PXD006430

PXD006430 is an original dataset announced via ProteomeXchange.

Title	Proteomic and phosphoproteomics profiling of breast cancer cells with altered expression level of the protein phosphatase TRAP
Description	Tartrate-resistant acid phosphatase (TRAP/ACP5) is a metalloenzyme of the group of acid phosphatases. High levels of TRAP protein have been associated with the development of cancer metastasis and with clinically relevant parameters of cancer progression and cancer aggressiveness. In order to investigate the molecular pathways responsible for the role of TRAP in such cancer related processes, we examined the changes in the proteome and phosphoproteome of MDA-MB-231 breast cancer cells determined by TRAP protein overexpression or knock-down. The dataset contains two different experimental setups. The first setup consists of the comparison between MDA-MB-231 breast cancer cells stably transfected with a full-length rat TRAP (TRAP3high) and MDA-MB-231 cells transfected with a mock insert (ctrl). The second setup consists of the comparison between TRAP3high cells transfected with a scrambled shRNA (scr) and TRAP3high cells transfected with either of two shRNAs targeting TRAP (sh2 and sh3+4). In the first experimental setup, we performed quantitative phosphoproteomic and proteomic analyses using SILAC. The two analyses identified respectively 3,290 unique phosphorylation sites corresponding to 1,059 genes, and 7,957 proteins corresponding to 7,846 genes. In the second experimental setup, we performed quantitative proteomics analysis using TMT, identifying 9,848 proteins corresponding to 9,189 genes. Integrated analysis of the generated data revealed a regulation of proteins involved in the cell adhesion process and extracellular matrix organization network. In particular, TGFβ isoform 2 (TGFβ2), TGFβ receptor type 1 (TβR1) and SMAD2 protein levels were increased upon TRAP upregulation, as well as phosphorylation of CD44 on residues localized in the intracellular portion of the protein. Finally, these results were validated by functional blocking and chemical inhibition of TGFβ2/TβR, which decreased TRAP-dependent cell migration and proliferation, and by blocking of CD44, which reduced TRAP3high cell proliferation. Altogether, we show that TRAP promotes metastasis-related cell properties in breast cancer cells via TGFβ2/TβR and CD44, thereby identifying a potential signaling mechanism associated to TRAP action in breast cancer cells.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:37:05.967.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Rui Branca
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	TMT6plex-126 reporter+balance reagent acylated residue; phosphorylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos; Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2017-05-02 08:34:28	ID requested
1	2017-09-04 05:20:22	announced
2	2017-10-23 05:48:11	announced	Updated publication reference for PubMed record(s): 28915803.
⏵ 3	2024-10-22 04:37:08	announced	2024-10-22: Updated project metadata.

Reithmeier A, Panizza E, Krumpel M, Orre LM, Branca RMM, Lehti, ö J, Ek-Rylander B, Andersson G, R and CD44 in MDA-MB-231 breast cancer cells. BMC Cancer, 17(1):650(2017) [pubmed]

10.1186/s12885-017-3616-7;

curator keyword: Biomedical

submitter keyword: breast cancer, TGFbeta, CD44, ACP5, MDA-MB-231, TRAP, migration,SILAC, cell adhesion, proliferation, TMT, TGF, extracellular matrix

Janne Lehtiö
contact affiliation	Department of Oncology-Pathology, Science for Life Laboratory and Karolinska Institutet, Stockholm, Sweden
contact email	janne.lehtio@ki.se
lab head
Rui Branca
contact affiliation	Clinical Proteomics Unit, Dep. of Oncology-Pathology
contact email	rui.mamede-branca@ki.se
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/2017/09/PXD006430

PRIDE project URI

• PRIDE
  1. PXD006430
     1. Label: PRIDE project
     2. Name: Proteomic and phosphoproteomics profiling of breast cancer cells with altered expression level of the protein phosphatase TRAP