Search results for "Enzyme Activation"

showing 10 items of 304 documents

Small molecule inhibitors and stimulators of inducible nitric oxide synthase in cancer cells from natural origin (phytochemicals, marine compounds, a…

2019

Nitric oxide synthases (NOS) are a family of isoforms, which generate nitric oxide (NO). NO is one of the smallest molecules in nature and acts mainly as a potent vasodilator. It participates in various biological processes ranging from physiological to pathological conditions. Inducible NOS (iNOS, NOS2) is a calcium-independent and inducible isoform. Despite high iNOS expression in many tumors, the role of iNOS is still unclear and complex with both enhancing and prohibiting actions in tumorigenesis. Nature presents a broad variety of natural stimulators and inhibitors, which may either promote or inhibit iNOS response. In the present review, we give an overview of iNOS-modulating agents w…

0301 basic medicineGene isoformPhytochemicalsNitric Oxide Synthase Type IIVasodilationmedicine.disease_causeBiochemistryNitric oxide03 medical and health scienceschemistry.chemical_compound0302 clinical medicineNeoplasmsmedicineAnimalsHumansEnzyme InhibitorsPharmacologyBiological ProductsNatural productMolecular StructurebiologySmall moleculeAnti-Bacterial AgentsEnzyme ActivationNitric oxide synthase030104 developmental biologyBiochemistrychemistry030220 oncology & carcinogenesisCancer cellbiology.proteinCarcinogenesisBiochemical Pharmacology
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Ellagitannin-rich cloudberry inhibits hepatocyte growth factorinduced cell migration and phosphatidylinositol 3-kinase/AKT activation in colon carcin…

2016

// Anne-Maria Pajari 1, 2 , Essi Paivarinta 1 , Lassi Paavolainen 3 , Elina Vaara 1 , Tuuli Koivumaki 4 , Ritu Garg 5 , Anu Heiman-Lindh 1 , Marja Mutanen 1 , Varpu Marjomaki 3 , Anne J. Ridley 2, 5 1 Department of Food and Environmental Sciences, Division of Nutrition, University of Helsinki, Helsinki, Finland 2 University College London, Ludwig Institute for Cancer Research, London, UK 3 Department of Biological and Environmental Science / Nanoscience Center, University of Jyvaskyla, Jyvaskyla, Finland 4 Department of Food and Environmental Sciences, Division of Food Chemistry, University of Helsinki, Helsinki, Finland 5 Randall Division of Cell & Molecular Biophysics, King’s College Lond…

0301 basic medicineMAPK/ERK pathwaycell migrationColorectal cancerCellMetastasisMicePhosphatidylinositol 3-Kinases0302 clinical medicineCell MovementHepatocyte Growth FactorHydrolyzable Tanninsmedicine.anatomical_structureOncology030220 oncology & carcinogenesisColonic NeoplasmsHepatocyte growth factormedicine.drugResearch PapersolumigraatioAntineoplastic Agentscolorectal cancerMet receptorAdenocarcinoma03 medical and health sciencesCell Line TumorellagitanninsmedicineJournal ArticleAnimalsHumansCell migrationProtein kinase Bbusiness.industryPlant Extractsta1182Cancerta3122medicine.diseaseMice Mutant StrainsMin mouseEnzyme ActivationMice Inbred C57BL030104 developmental biologyCancer cellImmunologyCancer researchbusinessRubusProto-Oncogene Proteins c-akt
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CAMKIIγ suppresses an efferocytosis pathway in macrophages and promotes atherosclerotic plaque necrosis

2017

Atherosclerosis is the underlying etiology of cardiovascular disease, the leading cause of death worldwide. Atherosclerosis is a heterogeneous disease in which only a small fraction of lesions lead to heart attack, stroke, or sudden cardiac death. A distinct type of plaque containing large necrotic cores with thin fibrous caps often precipitates these acute events. Here, we show that Ca2+/calmodulin-dependent protein kinase gamma (CaMKII gamma) in macrophages plays a major role in the development of necrotic, thin-capped plaques. Macrophages in necrotic and symptomatic atherosclerotic plaques in humans as well as advanced atherosclerotic lesions in mice demonstrated activation of CaMKII. We…

0301 basic medicineMalePathologymedicine.medical_specialtyPhagocytosisGene ExpressionInflammationApoptosisMice TransgenicBiologyPHAGOCYTOSISLIPID MEDIATORS03 medical and health sciencesNecrosisENDOPLASMIC-RETICULUM STRESSINFLAMMATIONCa2+/calmodulin-dependent protein kinaseC/EBP HOMOLOGOUS PROTEINmedicineMacrophageAnimalsHumansKINASE-IILiver X receptorEfferocytosisCells CulturedLiver X ReceptorsAPOE-DEFICIENT MICEc-Mer Tyrosine KinaseATF6MacrophagesAPOPTOTIC CELL ACCUMULATIONGeneral MedicineMERTKAtherosclerosisPlaque AtheroscleroticActivating Transcription Factor 6Enzyme ActivationMice Inbred C57BL030104 developmental biologyRESOLUTIONmedicine.symptomCalcium-Calmodulin-Dependent Protein Kinase Type 2LIVER-X-RECEPTORResearch ArticleSignal TransductionJournal of Clinical Investigation
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miR‐200c and phospho‐AKT as prognostic factors and mediators of osteosarcoma progression and lung metastasis

2016

Lung metastasis is the major cause of death in osteosarcoma patients. However, molecular mechanisms underlying this metastasis remain poorly understood. To identify key molecules related with pulmonary metastasis of pediatric osteosarcomas, we analyzed high-throughput miRNA expression in a cohort of 11 primary tumors and 15 lung metastases. Results were further validated with an independent cohort of 10 primary tumors and 6 metastases. In parallel, we performed immunohistochemical analysis of activated signaling pathways in 36 primary osteosarcomas. Only phospho-AKT associated with lower overall survival in primary tumors, supporting its role in osteosarcoma progression. CTNNB1 expression a…

0301 basic medicineOncologyMaleCancer ResearchmiR‐200cLung NeoplasmsCDH1MetastasisCohort Studies0302 clinical medicineCell MovementPhospho‐AKTPhosphorylationChildOsteosarcomabiologyGeneral MedicineArticlesCadherinsPrognosisPrimary tumorGene Expression Regulation Neoplasticmedicine.anatomical_structureLung metastasisOncology030220 oncology & carcinogenesisDisease ProgressionMolecular MedicineOsteosarcomaFemaleSignal Transductionmedicine.medical_specialtyAdolescentMesenchymal to epithelial transitionArticle03 medical and health sciencesYoung AdultAntigens CDInternal medicineCell Line TumormicroRNAGeneticsmedicineBiomarkers TumorHumansEpithelial–mesenchymal transitionCell ProliferationLungGene Expression ProfilingReproducibility of ResultsEpithelial CellsPediatric osteosarcomamedicine.diseaseSurvival AnalysisEnzyme ActivationMicroRNAs030104 developmental biologyTumor progressionbiology.proteinProto-Oncogene Proteins c-aktMolecular Oncology
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Propeptide glycosylation and galectin‐3 binding decrease proteolytic activation of human proMMP‐9/progelatinase B

2019

Matrix metalloproteinases (MMPs) are secreted as proenzymes, containing propeptides that interact with the catalytic zinc, thereby controlling MMP activation. The MMP‐9 propeptide is unique in the MMP family because of its post‐translational modification with an N‐linked oligosaccharide. ProMMP‐9 activation by MMP‐3 occurs stepwise by cleavage of the propeptide in an aminoterminal (pro‐AT) and carboxyterminal (pro‐CT) peptide. We chemically synthesized aglycosyl pro‐AT and pro‐CT and purified recombinant glycosylated pro‐ATS f−9. First, we report new cleavage sites in the MMP‐9 propeptide by MMP‐3 and neutrophil elastase. Additionally, we demonstrated with the use of western blot analysis a…

0301 basic medicinePNGase FN-linked glycosylationGlycosylationGlycosylationmatrix metalloproteinase‐9Galectin 3GalectinsProteolysisgalectin‐3Biochemistry03 medical and health scienceschemistry.chemical_compoundCongenital Disorders of Glycosylation0302 clinical medicineN-linked glycosylationmatrix metalloproteinase-9galectin-3medicineHumansZymographyAmino Acid SequenceProtein precursorMolecular BiologyN‐linked glycosylationEnzyme Precursorspropeptidemedicine.diagnostic_testbiologyBlood ProteinsOriginal ArticlesCell BiologyTrypsinEnzyme Activation030104 developmental biologyMatrix Metalloproteinase 9chemistryBiochemistryGelatinasesCase-Control Studiesproteolytic activation030220 oncology & carcinogenesisNeutrophil elastaseProteolysisbiology.proteinMatrix Metalloproteinase 3Original ArticleLeukocyte Elastasemedicine.drug
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BAX inhibitor-1 is a Ca(2+) channel critically important for immune cell function and survival.

2015

The endoplasmic reticulum (ER) serves as the major intracellular Ca(2+) store and has a role in the synthesis and folding of proteins. BAX (BCL2-associated X protein) inhibitor-1 (BI-1) is a Ca(2+) leak channel also implicated in the response against protein misfolding, thereby connecting the Ca(2+) store and protein-folding functions of the ER. We found that BI-1-deficient mice suffer from leukopenia and erythrocytosis, have an increased number of splenic marginal zone B cells and higher abundance and nuclear translocation of NF-κB (nuclear factor-κ light-chain enhancer of activated B cells) proteins, correlating with increased cytosolic and ER Ca(2+) levels. When put into culture, purifie…

0301 basic medicineProgrammed cell deathCytoplasmEncephalomyelitis Autoimmune ExperimentalCell SurvivalT-LymphocytesActive Transport Cell NucleusApoptosisBiologyEndoplasmic Reticulum03 medical and health sciencesAnimalsCalcium SignalingObesityMolecular BiologyCalcium signalingMice KnockoutOriginal PaperB-LymphocytesBAX inhibitor 1Endoplasmic reticulumNF-kappa BMembrane ProteinsCell BiologyLeukopeniaNFKB1Acquired immune systemCell biologyEnzyme ActivationMice Inbred C57BLCytosol030104 developmental biologyApoptosisCaspasesCalciumFemaleSpleen
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How Can Interleukin-1 Receptor Antagonist Modulate Distinct Cell Death Pathways?

2018

Multiple mechanisms of cell death exist (apoptosis, necroptosis, pyroptosis) and the subtle balance of several distinct proteins and inhibitors tightly regulates the cell fate toward one or the other pathway. Here, by combining coimmunoprecipitation, enzyme assays, and molecular simulations, we ascribe a new role, within this entangled regulatory network, to the interleukin-1 receptor antagonist (IL-1Ra). Our study enlightens that IL-1Ra, which usually inhibits the inflammatory effects of IL-1α/β by binding to IL-1 receptor, under advanced pathological states prevents apoptosis and/or necroptosis by noncompetitively inhibiting the activity of caspase-8 and -9. Consensus docking, followed by…

0301 basic medicineProgrammed cell deathProtein ConformationGeneral Chemical EngineeringNecroptosis-Library and Information SciencesMolecular Dynamics SimulationInhibitor of apoptosis01 natural sciencesArticle03 medical and health sciences0103 physical sciencesReceptorsmedicineCaspaseCaspase 8010304 chemical physicsbiologyCell DeathChemistryNeurodegenerationPyroptosisComputational BiologyReceptors Interleukin-1General Chemistrymedicine.diseaseCaspase 9Computer Science ApplicationsCell biologyXIAPEnzyme ActivationInterleukin 1 Receptor Antagonist Protein030104 developmental biologyApoptosisbiology.proteinThermodynamicsInterleukin-1
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P/CAF-mediated spermidine acetylation regulates histone acetyltransferase activity

2016

Histones and polyamines are important determinants of the chromatin structure. Histones form the core of nucleosome particles and their modification by acetylation of N-terminal tails is involved in chromatin structural changes and transcriptional regulation. Polyamines, including spermidine, are also targets of both cytoplasmic and nuclear acetylation, which in turn alters their affinity for DNA and nucleosomes. Previous studies report the interplay between polyamines metabolism and levels of histone acetylation, but the molecular basis of this effect is still unclear. In this work, we have analyzed the in vitro effect of spermidine on histone H3 acetylation catalyzed by P/CAF, a highly co…

0301 basic medicineSpermidine acetylationSpermidineSAP30BiologyHistones03 medical and health sciences0302 clinical medicineHistone H1Drug DiscoveryHistone H2AAnimalsHistone acetyltransferase activityp300-CBP Transcription FactorsHistone octamerHistone H3 acetylationHistone AcetyltransferasesPolytene ChromosomesPharmacologyAcetylationGeneral MedicineHistone acetyltransferaseEnzyme ActivationKineticsDrosophila melanogaster030104 developmental biologyBiochemistry030220 oncology & carcinogenesisbiology.proteinJournal of Enzyme Inhibition and Medicinal Chemistry
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Cytotoxicity of seven naturally occurring phenolic compounds towards multi-factorial drug-resistant cancer cells

2016

Abstract Introduction In medical oncology, multi-drug resistance (MDR) of cancer cells continues to be a major impediment. We are in quest of novel anti-proliferative agents to overcome drug-resistant tumor cells. Methods In the present study, we investigated the cytotoxicity of 7 naturally occurring phenolic compounds including two isoflavonoids alpinumisoflavone ( 1 ) and laburnetin ( 2 ), one biflavonoid amentoflavone ( 3) , three lignans pycnanthulignene A ( 4 ), pycnanthulignene B ( 5 ), and syringaresinol ( 7 ) and one xanthone, euxanthone ( 6 ) against 9 drug-sensitive and MDR cancer cell lines. The resazurin reduction assay was used to evaluate the cytotoxicity of these compounds, w…

0301 basic medicineSyringaresinolPharmaceutical SciencePharmacologyAmentoflavone03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePhenolsIsoflavonoidCell Line TumorNeoplasmsOxazinesDrug DiscoveryHumansCytotoxic T cellCytotoxicityMembrane Potential MitochondrialPharmacologyCell Cycle CheckpointsAlpinumisoflavoneAntineoplastic Agents PhytogenicDrug Resistance MultipleEnzyme Activation030104 developmental biologyXanthenesComplementary and alternative medicinechemistryDrug Resistance NeoplasmApoptosisCaspases030220 oncology & carcinogenesisCancer cellMolecular MedicineReactive Oxygen SpeciesPhytomedicine
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Phosphorylated immunoreceptor tyrosine-based activation motifs and integrin cytoplasmic domains activate spleen tyrosine kinase via distinct mechanis…

2018

Spleen tyrosine kinase (Syk) is involved in cellular adhesion and also in the activation and development of hematopoietic cells. Syk activation induced by genomic rearrangement has been linked to certain T-cell lymphomas, and Syk inhibitors have been shown to prolong survival of patients with B-cell lineage malignancies. Syk is activated either by its interaction with a double-phosphorylated immunoreceptor tyrosine-based activation motif (pITAM), which induces rearrangements in the Syk structure, or by the phosphorylation of specific tyrosine residues. In addition to its immunoreceptor function, Syk is activated downstream of integrin pathways, and integrins bind to the same region in Syk a…

0301 basic medicinekinaasitCell signalingentsyymitIntegrinsintegrinIntegrinAmino Acid MotifsMutation MissenseSykPeptidechemical and pharmacologic phenomenaBiochemistryspleen tyrosine kinase (Syk)environment and public healthBiokemia solu- ja molekyylibiologia - Biochemistry cell and molecular biology03 medical and health sciencesProtein DomainsLääketieteen bioteknologia - Medical biotechnologyenzyme kineticshemic and lymphatic diseasescell signalingHumansSyk KinaseTyrosinePhosphorylationCell adhesionMolecular Biologychemistry.chemical_classificationsoluviestintäintegriinit030102 biochemistry & molecular biologybiologyChemistryta1182hemic and immune systemsCell Biology3. Good healthCell biologyEnzyme Activationenzymes and coenzymes (carbohydrates)030104 developmental biologyAmino Acid SubstitutionCytoplasmbiology.proteinPhosphorylationPeptidessurface plasmon resonance (SPR)Signal Transduction
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