PXD013833

PXD013833 is an original dataset announced via ProteomeXchange.

Title	Vitamin C-induced breast cancer cell death is associated with remodeling the redox state of cysteine-containing proteins involved in translation and cell cycle progression
Description	Recent studies show vitamin C (VitC) pro-oxidant properties at high pharmacological concentrations which favor repurposing VitC as an anti-cancer therapeutic agent. However, redox-based anticancer properties of different forms of VitC are yet partially understood. We examined the difference between the reduced and oxidized forms of VitC, ascorbic acid (AA) and dehydroascorbic acid (DHA), in terms of cytotoxicity and redox mechanisms toward breast cancer cells. Our data showed that AA displays higher cytotoxicity towards triple-negative breast cancer (TNBC) cell lines in vitro than DHA. AA has a similar cytotoxicity on non-TNBC breast cancer cells with much less effect on noncancerous cell lines. Using MDA-MB-231, a representative TNBC cell line, we observed that cellular redox-state alterations conditioned AA- and DHA-induced cytotoxicity. Hydrogen peroxide (H2O2) accumulation extracellularly and in different intracellular compartments, and to a less degree, induced intracellular GSH oxidation, played a key role in AA-induced cytotoxicity. In contrast, DHA affected GSH oxidation and thus had less cytotoxicity. Furthermore, different cytotoxicity is observed among breast cancer cell lines. Bioinformatics analysis and biological experiments showed that peroxiredoxin 1 (PRDX1) expression levels correlates with AA differential cytotoxicity in breast cancer cells. A “redoxome” proteomics approach revealed that AA treatment altered the redox state of key antioxidant enzymes (PRDX 1-3) and a number of cysteines-containing proteins including many nucleic acid binding proteins and proteins involved in RNA, DNA and energetic processes. We showed that cell cycle progression delay and translation inhibition are parts of the underlying mechanisms for AA-induced cytotoxicity.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:56:41.465.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Thibaut LEGER
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	N-ethylmaleimide derivatized cysteine; biotinylated residue; phosphorylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion ETD

Revision	Datetime	Status	ChangeLog Entry
0	2019-05-14 02:12:58	ID requested
1	2019-08-16 00:39:57	announced
⏵ 2	2024-10-22 04:56:42	announced	2024-10-22: Updated project metadata.

El Banna N, Hatem E, Heneman-Masurel A, L, é, ger T, Ba, ï, lle D, Vernis L, Garcia C, Martineau S, Dupuy C, Vagner S, Camadro JM, Huang ME, Redox modifications of cysteine-containing proteins, cell cycle arrest and translation inhibition: Involvement in vitamin C-induced breast cancer cell death. Redox Biol, 26():101290(2019) [pubmed]

10.1016/j.redox.2019.101290;

submitter keyword: breast cancer, ascorbic acid,Vitamin C, dehydroascorbic acid, oxidative stress, redoxome

Meng-Er Huang
contact affiliation	CNRS UMR3348, Institut Curie, Bâtiment 110, Centre Universitaire, 91405 Orsay, France. Phone: 33-1-69863016; Fax: 33-1-69869429
contact email	meng-er.huang@curie.fr
lab head
Thibaut LEGER
contact affiliation	EHESP/LERES
contact email	thibaut.leger@ehesp.fr
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/08/PXD013833

PRIDE project URI

• PRIDE
  1. PXD013833
     1. Label: PRIDE project
     2. Name: Vitamin C-induced breast cancer cell death is associated with remodeling the redox state of cysteine-containing proteins involved in translation and cell cycle progression