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PXD001387

PXD001387 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleProteomics of Skin Proteins in Psoriasis
DescriptionHerein we demonstrate the efficacy of an unbiased proteomics screening approach for studying protein expression changes in the KC-Tie2 psoriasis mouse model, identifying multiple protein expression changes in the mouse and validating these changes in human psoriasis. KC-Tie2 mouse skin samples (n=3) were compared with littermate controls (n=3) using gel-based fractionation followed by label-free protein expression analysis. 5482 peptides mapping to 1281 proteins were identified and quantitated: 105 proteins exhibited fold-changes ≥2.0 including: stefin A1 (average fold change of 342.4 and an average P = 0.0082; cystatin A, human orthologue); slc25a5 (average fold change of 46.2 and an average P = 0.0318); serpinb3b (average fold change of 35.6 and an average P = 0.0345; serpinB1, human orthologue); and kallikrein related peptidase 6 (average fold change of 4.7 and an average P = 0.2474; KLK6). We independently confirmed mouse gene expression-based increases of selected genes including serpinb3b (17.4-fold, P < 0.0001), KLK6 (9.0-fold, P = 0.002), stefin A1 (7.3-fold; P < 0.001) and slc25A5 (1.5-fold; P = 0.05) using qRT-PCR on a second cohort of animals (n=8). Parallel LC/MS/MS analyses on these same samples verified protein-level increases of 1.3-fold (slc25a5; P < 0.05), 29,000-fold (stefinA1; P < 0.01), 322-fold (KLK6; P < 0.0001) between KC-Tie2 and control mice. To underscore the utility and translatability of our combined approach, we analyzed gene and protein expression levels in psoriasis patient skin and primary keratinocytes vs. healthy controls. Increases in gene expression for slc25a5 (1.8-fold), cystatin A (3.0-fold), KLK6 (5.8-fold) and serpinB1 (76-fold; all P < 0.05) were observed between healthy controls and involved lesional psoriasis skin and primary psoriasis keratinocytes. Moreover slc25a5, cystatin A, KLK6 and serpinB1 protein were all increased in lesional psoriasis skin compared to normal skin. These results highlight the usefulness of preclinical disease models using readily-available mouse skin and demonstrate the utility of proteomic approaches for identifying novel peptides/proteins that are differentially regulated in psoriasis that could serve as sources of auto-antigens or provide novel therapeutic targets for the development of new anti-psoriatic treatments.
HostingRepositoryPRIDE
AnnounceDate2014-10-30
AnnouncementXMLSubmission_2014-10-30_01:52:50.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD001387
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterKathleen Lundberg
SpeciesList scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationListOxidation; Carbamidomethyl
InstrumentLTQ Orbitrap Velos
Dataset History
RevisionDatetimeStatusChangeLog Entry
02014-10-08 08:26:21ID requested
12014-10-30 01:52:51announced
Publication List
Dataset with its publication pending
Keyword List
curator keyword: Biomedical, Biological
submitter keyword: LC-MSMS, Psoriasis, Trangenic Mouse
Contact List
Mark R. Chance
contact affiliationMark R. Chance, Ph.D. Vice Dean for Research Charles W. and Iona A. Mathias Professor of Cancer Research Director, Center for Proteomics and Bioinformatics School of Medicine Case Western Reserve University 930 BRB, 10900 Euclid Ave. Cleveland OH 44106
contact emailmark.chance@case.edu
lab head
Kathleen Lundberg
contact affiliationCase Western Reserve University
contact emailkathleen.lundberg@case.edu
dataset submitter
Full Dataset Link List
Dataset FTP location
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