Search results for "PROTEOMICS"

showing 10 items of 534 documents

Proteomic fingerprinting of apple fruit, juice, and cider via combinatorial peptide ligand libraries and MS analysis

2018

Combinatorial peptide ligand libraries coupled to MS was applied to extensively map the proteome of apple fruit, and to detect its presence in commercial apple juice and cider to evaluate their authenticity and genuineness. Using the Uniprot_Malus database, 96 proteins were detected in apples, among which 30 proteins were specifically captured via combinatorial peptide ligand libraries. Next, three proteins, previously recognized in fruits, were found in apple juice, which were involved in cellular metabolism of fruit maturation and in allergenic reactions. On the other hand, only one Malus allergen was identified in cider beads eluate, demonstrating that the industrial processes did not pr…

ProteomicsMalusProteomeClinical Biochemistry02 engineering and technology01 natural sciencesBiochemistryMass SpectrometryAnalytical ChemistryFruit maturationPeptide LibraryApple allergensPeptide ligandPlant ProteinsApple allergens; Apple fruit juice and cider; Combinatorial peptide ligand library; Mass spectrometry; Proteomic fingerprintingCellular metabolismbiologyChemistry010401 analytical chemistryMs analysis021001 nanoscience & nanotechnologybiology.organism_classificationProteomic fingerprinting0104 chemical sciencesApple fruit juice and ciderFruit and Vegetable JuicesBiochemistryFruitMalusProteomeUniProtCombinatorial peptide ligand library0210 nano-technologyApple Fruit JuiceELECTROPHORESIS
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Identification of proteins in excretory/secretory extracts of Echinostoma friedi (Trematoda) from chronic and acute infections.

2006

In the present study, we describe the investigation of Echinostoma friedi excretory/secretory products using a proteomic approach combined with the use of heterologous antibodies. We have identified 18 protein spots corresponding to ten proteins, including cytoskeletal proteins like actin, tropomyosin, and paramyosin; glycolytic enzymes like enolase, glyceraldehyde 3P dehydrogenase, and aldolase; detoxifying enzymes like GSTs; and stress proteins like heat shock protein (Hsp) 70. Among these proteins, both actin and, to a lesser extent, Hsp70, exhibited differential expression patterns between chronic and acute infections in the Echinostoma-rodent model, suggesting that these proteins may p…

ProteomicsMolecular Sequence DataBiologyProteomicsBiochemistrySpecies SpecificityHeat shock proteinCricetinaeEchinostomaAnimalsAmino Acid SequenceRats WistarCytoskeletonMolecular BiologyPeptide sequenceEchinostomiasisMesocricetusAldolase AProteinsTropomyosinHsp70RatsDisease Models AnimalSecretory proteinBiochemistryAcute DiseaseChronic Diseasebiology.proteinProteomics
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The Metalloprotease Meprin β Generates Amino Terminal-truncated Amyloid β Peptide Species

2012

The amyloid β (Aβ) peptide, which is abundantly found in the brains of patients suffering from Alzheimer disease, is central in the pathogenesis of this disease. Therefore, to understand the processing of the amyloid precursor protein (APP) is of critical importance. Recently, we demonstrated that the metalloprotease meprin β cleaves APP and liberates soluble N-terminal APP (N-APP) fragments. In this work, we present evidence that meprin β can also process APP in a manner reminiscent of β-secretase. We identified cleavage sites of meprin β in the amyloid β sequence of the wild type and Swedish mutant of APP at positions p1 and p2, thereby generating Aβ variants starting at the first or seco…

ProteomicsMolecular Sequence DataMutantPeptideBiologyHydroxamic AcidsCleavage (embryo)BiochemistryCatalysis03 medical and health sciences0302 clinical medicineAlzheimer Diseasemental disordersmedicineAmyloid precursor proteinHumansProtein IsoformsAmino Acid SequenceMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesMetalloproteinaseAmyloid beta-PeptidesWild typeBrainMetalloendopeptidasesMolecular Bases of DiseaseCell Biologymedicine.diseaseMolecular biologyProtein Structure TertiaryKineticsHEK293 CellsEnzymechemistryBiochemistryMutationMetalloproteasesbiology.proteinAmyloid Precursor Protein SecretasesAlzheimer's diseasePeptides030217 neurology & neurosurgeryJournal of Biological Chemistry
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Label-free profiling of skeletal muscle using high-definition mass spectrometry

2014

We report automated and time efficient (2 h per sample) profiling of muscle using ultra-performance liquid chromatography (LC) coupled directly with high-definition mass spectrometry (HDMSE). Soluble proteins extracted from rat gastrocnemius (n=10) were digested with trypsin and analysed in duplicate using a 90 min RPLC gradient. Protein identification and label-free quantitation were performed from HDMSE spectra analysed using TransOmics Informatics for Proteomics software. In total 1,514 proteins were identified. Of these, 811 had at least 3 unique peptides and were subsequently used to assess the dynamic range and precision of LC-HDMSE label-free profiling. Proteins analysed by LC-HDMSE …

ProteomicsMuscle Proteinsta3111ProteomicsMass spectrometryBiochemistryArticleMass Spectrometryion mobilityLiquid chromatography–mass spectrometryanimal proteomicsdata-independent acquisitionmedicineAnimalsData-independent acquisitionMuscle Skeletalta315Molecular Biologychemistry.chemical_classificationChromatographyta1184Skeletal muscleTricarboxylic acidTrypsinRatsLC-MSEnzymemedicine.anatomical_structurechemistryBiochemistryChromatography Liquidmedicine.drugPROTEOMICS
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Proteomic Approaches in Colon Cancer: Promising Tools for New Cancer Markers and Drug Target Discovery

2005

Novel technologies are needed from which to identify new and more efficient biomarkers and improved molecular targets for the expedient and accurate diagnosis and treatment of colorectal cancer. Many advances have been made in direct and virtual imaging for detection of polyps and malignant-type lesions. These require tissue verification before definitive intervention. Inclusion of a simple serum test, more accurate than CEA, especially for early cancer detection, would make virtual imaging much more successful. Proteomics, the study of the proteins and protein pathways involved in disease, is a new dimension in preclinical and clinical development. Mass spectrometric analysis of serum prot…

ProteomicsNeovascularization PathologicColorectal cancerAngiogenesisbusiness.industryDrug targetProtein Array AnalysisGastroenterologyCancerDiseasemedicine.diseaseProteomicsBioinformaticsSensitivity and SpecificitySpecimen HandlingOncologyColonic NeoplasmsBiomarkers TumormedicineProtein microarrayHumansBiomarker (medicine)businessClinical Colorectal Cancer
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Integrative proteomics: functional and molecular characterization of a particular glutamate-related neuregulin isoform.

2005

Glutamate is the major excitatory neurotransmitter in the mammalian brain and is related to memory by calcium-conducting receptors. Neuregulins have emerged as long-term modulating molecules of synaptic signaling by glutamate receptors, playing a role in some cognition/memory-related disorders and moreover being part of transient functional microdomains, called lipid rafts. Here we characterize one specific isoform of neuregulin as a central biomarker for glutamate-related signaling, integrating results from in vitro and in vivo models by a differential functional and proteomic approach.

ProteomicsNeuregulin-1Glutamic AcidNerve Tissue ProteinsBiochemistryHippocampusRats Sprague-DawleyAlzheimer DiseaseAnimalsHumansLearningProtein IsoformsNeuregulin 1ReceptorLipid raftCells CulturedbiologyGlutamate receptorGeneral ChemistryGlutamic acidCell biologyRatsbiology.proteinNeuregulinCalciumFemaleSynaptic signalingSignal transductionBiomarkersSignal TransductionJournal of proteome research
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Longitudinal CSF proteome profiling in mice to uncover the acute and sustained mechanisms of action of rapid acting antidepressant (2R,6R)-hydroxynor…

2021

Delayed onset of antidepressant action is a shortcoming in depression treatment. Ketamine and its metabolite (2R,6R)-hydroxynorketamine (HNK) have emerged as promising rapid-acting antidepressants. However, their mechanism of action remains unknown. In this study, we first described the anxious and depression-prone inbred mouse strain, DBA/2J, as an animal model to assess the antidepressant-like effects of ketamine and HNK in vivo. To decode the molecular mechanisms mediating HNK's rapid antidepressant effects, a longitudinal cerebrospinal fluid (CSF) proteome profiling of its acute and sustained effects was conducted using an unbiased, hypothesis-free mass spectrometry-based proteomics app…

ProteomicsNeurophysiology and neuropsychologyanimal structuresHydroxynorketaminePhysiologyGlucocorticoid receptor signalingAntidepressantCSFNeurosciences. Biological psychiatry. NeuropsychiatryBiologyPharmacologyProteomicsBiochemistryCellular and Molecular NeuroscienceEndocrinologyGlucocorticoid receptorNeurotrophic factorsmedicineOriginal Research ArticleKetamine ; CSF ; Antidepressant ; (2R6R)-Hydroxynorketamine ; Glucocorticoid receptor signaling ; ProteomicsRC346-429Molecular BiologyPI3K/AKT/mTOR pathwayEndocrine and Autonomic SystemsQP351-495Mechanism of action(2R6R)-Hydroxynorketamineembryonic structuresAntidepressantKetamineNeurology. Diseases of the nervous systemmedicine.symptomSignal transductionRC321-571Neurobiology of Stress
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An Organometallic Gold(I) Bis‐N‐Heterocyclic Carbene Complex with Multimodal Activity in Ovarian Cancer Cells

2020

Abstract The organometallic AuI bis‐N‐heterocyclic carbene complex [Au(9‐methylcaffeine‐8‐ylidene)2]+ (AuTMX2) was previously shown to selectively and potently stabilise telomeric DNA G‐quadruplex (G4) structures. This study sheds light on the molecular reactivity and mode of action of AuTMX2 in the cellular context using mass spectrometry‐based methods, including shotgun proteomics in A2780 ovarian cancer cells. In contrast to other metal‐based anticancer agents, this organogold compound is less prone to form coordinative bonds with biological nucleophiles and is expected to exert its drug effects mainly by non‐covalent interactions. Global protein expression changes of treated cancer cell…

ProteomicsNucleolusCancer | Very Important PaperContext (language use)Antineoplastic Agents010402 general chemistryProteomicsG-quadruplex01 natural sciencesCatalysischemistry.chemical_compoundgold complexesCaffeineCell Line TumorOrganometallic CompoundscancerHumansN-heterocyclic carbenesShotgun proteomicsMode of actionOvarian NeoplasmsFull Paper010405 organic chemistryChemistryOrganic ChemistryGeneral ChemistryFull PaperstelomeresG-quadruplexes0104 chemical sciencesddc:BiochemistryCancer cellFemaleGoldCarbeneMethane
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Proteome analysis of the fungus Aspergillus carbonarius under ochratoxin A producing conditions

2011

Aspergillus carbonarius is an important ochratoxin A producing fungus that is responsible for mycotoxin contamination of grapes and wine. In this study, the proteomes of highly (W04-40) and weakly (W04-46) OTA-producing A. carbonarius strains were compared to identify proteins that may be involved in OTA biosynthesis. Protein samples were extracted from two biological replicates and subjected to two dimensional gel electrophoresis analysis and mass spectrometry. Expression profile comparison (PDQuest software), revealed 21 differential spots that were statistically significant and showed a two-fold change in expression, or greater. Among these, nine protein spots were identified by MALDI-MS…

ProteomicsOchratoxin AProteomeFungusPolymerase Chain ReactionMicrobiologyMicrobiologyFungal Proteinschemistry.chemical_compoundBiosynthesisGene expressionRNA MessengerMycotoxinchemistry.chemical_classificationTwo-dimensional gel electrophoresisbiologyGeneral Medicinebiology.organism_classificationOchratoxinsAmino acidAspergillusBiochemistrychemistrySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationProteomeFood MicrobiologyFood ScienceInternational Journal of Food Microbiology
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Reproducible and Consistent Quantification of the Saccharomyces cerevisiae Proteome by SWATH-mass spectrometry *

2015

Targeted mass spectrometry by selected reaction monitoring (S/MRM) has proven to be a suitable technique for the consistent and reproducible quantification of proteins across multiple biological samples and a wide dynamic range. This performance profile is an important prerequisite for systems biology and biomedical research. However, the method is limited to the measurements of a few hundred peptides per LC-MS analysis. Recently, we introduced SWATH-MS, a combination of data independent acquisition and targeted data analysis that vastly extends the number of peptides/proteins quantified per sample, while maintaining the favorable performance profile of S/MRM. Here we applied the SWATH-MS t…

ProteomicsOsmosisSaccharomyces cerevisiae Proteins1303 BiochemistryOsmotic shockSaccharomyces cerevisiae610 Medicine & health10071 Functional Genomics Center ZurichSaccharomyces cerevisiaeOsmosisMass spectrometryBiochemistryMass SpectrometryAnalytical Chemistry1312 Molecular BiologyData-independent acquisitionMolecular Biology1602 Analytical ChemistryChromatographybiologySelected reaction monitoringTechnological Innovation and ResourcesReproducibility of Resultsbiology.organism_classificationTargeted mass spectrometryProteomeCarbohydrate Metabolism570 Life sciences; biologyPeptidesMolecular & Cellular Proteomics
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