Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Analysis of cysteine redox state with age in flies overexpressing catalase

ABSTRACT: Dysregulation of redox homeostasis has been implicated in the ageing process and the pathology of age-related diseases. To study redox signalling by hydrogen peroxide in vivo, we upregulated levels of the enzyme catalase in Drosophila.

INSTRUMENT(S):

ORGANISM(S): Drosophila Melanogaster (fruit Fly)

SUBMITTER: Andrew James

LAB HEAD: Helena M.

PROVIDER: PXD060330 | Pride | 2025-06-30

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	MEN2547A16MA3DigestofKMDD7CAT-1-3-130814-SJD.raw	Raw
	MEN2547A16MA4DigestofKMDD7CAT-1-3-130814-SJD.raw	Raw
	MEN2547A17MA3DigestofKMDD7CAT-2-3-130814-SJD.raw	Raw
	MEN2547A17MA4DigestofKMDD7CAT-2-3-130814-SJD.raw	Raw
	MEN2547A18MA3DigestofKMDD7CAT-3-3-130814-SJD.raw	Raw

Items per page:

1 - 5 of 61

Publications

Enhancing autophagy by redox regulation extends lifespan in Drosophila.

Lennicke Claudia C Bjedov Ivana I Grönke Sebastian S Menger Katja E KE James Andrew M AM Castillo-Quan Jorge Iván JI van Leeuwen Lucie A G LAG Foley Andrea A Buricova Marcela M Adcott Jennifer J Montoya Alex A Kramer Holger B HB Shliaha Pavel V PV Logan Angela A Cabreiro Filipe F Murphy Michael P MP Partridge Linda L Cochemé Helena M HM

Nature communications 20250625 1

Dysregulation of redox homeostasis is implicated in the ageing process and the pathology of age-related diseases. To study redox signalling by H2O2 in vivo, we established a redox-shifted model by manipulating levels of the H2O2-degrading enzyme catalase in Drosophila. Here we report that ubiquitous over-expression of catalase robustly extends lifespan in females. As anticipated, these flies are strongly resistant to a range of oxidative stress challen ...[more]

PMID: 40562835

Similar Datasets

Mechano-redox control of Mac-1 de-adhesion from ICAM-1 by protein disulfide isomerase promotes directional movement under flow

Project description:Quantification of the redox state of disulfide bonds in the beta 2 subunit of human recombinant Mac-1 integrin.

2023-04-09 | PXD032688 | Pride

Clostridium thermocellum DSM 1313 Transcriptional Responses to Redox Perturbation

Project description:Clostridium thermocellum is a promising CBP candidate organism capable of directly converting lignocellulosic biomass to ethanol. Low yields, productivities and growth inhibition prevent industrial deployment of this organism for commodity fuel production. Symptoms of potential redox imbalance such as incomplete substrate utilization, and fermentation products characteristic of overflow metabolism, have been observed during growth. This perceived redox imbalance may be in part responsible for the mentioned bioproductivity limitations. Toward better understanding the redox metabolism of C. thermocellum, we analyzed gene expression, using microarrays, during addition of two stress chemicals (methyl viologen and hydrogen peroxide) which we observed to change fermentation redox potential. High quality RNA was extracted from C. thermocellum grown on cellobiose in chemostat culture and exposed, separately, to methyl viologen and hydrogen peroxide. Transcriptome profiles were obtained at seven time points during actively growing fermentations, 3 minutes, 15 minutes, 35 minutes, 7 hours, 14 hours, 50 hours, and 60 hours after beginning exposure to each stressor. Exposure treatments were carried out in duplicate and reference/untreated samples were taken before and between treatments, after flushing of stressor chemicals and re-equilibration of growth conditions.

2015-07-29 | E-GEOD-71465 | biostudies-arrayexpress

Analysis of ageing-dependent thiol oxidation reveals early oxidation of proteins involved in core proteostasis functions

Project description:Oxidants have a profound impact on biological systems in physiology and under pathological conditions. Oxidative post-translational modifications of protein thiols are well-recognized as a readily occurring alteration of proteins. Changes in protein thiol redox state can modify the function of proteins and thus can control cellular processes. However, chronic oxidative stress causes oxidative damage to proteins with detrimental consequences for cellular function and organismal health. The development of techniques enabling the site-specific and quantitative assessment of protein thiol oxidation on a proteome-wide scale significantly expanded the number of known oxidation-sensitive protein thiols. However, lacking behind are large-scale data on the redox state of proteins during ageing, a physiological process accompanied by increased levels of endogenous oxidants. Here, we present the landscape of protein thiol oxidation in chronologically aged wild-type Saccharomyces cerevisiae in a time-dependent manner. Our data determine early oxidation targets in key biological processes governing the de novo production of proteins, folding, and protein degradation. Comparison to existing datasets reveals evolutionary conservation of early oxidation targets. To facilitate accessibility and cross-species comparison of the experimental data obtained, we created the OxiAge Database, a free online tool for the research community that integrates current datasets on thiol redoxomes in aged yeast, nematode Caenorhabditis elegans, fruit fly Drosophila melanogaster, and mouse Mus musculus.

2024-02-07 | PXD042047 | Pride

Monitoring global protein thiol-oxidation and protein S-mycothiolation in Mycobacterium smegmatis under hypochlorite stress

Project description:Mycothiol (AcCys-GlcN-Ins, MSH) is the major thiol-redox buffer in Actinomycetes, including Mycobacterium and Corynebacterium species. ). Protein S-mycothiolation controls the activities of several redox enzymes that function in detoxification of ROS and methionine sulfoxides, including the thiol peroxidase Tpx, the mycothiol peroxidase Mpx and the methionine sulfoxide reductase MsrA. Here we investigated the level of protein S-mycothiolation in Mycobacterium smegmatis under oxidative stress as well as its NaOCl stress response.

2017-06-30 | PXD003303 | Pride

A Novel Mechanism Mediated by Allosteric Disulfide Bonds Fine-Tunes Thrombus Formation

Project description:Mapping of disulfide bonds and quantification of their redox state in the human histidine rich glycoprotein

2024-04-11 | PXD050718 | Pride

Monitoring global protein thiol-oxidation and protein S-mycothiolation in Corynebacterium diphtheriae under hypochlorite stress

Project description:Mycothiol (AcCys-GlcN-Ins, MSH) is the major thiol-redox buffer in Actinomycetes, including Mycobacterium and Corynebacterium species. Protein S-mycothiolation controls the activities of several redox enzymes that function in detoxification of ROS and methionine sulfoxides, including the thiol peroxidase Tpx, the mycothiol peroxidase Mpx and the methionine sulfoxide reductase MsrA. Here we investigated the level of protein S-mycothiolation in Corynebacterium diphtheriae DSM43989 under oxidative stress as well as its NaOCl stress response.

2017-07-17 | PXD003321 | Pride

Regulation of titin-based cardiac stiffness by unfolded domain oxidation (UnDOx)

Project description:The relationship between oxidative stress and cardiac stiffness is thought to involve modifications to the giant muscle protein titin, which in turn can determine the progression of heart disease. In vitro studies have shown that S-glutathionylation and disulfide bonding of titin fragments could alter the elastic properties of titin; however, whether and where titin becomes oxidized in vivo is less certain. Here we demonstrate, using multiple models of oxidative stress in conjunction with mechanical loading, that immunoglobulin domains preferentially from the distal titin spring region become oxidized in vivo through the mechanism of unfolded domain oxidation (UnDOx). Via oxidation type-specific modification of titin, UnDOx modulates human cardiomyocyte passive force bidirectionally. UnDOx also enhances titin phosphorylation and, importantly, promotes non-constitutive folding and aggregation of unfolded domains. We propose a mechanism whereby UnDOx enables the controlled homotypic interactions within the distal titin spring to stabilize this segment and regulate myocardial passive stiffness.

2020-09-15 | PXD018174 | Pride

cys TMTRAQ_an integrative method for unbiased thiol-based redox proteomics

Project description:quantification of protein redox regulation. we combine cysteine reaction tandem mass tag(cysTMT) and isobaric tag for relative abd absolute quantification( ITRAQ) in one one experiment. we developed a double labeling strategy using iTRAQ and cysTMT in one experiment for simultaneous determination of quantifiable cysteine redox changes and protein level changes.

2017-02-02 | PXD001319 | Pride

Fly Stress - Fasting, but Not Aging, Dramatically Alters the Redox Status of Cysteine Residues on Proteins in Drosophila melanogaster

Project description:Altering the redox state of cysteine residues on protein surfaces is an important response to environmental challenges. While ageing and fasting alter many redox processes, the role of cysteine residues is uncertain. To address this we used a redox proteomic technique, Oxidative Isotope Coded Affinity TAgs (OxICAT), to assess cysteine residue redox changes in Drosophila melanogaster during ageing and fasting. This approach enabled us to simultaneously identify and quantify the redox state of several hundred cysteine residues in vivo.

2018-10-24 | PXD002195 | Pride

Changes in gene expression when the redox potential of steady state cultures of Staphylococcus aureus is lowered by addition of dithiothreitol

Project description:Staphylococcus aureus can survive in the low redox potential environment of the host cytosol. How low redox potential affects S. aureus USA300 Je2 was investigated by establishing aerobic steady state chemostat cultures and then perturbing the steady state by addition of the reducing agent dithiothreitol. These highly controlled steady state cultures allowed only one parameter (redox potential) changed. Dithiothreitol was used as a non-metabolizable reductant. Before and after perturbation samples were taken for gene expression profiling. Three independent biological replicates were analyzed.

2019-04-16 | E-MTAB-6924 | biostudies-arrayexpress

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data