Comparison of Lung Cancer Proteome Profiles 3: DIA
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Lung, Epithelial Cell
DISEASE(S): Lung Cancer
SUBMITTER: 
John Koomen
LAB HEAD: John Koomen
PROVIDER: PXD004684 | Pride | 2017-02-16
REPOSITORIES: Pride
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| F002526.dat | Other | |||
| F002527.dat | Other | |||
| F002528.dat | Other | |||
| F002529.dat | Other | |||
| F002531.dat | Other |
Items per page: 5 1 - 5 of 97 |
Publications
Relative protein quantification and accessible biology in lung tumor proteomes from four LC-MS/MS discovery platforms.
Stewart Paul A PA Fang Bin B Slebos Robbert J C RJ Zhang Guolin G Borne Adam L AL Fellows Katherine K Teer Jamie K JK Chen Y Ann YA Welsh Eric E Eschrich Steven A SA Haura Eric B EB Koomen John M JM
Proteomics 20170301 6
Discovery proteomics experiments include many options for sample preparation and MS data acquisition, which are capable of creating datasets for quantifying thousands of proteins. To define a strategy that would produce a dataset with sufficient content while optimizing required resources, we compared (1) single-sample LC-MS/MS with data-dependent acquisition to single-sample LC-MS/MS with data-independent acquisition and (2) peptide fractionation with label-free (LF) quantification to peptide f ...[more]
Similar Datasets
Project description:The goal of this project is to compare label free quantification, chemical labeling with tandem mass tags, and data independent acquisition discovery proteomics approaches using lung squamous cell carcinomas and adjacent lung tissues.
2017-02-16 | PXD004683 | Pride
Project description:The goal of this project is to compare label free quantification, chemical labeling with tandem mass tags, and data independent acquisition discovery proteomics approaches using lung squamous cell carcinomas and adjacent lung tissues. This additional single sample LC-MS/MS analysis with data dependent acquisition was performed to enable direct comparison to the PRIDE dataset, titled, "Comparison of Lung Cancer Proteome Profiles 3: DIA," where single samples were analyzed with LC-MS/MS using data independent acquisition.
2017-02-16 | PXD005733 | Pride
Project description:The goal of this project is to compare label free quantification, chemical labeling with tandem mass tags, and data independent acquisition discovery proteomics approaches using lung squamous cell carcinomas and adjacent lung tissues.
2017-02-16 | PXD004682 | Pride
Project description:We report an integrated analysis incorporating DNA copy number analyses, somatic exon mutations, mRNA expression via RNA-sequencing, and shotgun mass spectrometry analysis of protein abundance in 108 surgically resected squamous cell lung cancers (SCC) with accompanying clinical outcome, evaluation of tumor pathology, and other clinically relevant data. We identified three major subtypes of SCC at the proteomic level, with two groups associated with inflammation/immune response or oxidation-reduction biology. Inflamed tumors could be further sub-classified based on neutrophil infiltration or antigen presentation proteomes and reflected patterns of infiltrating immune cells. No gene mutations, mRNA signatures, or proteomic subclasses were associated with outcomes; however, the presence of B-cell rich tertiary lymph node structures could be associated with better patient outcomes. By integrating our proteogenomic data with publicly available RNA interference screen data, we identified TP63, PSAT1, and AKR1C3 as vulnerabilities in SCC, particularly in the redox proteomic group. This cohort and its deep molecular data serves as an important resource to better understand biology and targets associated with SCC.
2019-05-24 | PXD010357 | Pride
Project description:Bilateral retinoblastoma has served as a critical model for studying genetic predisposition to cancer, however international incidence of unilateral retinoblastoma is variable across populations suggesting the involvement of environmental factors. DNA from Human Papilloma Virus (HPV) has been found in human retinoblastoma tissue through polymerase chain reaction based methods in several independent reports. To search for HPV oncoproteins and characterize transcriptional profiles in retinoblastoma, we analyzed tumor tissue obtained after enucleation and cultured for one week from 13 previously untreated Mexican children with retinoblastoma. We identified the presence of E7 HPV oncoproteins using western blot analysis in HPV positive tumors, and using non-supervised methods of classification on gene expression microarrays data, tumors clustered according to the presence or absence of HPV DNA identified by PCR. These methods were unable to discriminate retinoblastoma tissues by laterality. 2,404 genes were differentially expressed between HPV positive and HPV negative retinoblastoma, including a group of genes involved in a transcriptional response to viral infection. This molecular evidence supports the hypothesis that HPV is involved in the molecular pathogenesis of these tumors. The 13 children and tumors examined here, are incident cases participating in a larger case-control study at two Pediatric Hospitals of third level of medical attention in Mexico City, that form part of the public health system. Nine different tumors positive and four negative to HPV by PCR were included in the experimental design. From these, seven are unilateral and six are bilateral and are considered biological replicas. Two unilateral and two bilateral cases were chosen to make technical replicas. From the surgical specimens, two tumor portions were obtained, one was frozen, DNA was extracted from it, and HPV status was assigned using MY09 and MY11 primers by PCR. Another portion of tumor tissue was used to grow in culture, separating viable cells from non viable cells through a ficoll gradient. In the eye, retinoblastoma usually grows into the vitreous which has no cells, and thus the tissue obtained is predominantly formed by tumor cells and few endothelial cells from capillaries in the tumor. Retinoblastoma grow in culture as non adherent cells, and when adherent cells were also present, cell suspension was moved to a new dish to keep retinoblastoma cells as the main or only cellular type as possible. We used a two channel platform with in house spotted microarrays. Since retinoblastoma has known classes: uni and bilateral, we sought to verify these classes or discover new, we used a class discovery approach and a reference experimental design. As the reference sample we used RNA form exponentially growing Saccharomyces cerevisiae because major signaling pathways and basic cellular processes among Saccharomyces cerevisiae and mammalian cells including cell cycle control and DNA repair mechanisms have a high degree of conservation. Also because yeast is easy to grow, and thus a reliable and robust source of reference RNA.
2008-05-20 | E-GEOD-11488 | biostudies-arrayexpress
Project description:Ptf1a and RbpjL form a complex. We wanted to identify genes that are regulated by the complex and distinguish those possibly regulated independently by Ptf1a and RbpjL in mouse pancreas using ChIP-seq technology. Chromatin Immunoprecipitations (ChIPs) for Ptf1a and RbpjL were performed with a number of mouse pancreas samples. Samples were sequenced with Solexa and sequenced DNA from Input (n=2), Ptf1a ChIP (n = 3), and RbpjL ChIP (n=2) samples were aligned to the NCBI Genome Build 37 M-^V mm9 to determine regions that were enriched for binding by Ptf1a and RbpjL.
2014-12-23 | E-MTAB-3197 | biostudies-arrayexpress
Project description:The proteasome recognizes target proteins that have been covalently marked by ubiquitin chains. The ubiquitin signal is subject to rapid editing at the proteasome, allowing it to reject substrates based on topological features of their attached ubiquitin chains. Editing is mediated by a key regulator of the proteasome, deubiquitinating enzyme Ubp6. The proteasome activates Ubp6, whereas Ubp6 inhibits the proteasome–both by deubiquitinating proteasome-bound ubiquitin conjugates, and through a noncatalytic effect that does not involve deubiquitination. We report mutants in both Ubp6 and proteasome subunit Rpt1 that abrogate Ubp6 activation. The Ubp6 mutations fall within its ILR element, defined here, which is conserved from yeast to mammals. The ILR is a component of the BL1 blocking loop, other parts of which obstruct ubiquitin access to the catalytic groove in free Ubp6. Rpt1 docking at the ILR opens the catalytic groove by rearranging not only BL1 but also a novel network of three directly interconnected active-site-blocking loops. Ubp6 activation and noncatalytic proteasome inhibition by Ubp6 are linked in that they were eliminated by the same Ubp6 and Rpt1 mutations. Ubp6 and ubiquitin together drive the proteasome into a unique conformational state associated with proteasome inhibition. Our results identify a multicomponent allosteric switch that exerts simultaneous control over the activity of both Ubp6 and the proteasome, and suggest that their active states are in general mutually exclusive.
2022-02-22 | PXD029402 | Pride
Project description:In a recent study, a teat disinfectant based on a nisin-producing Lactococcus cremoris displayed comparable efficacy to a conventional iodophor disinfectant in preventing dairy cow mastitis when implemented in the dairy cow milking routine. Here, we carried out a longitudinal study for an in-depth investigation of the milk proteome. Four groups of matched quarter milk with low and high somatic cell count (SCC) collected at the beginning (T0) and at the end (TF) of the trial were selected for analysis, for a total of 28 low SCC (LSCC) and 12 high SCC (HSCC) samples. The milk was delipidated, digested into peptides, and subjected to a proteomic analysis workflow entailing NanoHPLC separation and tandem mass spectrometry (LC-MS/MS) on an Orbitrap Fusion Tribrid mass spectrometer. The proteins were identified with MaxQuant, the proteomes were compared for identifying differential proteins, and their interaction networks were assessed with STRING. In LSCC milk at T0, 31 were increased or present only in the Lactococcus (L) disinfectant group (from now INCREASED in L) and 59 proteins were decreased in L disinfectant group or present only in the conventional iodophor (C) group (from now DECREASED in L). All were involved in metabolic pathways and were likely related to physiological differences between animals. In LSCC milk at TF, 34 proteins were INCREASED in L and 46 proteins were DECREASED in the L disinfectant group. Most belonged to physiological milk pathways, but 3 antimicrobial proteins were enriched in the L group at the end of the trial. In HSCC milk at T0, 54 proteins were INCREASED in L and 34 DECREASED in L. Most were involved in physiological metabolic pathways; 4 proteins with antimicrobial functions were higher in L at the beginning of the trial. In HSCC milk at TF, 67 proteins were INCREASED in L and 39 DECREASED in L. All the proteins enriched in C belonged to metabolic pathways, while up to 14 proteins enriched in L were involved in antibiotic, antimicrobial, and immune defense pathways. Cathelicidins were among the most prominent differential proteins with antimicrobial functions. At T0, cathelicidins were generally higher in HSCC than LSCC milk of both experimental groups, as expected. At TF, they were increased or unique only in the Lactococcus group, in both LSCC and HSCC milk. Western immunoblotting validation confirmed the proteomic findings. On the other hand, enzymatic assessment of n-acetyl-glucosaminidase (NAGase) did not highlight significant differences between the C and L groups, neither for LSCC nor for HSCC milk. In conclusion, the two disinfectants did not induce relevant functional changes in the milk proteome of healthy animals, except for three increased antimicrobial proteins in the Lactococcus group. On the other hand, in animals with an underlying mammary gland inflammation, the milk proteome of the Lactococcus group showed increased levels of several proteins with antibiotic, antimicrobial and immune defense functions. Among other factors, the selective immunostimulatory action of nisin, the antimicrobial effector of L. cremoris, might play a role in this observation.
2024-10-17 | PXD045030 | Pride
Project description:Twelve midlactation cows received 4 diets differing in forage-to-concentrate ration (High (HF) versus Low (LF) forage supplemented or not with lipids (HF with whole intact rapeseeds (HF-RS) and LF with sunflower oil (LF-SO)) 12 cows got into 4 groups, each cow was received 4 different diets in a latin square design Green*txt and Red_*txt raw data files contain Cy3 and Cy5 signal intensities, respectively.
2015-04-01 | E-GEOD-62728 | biostudies-arrayexpress
Project description:To better understand the signaling complexity of AXL, a member of the TAM family of receptor tyrosine kinases, we created a physical and functional map of AXL signaling interactions, phosphorylation events, and target-engagement of three AXL tyrosine kinase inhibitors (TKI). We assessed AXL protein-complexes using BioID, effects of AXL TKI on global phosphoproteins using mass spectrometry, and target engagement of AXL TKI using activity-based protein profiling. BioID identifies AXL-interacting proteins that are mostly involved in cell adhesion/migration. Global phosphoproteomics reveal that AXL inhibition deregulates phosphorylation of peptides involved in phosphatidylinositol-mediated signaling and cell adhesion/migration. Comparison of three AXL inhibitors reveals that TKI RXDX-106 inhibits pAXL, pAKT and migration/invasion of these cells without reducing their viability, while Bemcentinib exerts AXL-independent phenotypic effects. Proteomic characterization of these TKIs reveals that they inhibit diverse targets in addition to AXL, with Bemcentinib having the most off-targets. AXL and EGFR TKI co-treatment did not reverse resistance in cell line models of Erlotinib resistance. However, a unique vulnerability was identified in one persister clone, wherein combination of Bemcentinib and Erlotinib inhibited cell viability and signaling. We also show that AXL is overexpressed in ~30-40% of NSCLC but rarely in SCLC. NSCLC cells have a wide range of AXL protein expression, with basal activation detected rarely. Overall, we evaluate the mechanisms of action of AXL in lung cancer which can be used to establish assays to measure drug targetable active AXL complexes in patient tissues and inform the strategy for targeting its signaling network as an anticancer therapy.
2022-10-14 | PXD023923 | Pride