Search results for "Methionine"

showing 10 items of 172 documents

Paramagnetic NMR investigations of Co(II) and Ni(II) amicyanin.

1999

The paramagnetic 1H NMR spectra of the Co(II) and Ni(II) substituted forms of the type 1 blue copper protein (cupredoxin) amicyanin have been assigned. This is the first such analysis of a cupredoxin, which has a distorted tetrahedral active site with the ligands provided by two histidines, a cysteine and a methionine. The isotropic shifts of the resonances in these spectra are compared with those of Co(II) and Ni(II) azurin. A number of interesting similarities and differences are found. The coordination of the metal by the two equatorial histidine ligands is very similar in both proteins. The interaction between the introduced metal and the thiolate sulfur of the equatorial cysteine ligan…

AmicyaninMagnetic Resonance SpectroscopyCopper proteinPhotochemistryLigandsBiochemistryInorganic ChemistryMethionineBacterial ProteinsAzurinNickelHistidineHistidineBinding SitesbiologyLigandChemistryActive siteCobaltCrystallographybiology.proteinProton NMRSpectrophotometry UltravioletAzurinCopperCysteineJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
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Inhibitory effects of N-acetylcysteine on superoxide anion generation in human polymorphonuclear leukocytes.

1997

Abstract It has been suggested that reactive oxygen species released by activated polymorphonuclear leukocytes (PMN) in man is one mechanism of tissue injury. Therapeutic action aimed at increasing antioxidant defence mechanisms is still a clinical challenge. This study examines the activity of N-acetylcysteine, a known antioxidant, in the protection of PMN exposed in-vitro to the chemoattractant peptide fMet-Leu-Phe (FMLP), the protein kinase C activator phorbol myristate acetate or the lipid peroxidation promoter t-butyl hydroperoxide. FMLP (3–300 nm) and phorbol myristate acetate (160 pm–160 nm) induced concentration-related superoxide anion generation. Pre-treatment with N-acetylcystein…

AnionsAntioxidantNeutrophilsmedicine.medical_treatmentPharmaceutical Sciencechemistry.chemical_elementCalciumLipid peroxidationchemistry.chemical_compoundtert-ButylhydroperoxideSuperoxidesmedicineHumansProtein kinase CProtein Kinase CPharmacologychemistry.chemical_classificationReactive oxygen speciesSuperoxideGlutathioneMalondialdehydeMolecular biologyGlutathioneAcetylcysteinePeroxidesEnzyme ActivationN-Formylmethionine Leucyl-PhenylalanineBiochemistrychemistryTetradecanoylphorbol AcetateCalciumLipid PeroxidationThe Journal of pharmacy and pharmacology
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Ag+ Complexes as Potential Therapeutic Agents in Medicine and Pharmacy

2019

Silver is a non-essential element with promising antimicrobial and anticancer properties. This work is a detailed summary of the newest findings on the bioinorganic chemistry of silver, with a special focus on the applications of Ag+ complexes and nanoparticles. The coordination chemistry of silver is given a reasonable amount of attention, summarizing the most common silver binding sites and giving examples of such binding motifs in biologically important proteins. Possible applications of this metal and its complexes in medicine, particularly as antibacterial and antifungal agents and in cancer therapy, are discussed in detail. The most recent data on silver nanoparticles are also summari…

Antifungalsilver nanoparticlesSilvermedicine.drug_classCancer therapyMetal NanoparticlesNanoparticleAntineoplastic Agents02 engineering and technologyPharmacology010402 general chemistry01 natural sciencesBiochemistrySilver(I) complexesSilver nanoparticleCoordination complexStructure-Activity RelationshipAnti-Infective AgentsCoordination ComplexesDrug DiscoverymedicineHumansAmino Acid SequenceAmino AcidsIonsPharmacologychemistry.chemical_classificationMolecular StructureChemistryOrganic Chemistryantibacterial and anticancer activity of Ag+021001 nanoscience & nanotechnologyCombinatorial chemistry0104 chemical sciencescysteine and methionine motifsMolecular Medicine0210 nano-technologyProtein BindingCurrent Medicinal Chemistry
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Antiproliferative and chemomodulatory effects of interferon-γ on doxorubicin-sensitive and -resistant tumor cell lines

1993

Biological agents might offer various therapeutic opportunities in the treatment of cancer, including a direct and/or host-mediated antiproliferative effect and also the possibility to favorably modulate tumor resistance to antineoplastic drugs. We studied the in vitro antiproliferative effects of interferon (IFN)-gamma on the mouse B16 melanoma and Friend erythroleukemia, and the human K562 erythroleukemia, as doxorubicin (DXR)-sensitive and -resistant (multidrug resistant) variants. These effects were marked in B16 melanoma and rather slight in K562 erythroleukemia, without any difference between the DXR-sensitive and -resistant lines. The chemosensitive variant of Friend erythroleukemia …

Antimetabolites AntineoplasticCancer Researchmedicine.medical_treatmentDrug ResistanceMelanoma ExperimentalInterferon-gammaMicechemistry.chemical_compoundInterferonMethionine Sulfoximinehemic and lymphatic diseasesTumor Cells CulturedmedicineAnimalsHumansCytotoxic T cellPharmacology (medical)DoxorubicinButhionine sulfoximineInterferon gammaButhionine SulfoximinePharmacologyGlutathioneFriend murine leukemia virusCytokineOncologychemistryDoxorubicinCell cultureCancer researchLeukemia Erythroblastic AcuteCell Divisionmedicine.drugK562 cellsAnti-Cancer Drugs
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Effect of nonprotein thiols on protein synthesis in isolated rat hepatocytes.

1996

The ability of nonprotein thiols to modulate rates of protein synthesis was investigated in isolated rat hepatocytes. Addition of cysteine stimulates protein labelling by [14C]Leucine. Glutathione depletion, induced by in vivo administration of L-buthionine sulfoximine and diethylmaleate, did not alter the effect of cysteine, although it decreased the rate of protein synthesis by 32%. The effect of cysteine on protein synthesis does not seem to be related to a perturbation of the redox state of the NAD+/NADH system or to changes in the rate of gluconeogenic pathway. The following observations indicate that cysteine may stimulate protein synthesis by increasing intracellular levels of aspart…

AntimetabolitesBiologyCellular and Molecular Neurosciencechemistry.chemical_compoundMethionineMethionine SulfoximineProtein biosynthesisAnimalsButhionine sulfoximineCarbon RadioisotopesCysteineSulfhydryl CompoundsAmino AcidsRats WistarMolecular BiologyButhionine SulfoximineCells CulturedPharmacologychemistry.chemical_classificationMaleatesAminooxyacetic AcidCell BiologyGlutathioneAmino acidRatsKineticsEnzymechemistryBiochemistryLiverProtein BiosynthesisMolecular MedicineNAD+ kinaseLeucineCysteineExperientia
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Glutathione metabolism in primary astrocyte cultures: flow cytometric evidence of heterogeneous distribution of GSH content.

1993

The time-course of intracellular glutathione (GSH) values after incubation with L-buthionine-(S,R)-sulfoximine (BSO), a selective inhibitor of gamma-glutamylcysteine synthetase, showed that glutathione turns over with a half-life of 5 h. Intracellular GSH was assayed by flow cytometry using three different methods. Astrocytes showed a narrow range of cellular size but a wide range of intracellular GSH. This heterogeneity was resolved into three distinct subpopulations which represent 20%, 35% and 45% of the total astrocyte number. The less abundant subpopulation had the lower GSH content, while the most abundant was the subpopulation with the higher content. Over 95% of astrocytes were in t…

AntimetabolitesNerve Tissue ProteinsBiologyFlow cytometrychemistry.chemical_compoundCytosolMethionine SulfoximinemedicineAnimalsButhionine sulfoximineRats WistarMolecular BiologyButhionine SulfoximineCells CulturedBrain ChemistryCerebral Cortexmedicine.diagnostic_testGeneral NeuroscienceCell CycleGlutathioneMetabolismDNAHydrogen-Ion ConcentrationFlow CytometryGlutathioneRatsCytosolmedicine.anatomical_structurechemistryBiochemistryAnimals NewbornAstrocytesNeurogliaNeurology (clinical)IntracellularDevelopmental BiologyAstrocyteHalf-LifeBrain research
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Glutathione metabolism in skeletal muscle derived cells of the L6 line

1993

Skeletal muscle derived L6 myoblasts possess a considerably high resting total glutathione (TGSH) pool. Exposure to L-buthionine-[S,R]-sulphoximine resulted in a 90% depletion of the intracellular TGSH pool. All the key enzymes of glutathione metabolism, especially glutathione S-transferase, were observed to be considerably active in the undifferentiated cells. Se-dependent glutathione peroxidase activity appeared to account for most of the total GSH peroxidase activity of the cells. A significant contribution of gamma-glutamyl transpeptidase-independent (5 mM acivicin insensitive) mechanism to the extracellular GSH uptake capacity of the muscle cells was evident. Efflux of oxidized glutath…

AntioxidantGPX3AntimetabolitesPhysiologymedicine.medical_treatmentGlutathione reductaseBiologyCell Linechemistry.chemical_compoundtert-ButylhydroperoxideMethionine SulfoximinemedicineAnimalsMyocyteInhibinsButhionine SulfoximineAcivicinGlutathione TransferaseMusclesSkeletal muscleGlutathioneMetabolismGlutathioneActivinsPeroxidesRatsmedicine.anatomical_structureBiochemistrychemistryEnergy MetabolismActa Physiologica Scandinavica
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DNA methylation and histone acetylation of rat methionine adenosyltransferase 1A and 2A genes is tissue-specific.

2000

Methionine adenosyltransferase (MAT) catalyzes the biosynthesis of S-adenosylmethionine (AdoMet). In mammals MAT activity derives from two separate genes which display a tissue-specific pattern of expression. While MAT1A is expressed only in the adult liver, MAT2A is expressed in non-hepatic tissues. The mechanisms behind the selective expression of these two genes are not fully understood. In the present report we have evaluated MAT1A and MAT2A methylation in liver and in other tissues, such as kidney, by methylation-sensitive restriction enzyme digestion of genomic DNA. Our data indicate that MAT1A is hypomethylated in liver and hypermethylated in non-expressing tissues. The opposite situ…

Blotting WesternBiologyIn Vitro TechniquesKidneyBiochemistryHistonesHistone methylationAnimalsRats WistarEpigenomicsDNA methylationMyocardiumAnti-acetylated H4Kidney metabolismAcetylationCell BiologyMethylationMethionine AdenosyltransferaseDNA MethylationMolecular biologyRatsBlotting SouthernHistoneHistone acetylationLiverOrgan SpecificityMethionine AdenosyltransferaseHistone methyltransferaseDNA methylationbiology.proteinMethionine adenosyltransferaseGene expressionSpleenThe international journal of biochemistrycell biology
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[The activation of methionine for transmethylation in regenerating rat liver and hepatoma].

1958

The activity of methionine-activating enzyme has been measured in normal and regenerating rat liver and in hepatoma cells.

Cancer Researchmedicine.medical_specialtyCarcinoma HepatocellularMethionine metabolismBiochemical Phenomenachemistry.chemical_compoundMethionineInternal medicinemedicineAnimalschemistry.chemical_classificationMethionineHematologyChemistryLiver NeoplasmsGeneral Medicinedigestive system diseasesRatsLiver metabolismEnzymeOncologyBiochemistryLiverRat liverHepatoma cellTransmethylationZeitschrift fur Krebsforschung
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Streptolysin O-permeabilized granulocytes shed L-selectin concomitantly with ceramide generation via neutral sphingomyelinase

2000

Abstract Cleavage of membrane-associated L-selectin regulates leukocyte rolling on vascular endothelium at sites of inflammation. We report that rapid and massive shedding of L-selectin occurs from granulocytes attacked by the pore-forming bacterial toxin streptolysin O (SLO). Shedding was not induced by an SLO mutant that retained binding capacity but lacked pore-forming activity. Cells permeabilized with SLO exhibited a 1.5-fold increase in the activity of neutral sphingomyelinase, which was accompanied by increased ceramide formation. L-selectin cleavage was inducible by treatment of cells with bacterial sphingomyelinase, and also through exogenous application of a cell-permeable ceramid…

CeramideImmunologyInflammationCell BiologySphingomyelin phosphodiesteraseSheddaseN-Formylmethionine leucyl-phenylalanineBiologyCell biologychemistry.chemical_compoundchemistryBiochemistrymedicineImmunology and AllergyStaurosporineStreptolysinmedicine.symptomSphingomyelinmedicine.drugJournal of Leukocyte Biology
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