.1 mM methionine + 0.1 mM cysteine (complete) or supplemented only with 0.1 mM methionine (cysteine-free). Cells were cultured in either medium for 42 h (Long + Cys; Long -Cys) or in cysteine-free medium for 36 h followed by 6 h in complete medium (Short +Cys). Experiment Overall Design: Second experiment: C3A/HepG2 cells were cultured in sulfur amino acid-free DMEM supplemented with 0.1 mM Met and 0.1 mM Cys (complete) or supplemented only with 0.1 mM Met (cysteine-devoid). Cells were cultured in complete medium for 42 h (Long +Cys) or in complete medium for 36 h followed by cysteine-devoid medium for 6 h (Short -Cys).

2008-06-16 | E-GEOD-9517 | biostudies-arrayexpress

Physiological response of S. cerevisiae excess cysteine or cystine

Project description:Excess cysteine (and cystine) is known to be toxic in organisms. Due to the absence of cysteine dioxygenase (involved in degradation of excess cysteine in humans and pathogenic fungi) in non pathogenic fungi such as S. cerevisiae, mechanism of cysteine (and cystine) tolerance is yet to be addressed.

2017-06-13 | GSE87794 | GEO

DrugMap: A quantitative pan-cancer analysis of cysteine ligandability (ChIP-Seq)

Project description:DrugMap: A quantitative pan-cancer analysis of cysteine ligandability (ChIP-Seq)

| PRJNA1079741 | ENA

DrugMap: A quantitative pan-cancer analysis of cysteine ligandability (RNA-Seq)

Project description:DrugMap: A quantitative pan-cancer analysis of cysteine ligandability (RNA-Seq)

| PRJNA1079745 | ENA