Search results for "Enzyme activator"

showing 10 items of 39 documents

Phenoloxidases in ascidian hemocytes: characterization of the pro-phenoloxidase activating system.

2003

The phenoloxidase (PO) activity of the hemocytes lysate supernatant from three ascidians species, assayed by means of 3-methyl-2-benzothiazolinone hydrazone hydrochloride, have been compared. PO-containing hemocytes were identified by a cytochemical reaction and the enzymatic activity measured by a spectrophotometric assay of lysate supernatant from hemocyte populations separated on a discontinuous Percoll density gradient. In Styela plicata, the enzyme appeared to be contained in morula cells only. In Ciona intestinalis, PO activity was shown in univacuolar refractile granulocyte and granular hemocyte. In Phallusia mammillata both compartment cell and granular hemocytes were positive. Enzy…

LysisHemocytesCiona intestinaliCell separationPhysiologySettore BIO/05 - ZoologiaHemocyteBiologyTunicateBiochemistryEnzyme activatormedicineAnimalsCiona intestinalisPhallusia mammillataBenzothiazolesUrochordataMolecular BiologyPolyacrylamide gel electrophoresischemistry.chemical_classificationMonophenol MonooxygenaseImmunityHydrazonesTrypsinbiology.organism_classificationMolecular biologyEnzyme ActivationThiazolesEnzymeStyela plicatachemistryStyela plicataPhenoloxidasePercollmedicine.drugComparative biochemistry and physiology. Part B, Biochemistrymolecular biology
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Emerging MEK inhibitors

2010

IMPORTANCE OF THE FIELD: The Ras/Raf/MEK/ERK pathway is often activated by genetic alterations in upstream signaling molecules. Integral components of this pathway such as Ras and B-Raf are also activated by mutation. The Ras/Raf/MEK/ERK pathway has profound effects on proliferative, apoptotic and differentiation pathways. This pathway can often be effectively silenced by MEK inhibitors. AREAS COVERED BY THIS REVIEW: This review will discuss targeting of MEK which could lead to novel methods to control abnormal proliferation which arises in cancer and other proliferative diseases. This review will cover the scientific literature from 1980 to present and is a follow on from a review which fo…

MAPK/ERK pathwayCell signalingAntineoplastic Agentsmedicine.disease_causemekerkEnzyme activatorNeoplasmsAntineoplastic Combined Chemotherapy ProtocolsmedicineAnimalsHumansPharmacology (medical)Protein phosphorylationProtein Kinase InhibitorsMEK inhibitorsCell ProliferationCancerPharmacologyapoptosis; cancer; erk; kinases; mek; mek inhibitors; proliferative disorders; protein phosphorylation; signal transductionproliferative disordersMutationKinasebusiness.industryapoptosisApoptosiCancerDrugs InvestigationalMAP Kinase Kinase Kinasesmedicine.diseaseprotein phosphorylationCell biologyEnzyme ActivationTreatment OutcomekinasesChemotherapy AdjuvantRadiotherapy AdjuvantSignal transductionbusinesssignal transductionExpert Opinion on Emerging Drugs
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17β-oestradiol up-regulates longevity-related, antioxidant enzyme expression via the ERK1 and ERK2[MAPK]/NFκB cascade

2005

Females live longer than males. Oestrogens protect females against aging by up-regulating the expression of antioxidant, longevity-related genes such as glutathione peroxidase (GPx) and Mn-superoxide dismutase (Mn-SOD). The mechanism through which oestrogens up-regulate those enzymes remains unidentified, but may have implications for gender differences in lifespan. We show that physiological concentrations of oestradiol act through oestrogen receptors to reduce peroxide levels in MCF-7 cells (a mammary gland tumour cell line). Oestradiol increases MAP kinase (MAPK) activation as indicated by ERK1 and ERK2 phosphorylation in MCF-7 cells, which in turn activates the nuclear factor kappa B (N…

MAPK/ERK pathwaychemistry.chemical_classificationAgingmedicine.medical_specialtyP50Glutathione peroxidaseCell BiologyBiologyEnzyme activatorEndocrinologyDownregulation and upregulationchemistryMitogen-activated protein kinaseInternal medicinemedicinebiology.proteinPhosphorylationskin and connective tissue diseasesReceptorAging Cell
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Post-transcriptional analysis of rat mitochondrial D-3-hydroxybutyrate dehydrogenase control through development and physiological stages.

1991

Abstract The nuclear encoded mitochondrial D -3-hydroxybutyrate dehydrogenase (BDH) is synthesized in the cytosal as a larger precursor. This membrane enzyme which requires lecithin for activity plays an essential role in energy metabolism as a ketone bodies-converting enzyme. A cDNA clone of the rat liver enzyme encompassing an antigenic determinant peptide has been isolated after immunoscreening of a λ gt11 expression library. The nucleotide sequence of this 279-base cDNA insert contains a single open reading frame of 93 amino-acids, which represents about a third of the mature enzyme. Amino-acid sequence analysis predicts a hydrophobic stretch of 29 amino-acids long which probably functi…

MaleAgingBlotting WesternMolecular Sequence DataBiologyGene Expression Regulation EnzymologicEnzyme activatorHydroxybutyrate DehydrogenaseComplementary DNAImmunoscreeningGene expressionAnimalsAmino Acid SequenceCloning MolecularRNA Processing Post-TranscriptionalGenechemistry.chemical_classificationMessenger RNASex CharacteristicsBase SequenceEstradiolRats Inbred StrainsCell BiologyGeneral MedicineDNABlotting NorthernEmbryo MammalianMolecular biologyDietary FatsMitochondriaRatsOpen reading frameEnzymeBiochemistrychemistryOrgan SpecificityFemaleCorticosteroneBiology of the cell
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Riociguat versus sildenafil on hypoxic pulmonary vasoconstriction and ventilation/perfusion matching

2017

Introduction Current treatment with vasodilators for pulmonary hypertension associated with respiratory diseases is limited by their inhibitory effect on hypoxic pulmonary vasoconstriction (HPV) and uncoupling effects on ventilation-perfusion (V'/Q'). Hypoxia is also a well-known modulator of the nitric oxide (NO) pathway, and may therefore differentially affect the responses to phosphodiesterase 5 (PDE5) inhibitors and soluble guanylyl cyclase (sGC) stimulators. So far, the effects of the sGC stimulator riociguat on HPV have been poorly characterized. Materials and methods Contraction was recorded in pulmonary arteries (PA) in a wire myograph. Anesthetized rats were catheterized to record …

MaleAnoxemiaPulmonologyPulmonary FibrosisVasodilator Agentslcsh:MedicineVasodilation030204 cardiovascular system & hematologyPharmacologyVascular Medicinechemistry.chemical_compound0302 clinical medicineSoluble Guanylyl CyclaseHypoxic pulmonary vasoconstrictionPulmonary fibrosisMedicine and Health SciencesPulmonary Arterieslcsh:ScienceHypoxiaMultidisciplinaryVasodilatorsDrugsRespiratory organs diseasesArteriesMiddle AgedChemistryPhysical Sciencescardiovascular systemFemalemedicine.symptomAnatomyMedicamentsmedicine.drugResearch ArticleChemical Elementsinorganic chemicalsSildenafilHypertension PulmonaryChronic Obstructive Pulmonary DiseaseEnzyme ActivatorsIn Vitro TechniquesPulmonary ArteryRiociguatSildenafil CitrateMalalties de l'aparell respiratori03 medical and health sciencesMedical HypoxiamedicineVentilation-Perfusion RatioAnimalsHumansRats WistarAgedPharmacologybusiness.industrylcsh:RAnoxèmiaBiology and Life SciencesHypoxia (medical)Phosphodiesterase 5 Inhibitorsmedicine.diseasePulmonary hypertensionFibrosisRatsOxygenDisease Models AnimalPyrimidines030228 respiratory systemchemistryVasoconstrictionCardiovascular AnatomyPyrazolesBlood Vesselslcsh:QSoluble guanylyl cyclasebusinessDevelopmental Biology
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Distant Homology Modeling of LCAT and Its Validation through In Silico Targeting and In Vitro and In Vivo Assays

2013

LCAT (lecithin:cholesterol acyltransferase) catalyzes the transacylation of a fatty acid of lecithin to cholesterol, generating a cholesteryl ester and lysolecithin. The knowledge of LCAT atomic structure and the identification of the amino acids relevant in controlling its structure and function are expected to be very helpful to understand the enzyme catalytic mechanism, as involved in HDL cholesterol metabolism. However - after an early report in the late '90 s - no recent advance has been made about LCAT three-dimensional structure. In this paper, we propose an LCAT atomistic model, built following the most up-to-date molecular modeling approaches, and exploiting newly solved crystallog…

MaleModels MolecularProtein StructureDrug Research and DevelopmentProtein Conformationlcsh:MedicineBiologyBiochemistryCatalysisSubstrate SpecificityPhosphatidylcholine-Sterol O-AcyltransferaseMicechemistry.chemical_compoundEnzyme activatorTransacylationProtein structureDrug DiscoveryHydrolaseCatalytic triadBiochemical SimulationsMedicine and Health SciencesAnimalsHumansHomology modelingBiomacromolecule-Ligand Interactionslcsh:SciencePharmacologyBinding SitesPlasma ProteinsMultidisciplinarylcsh:RBiology and Life SciencesProteinsEnzyme structureEnzyme ActivationMolecular Docking SimulationchemistryBiochemistryMutationEnzyme StructureEnzymologyBiocatalysisCholesteryl esterlcsh:QResearch ArticleBiotechnologyPLoS ONE
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Permissive and suppressive effects of dexamethasone on enzyme induction in hepatocyte co-cultures.

2002

1. Steroids are known to act as permissive factors in hepatocytes. This study shows that dexamethasone (DEX) is a permissive factor for induction of CYP2B1/2, CYP3A1, CYP2A1 and probably also CYP2C11 in cultures with primary rat hepatocytes. 2. The induction factor of phenobarbital (PB)-induced formation of 16beta-hydroxytestosterone (OHT), a testosterone biotransformation product predominantly formed by CYP2B1, is increased 18-fold by the addition of 32 nM DEX to the culture medium. Interestingly, higher concentrations of DEX up to 1000 nM led to a concentration-dependent maximally 5-fold decrease (p = 0.002) of phenobarbital-induced 16beta-OHT formation compared with the effect observed w…

Malemedicine.medical_specialtyTime FactorsHealth Toxicology and MutagenesisAnti-Inflammatory AgentsBiologyToxicologyBiochemistryDexamethasoneRats Sprague-DawleyEnzyme activatorInternal medicinepolycyclic compoundsmedicineCytochrome P-450 CYP1A1AnimalsCytochrome P-450 CYP3AProtein IsoformsPermissiveEnzyme inducerCytochrome P450 Family 2DexamethasoneCells CulturedPharmacologyCryopreservationDose-Response Relationship DrugBiological activityGeneral MedicineIn vitroCoculture TechniquesRatsEnzyme ActivationEndocrinologymedicine.anatomical_structureLiverSteroid 16-alpha-HydroxylaseHepatocytePhenobarbitalCytochrome P-450 CYP2B1Steroid Hydroxylasesbiology.proteinHepatocytesHydroxytestosteronesAryl Hydrocarbon HydroxylasesExcitatory Amino Acid Antagonistshormones hormone substitutes and hormone antagonistsGlucocorticoidmedicine.drugXenobiotica; the fate of foreign compounds in biological systems
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Functional and structural insights into astacin metallopeptidases

2012

The astacins are a family of multi-domain metallopeptidases with manifold functions in metabolism. They are either secreted or membrane-anchored and are regulated by being synthesized as inactive zymogens and also by colocalizing protein inhibitors. The distinct family members consist of N-terminal signal peptides and pro-segments, zincdependent catalytic domains, further downstream extracellular domains, transmembrane anchors, and cytosolic domains. The catalytic domains of four astacins and the zymogen of one of these have been structurally characterized and shown to comprise compact ~200-residue zinc-dependent moieties divided into an N-terminal and a C-terminal sub-domain by an active-s…

MetzincinSignal peptideStereochemistryMolecular Sequence DataClinical BiochemistryTolloidMatrix metalloproteinaseBiologyBiochemistryEvolution Molecular03 medical and health sciencesEnzyme activatorBone morphogenetic proteinsZymogenAnimalsHumansProtease InhibitorsAmino Acid SequenceTyrosineMolecular BiologyPeptide sequence030304 developmental biologyEnzyme Precursors0303 health sciences030302 biochemistry & molecular biologyMetalloendopeptidasesMeprinTransmembrane protein3. Good healthEnzyme ActivationBiochemistryAstacinCatalytic domainsbchm
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Effect of triterpenoids on the inflammation induced by protein kinase C activators, neuronally acting irritants and other agents.

2000

In order to establish the mode of the anti-inflammatory activity of triterpenoids, 11 naturally occurring compounds were assayed on mouse ear oedema induced by the protein kinase C activators, mezerein, 12-O-tetradecanoylphorbol-13-acetate (TPA), two 12-deoxyphorbol-13-monoesters (13-tetradecanoate (DPT) and 13-phenylacetate (DPP)) and bryostatin 1, and by resiniferatoxin, xylene and arachidonic acid. The effects on bradykinin-induced paw oedema and on the rat skin inflammation caused by hydrogen peroxide were also examined. The oedema induced by mezerein and DPT was reduced to different extents by the triterpenoids administered epicutaneously (0.5 mg per ear). Against DPT-induced oedema, l…

MezereinTime FactorsBryostatin 1ResiniferatoxinAnti-Inflammatory AgentsEnzyme ActivatorsPharmacologyBradykininchemistry.chemical_compoundGlucose OxidaseMiceAnimalsEdemaBryostatinRats WistarProtein kinase AProtein kinase CProtein Kinase CSkinPharmacologyNeurogenic inflammationArachidonic AcidMolecular StructureTerpenesBiological activityEarTriterpenesRatschemistryBiochemistryIrritantsDermatitis IrritantFemaleDiterpenesNeurogenic InflammationReactive Oxygen SpeciesEuropean journal of pharmacology
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Similar enzyme activation and catalysis in hemocyanins and tyrosinases

2006

This review presents the common features and differences of the type 3 copper proteins with respect to their structure and function. In spite of these differences a common mechanism of activation and catalysis seems to have been preserved throughout evolution. In all cases the inactive proenzymes such as tyrosinase and catecholoxidase are activated by removal of an amino acid blocking the entrance channel to the active site. No other modification at the active site seems to be necessary to enable catalytic activity. Hemocyanins, the oxygen carriers in many invertebrates, also behave as silent inactive enzymes and can be activated in the same way. The molecular basis of the catalytic process…

Models MolecularCopper proteinmedicine.medical_treatmentTyrosinaseCatalysisEnzyme activatorProtein structureGeneticsmedicineAnimalsHumanschemistry.chemical_classificationbiologyMonophenol MonooxygenaseActive siteHemocyaninGeneral MedicineProtein Structure TertiaryAmino acidEnzyme ActivationOxygenEnzymeBiochemistrychemistryHemocyaninsbiology.proteinProtein BindingGene
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