PXD053244

PXD053244 is an original dataset announced via ProteomeXchange.

Title	PX-12 Modulates Vorinostat-induced acetylation and methylation marks in CAL 27 cells
Description	The hypoxic tumor microenvironment (TME) is a common hallmark of solid cancers, including oral squamous cell carcinoma (OSCC). Hypoxia is predominantly regulated by the hypoxia-inducible factor-1 alpha (HIF-1α) and can alter the histone acetylation and methylation profile involved in drug resistance and possible therapeutic options for solid cancer. Vorinostat (suberoylanilide hydroxamic acid, SAHA) is a histone deacetylase inhibitor (HDACi) that targets HIF-1α stability, whereas PX-12 (1-methylpropyl 2-imidazolyl disulfide) is a thioredoxin-1 (Trx-1) inhibitor that prevents HIF-1α accumulation. Although HDACi are efficient in cancer treatment, they are accompanied by several adverse effects and increased resistance. This can be averted by combining HDACi with a Trx-1 inhibitor, as both inhibitors are connected by interlinked inhibitory pathways. HDACi inhibit Trx-1, leading to elevated reactive oxygen species (ROS) formation and death in cancerous cells; consequently, utilizing a Trx-1 inhibitor can boost the efficacy of HDACi. Previously, we investigated a synergistic interaction between vorinostat and PX-12 in an oral squamous carcinoma (OSCC) cell line under hypoxia. Here, we report to determine the effect of both inhibitors on histone acetylation and methylation expression levels under hypoxia in the CAL 27 cell line using mass spectrometry. We found several crucial histone marks, such as H3K4me1, H3K9ac, H3K9me, H3K14ac, H3K27me, H3K36me, H4K12Ac, and H4K16ac. The global analysis for histone acetylation and methylation and on specific residue shows their expression level was altered differentially by individual and combined inhibitor treatment. Our results provide an implication to investigate the underlying epigenetic mechanisms of histone acetylation and methylation levels in oral squamous cell carcinoma for a better understanding of developing drugs for cancer therapy.
HostingRepository	PRIDE
AnnounceDate	2025-05-07
AnnouncementXML	Submission_2025-05-06_20:07:03.822.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Simone Sidoli
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monomethylated residue; acetylated residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2024-06-19 20:05:20	ID requested
⏵ 1	2025-05-06 20:07:04	announced

10.1080/17501911.2024.2441652;

Akhlaq R, Ahmed T, Khan T, Yaseen Jeelani SU, Joseph-Chowdhury JN, Sidoli S, Musharraf SG, Ali A, PX-12 modulates vorinostat-induced acetylation and methylation marks in CAL 27 cells. Epigenomics, 17(2):79-87(2025) [pubmed]

submitter keyword: oral squamous cell carcinoma (OSCC), hypoxia,Histone acetylation, histone methylation, Vorinostat

Simone Sidoli
contact affiliation	Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, United States
contact email	simone.sidoli@einsteinmed.edu
lab head
Simone Sidoli
contact affiliation	Albert Einstein College of Medicine
contact email	simone.sidoli@gmail.com
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/2025/05/PXD053244

PRIDE project URI

• PRIDE
  1. PXD053244
     1. Label: PRIDE project
     2. Name: PX-12 Modulates Vorinostat-induced acetylation and methylation marks in CAL 27 cells