Search results for "MASS SPECTROMETRY"

showing 10 items of 2544 documents

Quantitative Proteomics Reveals Changes Induced by TIMP-3 on Cell Membrane Composition and Novel Metalloprotease Substrates

2021

Ectodomain shedding is a key mechanism of several biological processes, including cell-communication. Disintegrin and metalloproteinases (ADAMs), together with the membrane-type matrix metalloproteinases, play a pivotal role in shedding transmembrane proteins. Aberrant shedding is associated to several pathological conditions, including arthritis. Tissue inhibitor of metalloproteases 3 (TIMP-3), an endogenous inhibitor of ADAMs and matrix metalloproteases (MMPs), has been proven to be beneficial in such diseases. Thus, strategies to increase TIMP-3 bioavailability in the tissue have been sought for development of therapeutics. Nevertheless, high levels of TIMP-3 may lead to mechanism-based …

0301 basic medicineProteomicsADAM15ProteomeCellMatrix metalloproteinaseMass SpectrometryCell membranelcsh:Chemistryanalysis [Proteome]lcsh:QH301-705.5proteomicSpectroscopybiologyChemistrytissue inhibitor of metalloproteases 3 (TIMP-3)General MedicineTransmembrane proteinComputer Science ApplicationsCell biologymedicine.anatomical_structureEctodomainddc:540TIMP3 protein humanmetalloproteinaseectodomain sheddingmetabolism [Tissue Inhibitor of Metalloproteinase-3]Quantitative proteomicsADAM15 protein humanchemistry [Cell Membrane]Catalysismetabolism [Cell Membrane]ArticlemetalloproteinasesInorganic Chemistry03 medical and health sciencestissue inhibitor of metalloproteases 3 (TIMP-3).medicineDisintegrinHumansPhysical and Theoretical ChemistryMolecular BiologyTissue Inhibitor of Metalloproteinase-3030102 biochemistry & molecular biologyOrganic ChemistryCell MembraneMembrane Proteinsmetabolism [Proteome]ADAM Proteins030104 developmental biologyHEK293 Cellslcsh:Biology (General)lcsh:QD1-999metabolism [ADAM Proteins]biology.proteinmetabolism [Membrane Proteins]International Journal of Molecular Sciences
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SWATH-MS based quantitative proteomics analysis reveals that curcumin alters the metabolic enzyme profile of CML cells by affecting the activity of m…

2018

Background Chronic myelogenous leukemia (CML) is a myeloproliferative disorder caused by expression of the chimeric BCR-ABL tyrosine kinase oncogene, resulting from the t(9;22) chromosomal translocation. Imatinib (gleevec, STI-571) is a selective inhibitor of BCR-ABL activity highly effective in the treatment of CML. However, even though almost all CML patients respond to treatment with imatinib or third generation inhibitors, these drugs are not curative and need to be taken indefinitely or until patients become resistant. Therefore, to get a definitive eradication of leukemic cells, it is necessary to find novel therapeutic combinations, for achieving greater efficacy and fewer side effec…

0301 basic medicineProteomicsCancer ResearchCurcuminCML cellsCellReceptors Cytoplasmic and NuclearKaryopherinsTransfectionlcsh:RC254-282Mass SpectrometrymiR-22/IPO7/HIF-1α axis03 medical and health scienceschemistry.chemical_compound0302 clinical medicinemiR-22/IPO7/HIF-1α axiSettore BIO/13 - Biologia Applicatahemic and lymphatic diseasesCell Line TumorLeukemia Myelogenous Chronic BCR-ABL PositivemedicineHumansCML cells; Curcumin; miR-22/IPO7/HIF-1α axis; SWATH-MS; Oncology; Cancer ResearchOncogeneChemistryResearchCML cellImatinibTransfectionmedicine.diseaseHypoxia-Inducible Factor 1 alpha Subunitlcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogens3. Good healthMicroRNAs030104 developmental biologymedicine.anatomical_structureOncology030220 oncology & carcinogenesisCancer researchCurcuminSWATH-MSK562 CellsTyrosine kinaseK562 cellsChronic myelogenous leukemiamedicine.drug
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Self-packed core shell nano liquid chromatography columns and silica-based monolithic trap columns for targeted proteomics.

2016

Self-preparation of nano liquid chromatography (nLC) columns has advantages regarding cost and flexibility. For targeted proteomics, we evaluated several approaches for particle-packing nLC columns and manufacturing fritless silica-based monolithic trap columns (50μm inner diameter). Our preferred approach for nLC column preparation was to magnetically stir Accucore core shell particles (C18 stationary phase) in ACN/water (80/20, v/v) suspensions during pressure-driven filling of polymer-fritted standard fused silica capillaries. The columns were ready for use about one hour after preparation had begun. They had comparable peak capacities (peptides) to commercial columns, and satisfactory w…

0301 basic medicineProteomicsCapillary action01 natural sciencesBiochemistryMass SpectrometryAnalytical ChemistryNano liquid chromatographyCore shell03 medical and health sciencesColumn (typography)Cell Line TumorNano-PressureHumansMonolithChromatography High Pressure LiquidgeographyChromatographygeography.geographical_feature_categoryChemistry010401 analytical chemistryOrganic ChemistryGeneral MedicineTrap (plumbing)Silicon Dioxide0104 chemical sciencesTargeted proteomics030104 developmental biologyMicroscopy Electron ScanningCholestanetriol 26-MonooxygenaseNanoparticlesPeptidesJournal of chromatography. A
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Orange proteomic fingerprinting: From fruit to commercial juices.

2015

Combinatorial peptide ligand library technology, coupled to mass spectrometry, has been applied to extensively map the proteome of orange pulp and peel and, via this fingerprinting, to detect its presence in commercial orange juices and drinks. The native and denaturing extraction protocols have captured 1109 orange proteins, as identified by LC-MS/MS. This proteomic map has been searched in an orange concentrate, from a Spanish juice manufacturer, as well as in commercial orange juices and soft drinks. The presence of numerous orange proteins in commercial juices has demonstrated the genuineness of these products, prepared by using orange fruits as original ingredients. However, the low nu…

0301 basic medicineProteomicsProteomeOrange (colour)01 natural sciencesAnalytical ChemistryBeverages03 medical and health sciencesTandem Mass SpectrometryLc ms msFood scienceOrange juiceLC-MS/MSPeptide ligandOrange fruitPlant ProteinsOrange juiceCombinatorial peptide ligand library; LC-MS/MS; Orange fruit; Orange juice; Protein; Proteomics; Food Science; Analytical ChemistryChromatographyChemistryProtein010401 analytical chemistryGeneral Medicine0104 chemical sciences030104 developmental biologyFruitProteomeCombinatorial peptide ligand libraryCitrus × sinensisFood ScienceCitrus sinensisFood chemistry
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Proteomic fingerprinting of mistletoe (Viscum album L.) via combinatorial peptide ligand libraries and mass spectrometry analysis

2017

Abstract Combinatorial peptide ligand libraries (CPLLs), coupled to mass spectrometry (MS) analysis, have been used to investigate in depth the proteome of Viscum album L. (VA), commonly named European mistletoe, in order to provide a first proteomic fingerprinting. For this purpose, the proteins were captured via CPLLs at two different pH values (acidic and neutral). A total of 648 non-redundant proteins were identified by using two different databases. The two pH values, chosen for bead incubations, have contributed to increment the capture ability: 56% and 31% of CPLLs species were respectively recognized at pH 7.2 and at pH 2.2. Finally the biological function of identified proteins was…

0301 basic medicineProteomicsProteomeViscum albumCancer therapyBiophysicsComputational biologyBioinformaticsProteomicsMass spectrometryBiochemistry03 medical and health sciencesHuman health0302 clinical medicinePeptide LibraryViscum albumPeptide libraryPeptide ligandPlant ProteinsbiologyMass spectrometryPlant Extractsbiology.organism_classificationEuropean mistletoeProteomic fingerprinting030104 developmental biology030220 oncology & carcinogenesisProteomeCombinatorial peptide ligand library; European mistletoe; Mass spectrometry; Proteomic fingerprinting; Plant Extracts; Plant Proteins; Proteome; Viscum album; Peptide Library; Proteomics; Biophysics; BiochemistryCombinatorial peptide ligand library
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The Human Proteome Organization–Proteomics Standards Initiative Quality Control Working Group: Making quality control more accessible for biological …

2017

To have confidence in results acquired during biological mass spectrometry experiments, a systematic approach to quality control is of vital importance. Nonetheless, until now, only scattered initiatives have been undertaken to this end, and these individual efforts have often not been complementary. To address this issue, the Human Proteome Organization–Proteomics Standards Initiative has established a new working group on quality control at its meeting in the spring of 2016. The goal of this working group is to provide a unifying framework for quality control data. The initial focus will be on providing a community-driven standardized file format for quality control. For this purpose, the…

0301 basic medicineProteomicsQuality ControlProteomics Standards InitiativeProteomeChemistrymedia_common.quotation_subjectControl (management)File formatData scienceMass SpectrometryAnalytical ChemistryVariety (cybernetics)03 medical and health sciences030104 developmental biologyControl dataHuman proteome projectHumansUse caseQuality (business)Databases Proteinmedia_common
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The Small Heat Shock Protein α-Crystallin B Shows Neuroprotective Properties in a Glaucoma Animal Model

2017

Glaucoma is a neurodegenerative disease that leads to irreversible retinal ganglion cell (RGC) loss and is one of the main causes of blindness worldwide. The pathogenesis of glaucoma remains unclear, and novel approaches for neuroprotective treatments are urgently needed. Previous studies have revealed significant down-regulation of α-crystallin B as an initial reaction to elevated intraocular pressure (IOP), followed by a clear but delayed up-regulation, suggesting that this small heat-shock protein plays a pathophysiological role in the disease. This study analyzed the neuroprotective effect of α-crystallin B in an experimental animal model of glaucoma. Significant IOP elevation induced b…

0301 basic medicineProteomicsRetinal Ganglion Cellsgenetic structuresNerve fiber layerGlaucomaCell CountMass Spectrometrylcsh:ChemistryPathogenesischemistry.chemical_compound0302 clinical medicineexperimental glaucoma; α-crystallin B; neuroprotection; proteomicsProtein Interaction Mapslcsh:QH301-705.5Spectroscopyα-crystallin BGeneral MedicineComputer Science ApplicationsUp-Regulationmedicine.anatomical_structureNeuroprotective AgentsRetinal ganglion cellneuroprotectionRetinal Neuronsmedicine.medical_specialtyDown-RegulationBiologyNeuroprotectionCatalysisArticleInorganic Chemistry03 medical and health sciencesCrystallinOphthalmologyHeat shock proteinmedicineElectroretinographyAnimalsPhysical and Theoretical ChemistryMolecular BiologyIntraocular Pressureexperimental glaucomaOrganic Chemistryalpha-Crystallin B ChainRetinalGlaucomamedicine.diseaseeye diseasesDisease Models Animal030104 developmental biologylcsh:Biology (General)lcsh:QD1-999chemistry030221 ophthalmology & optometrysense organsInternational Journal of Molecular Sciences; Volume 18; Issue 11; Pages: 2418
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Data for the identification of proteins and post-translational modifications of proteins associated to histones H3 and H4 in S. cerevisiae, using tan…

2016

Tandem affinity purification method (TAP) allows the efficient purification of native protein complexes which incorporate a target protein fused with the TAP tag. Purified multiprotein complexes can then be subjected to diverse types of proteomic analyses. Here we describe the data acquired after applying the TAP strategy on histones H3 and H4 coupled with mass spectrometry to identify associated proteins and protein post-translational modifications in the budding yeast, Saccharomyces cerevisiae. The mass spectrometry dataset described here consists of 14 files generated from four different analyses in a 5600 Triple TOF (Sciex) by information‐dependent acquisition (IDA) LC–MS/MS. The above …

0301 basic medicineProteomicsSaccharomyces cerevisiaeComputational biologyProteomicsMass spectrometrylcsh:Computer applications to medicine. Medical informaticsTandem affinity purificationHistones03 medical and health scienceslcsh:Science (General)Data ArticleTandem affinity purificationMultidisciplinaryChromatography030102 biochemistry & molecular biologybiologybiology.organism_classificationYeastChromatinYeastChromatin030104 developmental biologyHistonebiology.proteinlcsh:R858-859.7Target proteinlcsh:Q1-390Post-translational modificationsData in Brief
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Label-free quantification in ion mobility-enhanced data-independent acquisition proteomics.

2016

Unbiased data-independent acquisition (DIA) strategies have gained increased popularity in the field of quantitative proteomics. The integration of ion mobility separation (IMS) into DIA workflows provides an additional dimension of separation to liquid chromatography-mass spectrometry (LC-MS), and it increases the achievable analytical depth of DIA approaches. Here we provide a detailed protocol for a label-free quantitative proteomics workflow based on ion mobility-enhanced DIA, which synchronizes precursor ion drift times with collision energies to improve precursor fragmentation efficiency. The protocol comprises a detailed description of all major steps including instrument setup, filt…

0301 basic medicineProteomicsTime FactorsProteomeComputer scienceQuantitative proteomicsProteolytic enzymesProteinsProteomicsMass spectrometryGeneral Biochemistry Genetics and Molecular BiologyChemistry Techniques AnalyticalMass Spectrometry03 medical and health sciencesLabel-free quantification030104 developmental biologyProteomeHumansData-independent acquisitionSample preparationBiological systemChromatography LiquidHeLa CellsNature protocols
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Elucidating the molecular physiology of lantibiotic NAI-107 production in Microbispora ATCC-PTA-5024.

2016

Background The filamentous actinomycete Microbispora ATCC-PTA-5024 produces the lantibiotic NAI-107, which is an antibiotic peptide effective against multidrug-resistant Gram-positive bacteria. In actinomycetes, antibiotic production is often associated with a physiological differentiation program controlled by a complex regulatory and metabolic network that may be elucidated by the integration of genomic, proteomic and bioinformatic tools. Accordingly, an extensive evaluation of the proteomic changes associated with NAI-107 production was performed on Microbispora ATCC-PTA-5024 by combining two-dimensional difference in gel electrophoresis, mass spectrometry and gene ontology approaches. R…

0301 basic medicineProteomicsfood.ingredientMetabolic networkATP-binding cassette transporterActinomycetes Antibiotic production Differential proteomics 2D-DIGE and mass spectrometry Metabolic pathways Regulatory network Molecular and cellular functionsBiologyBioinformaticsProteomicsGram-Positive Bacteria03 medical and health sciencesfoodBacteriocinsActinomycetesGenetics2D-DIGE and mass spectrometryDifferential proteomics2. Zero hungerGel electrophoresisLipid metabolismRegulatory networkbiology.organism_classificationDrug Resistance MultipleAnti-Bacterial AgentsActinobacteriaMetabolic pathway030104 developmental biologyBiochemistryMicrobisporaMetabolic pathwaysATP-Binding Cassette TransportersAntibiotic productionPeptidesBacteriaMolecular and cellular functionsBiotechnologyResearch ArticleBMC genomics
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