Dataset Information

Hs_PanLibrary_U2OS_Hela

ABSTRACT: Hs_PanLibrary_U2OS_Hela

REANALYSIS of: PXD000953

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Others

SUBMITTER: Rosenberger G, et al.

PROVIDER: PAe005351 | PeptideAtlas | 2014-12-31

REPOSITORIES: PeptideAtlas

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Publications

A repository of assays to quantify 10,000 human proteins by SWATH-MS.

Rosenberger George G Koh Ching Chiek CC Guo Tiannan T Röst Hannes L HL Kouvonen Petri P Collins Ben C BC Heusel Moritz M Liu Yansheng Y Caron Etienne E Vichalkovski Anton A Faini Marco M Schubert Olga T OT Faridi Pouya P Ebhardt H Alexander HA Matondo Mariette M Lam Henry H Bader Samuel L SL Campbell David S DS Deutsch Eric W EW Moritz Robert L RL Tate Stephen S Aebersold Ruedi R

Scientific data 20140916

Mass spectrometry is the method of choice for deep and reliable exploration of the (human) proteome. Targeted mass spectrometry reliably detects and quantifies pre-determined sets of proteins in a complex biological matrix and is used in studies that rely on the quantitatively accurate and reproducible measurement of proteins across multiple samples. It requires the one-time, a priori generation of a specific measurement assay for each targeted protein. SWATH-MS is a mass spectrometric method th ...[more]

PMID: 25977788

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Project description:Endoglin (EDG) is a cell surface protein with an important role in the establishment of neo-angiogenesis and vasculogenic mimicry. EDG is part of the transforming growth factor-β (TGF-β) family, acting as an important co-receptor. EDG is shed from the cell surface into the extracellular compartment by matrix metalloproteinase 14 (MMP14), in its soluble form (sEDG). Both transmembrane and soluble forms of EDG exert important signaling functions in the development of new blood vessels and tumour progression. To better understand the role of EDG in Ewing sarcoma (ES), a deadly neoplasm of late childhood and adolescence, we test the efficacy of OMTX703, an endoglin-targeting antibody-drug conjugate in ES8 xenograft. Having determined an optimal dose for OMTX703, an additional experiment was conducted to assess the mechanism(s) of OMTX703 action and its potential mechanism(s) of resistance following a 2-week exposure to OMTX703 at 0, 10, 30, and 60 mg/kg; 246 proteins were assessed by reverse-phase protein array (RPPA). Analysis of variance (ANOVA), Pearson’s correlation as distance metric and Ward’s linkage as the clustering method using a false discovery rate (FDR) of 0.01, identified 60 proteins that discriminated between treatment groups (Matrix#1-Normalized Values). To investigate the proteomic changes associated with the heightened clinical activity of the 60 mg/kg dose, a secondary analysis was performed, which grouped the 10 mg/kg OMTX703 samples and the 10 mg/kg OMTX003 ones with the placebo-treated samples (Matrix#2-Normalized Values). Using a FDR of 0.0001, an absolute log2 fold change of 1.5, Pearson’s correlation as distance metric and Ward’s linkage as the clustering method, 22 proteins were discriminately identified between the 3 treatment groups (Matrix#2-Normalized Values). Notably, a protein regulator of altered metabolism (RPS6) was exclusively upregulated following OMTX703 (60mg/kg), and a second metabolism biomarker (LDHA) was down-expressed in the 30 and 60 mg/kg-treated groups. Conversely, BRD4 was one of about a dozen proteins that were preferentially down-regulated in samples treated only by 60 mg/kg.

Dataset Information

Hs_PanLibrary_U2OS_Hela

Publications

A repository of assays to quantify 10,000 human proteins by SWATH-MS.

Similar Datasets

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