Search results for "phosphate"

showing 10 items of 1874 documents

Reply: 18F-FDG PET for Routine Posttreatment Surveillance in Oral and Oropharyngeal Squamous Cell Carcinoma

2010

1164 Objectives 68Ga-BPAMD (BPAMD = (4-{[bis-(phosphonomethyl))carbamoyl]methyl}-7,10-bis(carboxy methyl)-1,4,7,10-tetraazacyclododec-1-yl)acetic acid) was used in a first human in vivo study for diagnosis of osteoblastic bone metastases. The DOTA-based bisphosphonate ligand BPAMD may also be suitable for complexation with therapeutic radionuclides such as 177Lu. The same ligand thus may be used for diagnosis, dosimetry calculation, therapy and therapy control via PET/CT. Methods 177Lu was provided in 0.04 M HCl via the 176Yb(n,γ)177Yb→177Lu production process. Labelling was studied using different amounts of ligand in acetate buffer at pH 4-5 and different temperatures. For quality control…

Oncologymedicine.medical_specialtybiologyChemistrymedicine.medical_treatmentPharmacologyBisphosphonateLigand (biochemistry)Acetic acidchemistry.chemical_compoundFarnesyl diphosphate synthaseIn vivoLabellingInternal medicineRadionuclide therapymedicinebiology.proteinDOTARadiology Nuclear Medicine and imagingJournal of Nuclear Medicine
researchProduct

Improving Brain Creatine Uptake by Klotho Protein Stimulation: Can Diet Hit the Big Time?

2021

Creatine plays a pivotal role in cellular bioenergetics, acting as a temporal and spatial energy buffer in cells with high and fluctuating energy requirements (1). Jeopardizing delicate creatine homeostasis can be detrimental to many energy-demanding tissues, including the brain. For instance, cerebral creatine hypometabolism accompanies various neurological conditions, including a number of developmental disorders (2, 3), neurodegenerative and cerebrovascular diseases (4, 5), and brain cancer (6). A reduced creatine availability in the brain has been thus recognized as an apposite therapeutic target, and supplying exogenous creatine to compensate for a disease-driven shortfall emerged as a…

OpinionNutrition and Dieteticsvitamin D2Nutrition. Foods and food supplybrainKlotho (KL)Endocrinology Diabetes and Metabolismphosphate-restricted dietVDP::Medisinske Fag: 700::Helsefag: 800::Ernæring: 811creatineCT1low-calorie high-protein dietTX341-641curcuminNutritionFood ScienceFrontiers in Nutrition
researchProduct

Effect of Sitagliptin on Cardiovascular Outcomes in Type 2 Diabetes

2015

BACKGROUND: Data are lacking on the long-term effect on cardiovascular events of adding sitagliptin, a dipeptidyl peptidase 4 inhibitor, to usual care in patients with type 2 diabetes and cardiovascular disease. METHODS: In this randomized, double-blind study, we assigned 14,671 patients to add either sitagliptin or placebo to their existing therapy. Open-label use of antihyperglycemic therapy was encouraged as required, aimed at reaching individually appropriate glycemic targets in all patients. To determine whether sitagliptin was noninferior to placebo, we used a relative risk of 1.3 as the marginal upper boundary. The primary cardiovascular outcome was a composite of cardiovascular deat…

Oralmedicine.medical_specialtyHeart diseasesGlycosylatedAdministration Oralheart failureType 2 diabetesDipeptidyl peptidase-4 inhibitorKaplan-Meier EstimatePlaceboSitagliptin PhosphateSitagliptin Cardiovascular Outcomeschemistry.chemical_compoundDrug TherapyDouble-Blind MethodInternal medicineDiabetes MellitusmedicineHumansHypoglycemic AgentsGlycated HemoglobinHemoglobin A GlycosylatedAdministration Oral; Cardiovascular Diseases; Diabetes Mellitus Type 2; Double-Blind Method; Drug Therapy Combination; Follow-Up Studies; Heart Diseases; Heart Failure; Hemoglobin A Glycosylated; Hospitalization; Humans; Hypoglycemic Agents; Kaplan-Meier Estimate; Pyrazines; Sitagliptin Phosphate; Triazoles; Medicine (all)business.industryMedicine (all)SemaglutideSitagliptin PhosphateHemoglobin AGeneral MedicineTriazolesta3121medicine.diseaseSurgeryHospitalizationCardiovascular diseaseschemistryDiabetes Mellitus Type 2SitagliptinPyrazinesAdministrationCombinationDrug Therapy CombinationGlycated hemoglobinbusinessType 2Alogliptinmedicine.drugFollow-Up StudiesNew England Journal of Medicine
researchProduct

Host–guest blue light-emitting electrochemical cells

2014

Carbazole, a commonly used hole-transporter for organic electronics, has been modified with an imidazolium cation and a hexafluorophosphate counter-anion to give an ionic hole-transporter. It has been applied as one of the hosts in a host–guest blue light-emitting electrochemical cell (LEC) with the neutral blue emitter FIrPic. We have obtained efficient and bright blue LECs with an electroluminescence maximum at 474 nm and efficacy of 5 cd A−1 at a luminance of 420 cd m−2, thereby demonstrating the potential of the ionic organic charge-transporters and of the host–guest architecture for LECs.

Organic electronicsMaterials scienceCarbazoleInorganic chemistryIonic bondingGeneral ChemistryElectroluminescenceElectrochemical cellchemistry.chemical_compoundchemistryHexafluorophosphateMaterials ChemistryCommon emitterBlue lightJ. Mater. Chem. C
researchProduct

Cytotoxic Action of Serratia marcescens Hemolysin on Human Epithelial Cells

1999

ABSTRACT Incubation of human epithelial cells with nanomolar concentrations of chromatographically purified Serratia marcescens hemolysin (ShlA) caused irreversible vacuolation and subsequent lysis of the cells. Vacuolation differed from vacuole formation by Helicobacter pylori VacA. Sublytic doses of ShlA led to a reversible depletion of intracellular ATP. Restoration to the initial ATP level was presumably due to the repair of the toxin damage and was inhibited by cycloheximide. Pores formed in epithelial cells and fibroblasts without disruption of the plasma membrane, and the pores appeared to be considerably smaller than those observed in artificial lipid membranes and in erythrocytes a…

OsmosisImmunologyOligosaccharidesVacuoleCycloheximideHemolysin ProteinsMicrobiologyHemolysisMicrobiologychemistry.chemical_compoundHemolysin ProteinsAdenosine TriphosphateBacterial ProteinsTumor Cells CulturedHumansPropidium iodideCytotoxicitySerratia marcescensbiologyHemolysinEpithelial CellsFibroblastsbiology.organism_classificationInfectious DiseasesEukaryotic CellschemistrySerratia marcescensMolecular and Cellular PathogenesisPotassiumParasitologyTrypan blueHeLa Cells
researchProduct

Insight into the primary mode of action of TiO2 nanoparticles on Escherichia coli in the dark.

2015

16 pages; International audience; Large-scale production and incorporation of titanium dioxide nanoparticles (NP-TiO2 ) in consumer products leads to their potential release into the environment and raises the question of their toxicity. The bactericidal mechanism of NP-TiO2 under UV light is known to involve oxidative stress due to the generation of reactive oxygen species. In the dark, several studies revealed that NP-TiO2 can exert toxicological effects. However, the mode of action of these nanoparticles is still controversial. In the present study, we used a combination of fluorescent probes to show that NP-TiO2 causes Escherichia coli membrane depolarization and loss of integrity, lead…

Osmotic stressOsmotic shock[ SDV.TOX.ECO ] Life Sciences [q-bio]/Toxicology/Ecotoxicology010501 environmental sciencesBiology[ SDV.MP.BAC ] Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriologymedicine.disease_cause01 natural sciencesBiochemistryMicrobiologyPermeability03 medical and health sciencesAdenosine TriphosphateOsmotic PressuremedicineExtracellularEscherichia coliMagnesiumMode of actionTranscriptomicsMolecular Biology030304 developmental biology0105 earth and related environmental scienceschemistry.chemical_classificationTitanium0303 health sciencesReactive oxygen speciesMicrobial ViabilityToxicityEscherichia coli ProteinsSodiumDepolarizationTitanium dioxide nanoparticlesMetabolism[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyBiochemistrychemistryBiophysicsPotassiumNanoparticles[SDV.TOX.ECO]Life Sciences [q-bio]/Toxicology/EcotoxicologyTranscriptomeOxidative stressIntracellular
researchProduct

C172S Substitution in the Chloroplast-encoded Large Subunit Affects Stability and Stress-induced Turnover of Ribulose-1,5-bisphosphate Carboxylase/Ox…

1999

Previous work has indicated that the turnover of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco; EC 4.1.1. 39) may be controlled by the redox state of certain cysteine residues. To test this hypothesis, directed mutagenesis and chloroplast transformation were employed to create a C172S substitution in the Rubisco large subunit of the green alga Chlamydomonas reinhardtii. The C172S mutant strain was not substantially different from the wild type with respect to growth rate, and the purified mutant enzyme had a normal circular dichroism spectrum. However, the mutant enzyme was inactivated faster than the wild-type enzyme at 40 and 50 degrees C. In contrast, C172S mutant …

OxygenaseChloroplastsProtein ConformationRibulose-Bisphosphate CarboxylaseMutantChlamydomonas reinhardtiiBiochemistrychemistry.chemical_compoundEnzyme StabilitySerineAnimalsCysteineMolecular BiologyCysteine metabolismRibulose 15-bisphosphatebiologyCircular DichroismRuBisCOWild typeCell Biologybiology.organism_classificationChloroplastPhenotypeAmino Acid SubstitutionchemistryBiochemistryMutagenesis Site-Directedbiology.proteinSpectrophotometry UltravioletOxidation-ReductionChlamydomonas reinhardtiiJournal of Biological Chemistry
researchProduct

Cysteines 449 and 459 modulate the reduction-oxidation conformational changes of ribulose 1.5-bisphosphate carboxylase/oxygenase and the translocatio…

2006

The role of cysteines 449 (Cys449) and 459 (Cys459) from the large subunit (LS) of ribulose 1-5-bisphosphate carboxylase/oxygenase (Rubisco) in the reduction-oxidation (redox) regulation of the enzyme was assessed by site-directed mutagenesis of these residues and chloroplast transformation of Chlamydomonas reinhardtii. In vitro studies indicated that mutations C449S, C459S or C449S/ C459S do not affect the activity and proteolytic susceptibility of the enzyme in the reduced state. However, when oxidized, the mutant enzymes differed from the wild type (WT), showing an increased resistance to inactivation and, in the case of the double mutant (DM), an altered structural conformation as refle…

OxygenaseProtein ConformationPhysiologyRibulose-Bisphosphate CarboxylaseBlotting WesternChlamydomonas reinhardtiiPlant ScienceBiologychemistry.chemical_compoundCysteinechemistry.chemical_classificationRibulose 15-bisphosphateRibuloseCell MembraneRuBisCOWild typebiology.organism_classificationPyruvate carboxylaseProtein TransportEnzymeBiochemistrychemistryMutagenesis Site-Directedbiology.proteinElectrophoresis Polyacrylamide GelOxidation-ReductionPlant, Cell and Environment
researchProduct

Modification of the proteolytic fragmentation pattern upon oxidation of cysteines from ribulose 1,5-bisphosphate carboxylase/oxygenase.

2003

The proteolytic susceptibility of the native CO 2 -fixing photosynthetic enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39, Rubisco) has been shown to increase in vitro after oxidative treatments that affect cysteine thiols. A limited incubation of oxidized (pretreated with the disulfide cystamine) Rubisco from Chlamydomonas reinhardtii with subtilisin or proteinase K generated fragments of molecular mass about 53 kDa (band I in SDS-PAGE) and 47 kDa (band II) derived from the large subunit (55 kDa) of the enzyme. In contrast, proteolysis of the reduced Rubisco (pretreated with the free thiol cysteamine) produced only the 53 kDa band. The same fragmentation pattern was repr…

OxygenaseProtein subunitRibulose-Bisphosphate CarboxylaseMolecular Sequence DataBiochemistrychemistry.chemical_compoundEndopeptidasesAnimalsEuglena gracilisAmino Acid SequenceCysteineConserved SequenceRibulose 15-bisphosphatebiologyRibuloseHydrolysisfungiRuBisCOSubtilisinPeptide FragmentsKineticsProtein SubunitschemistryBiochemistryModels Chemicalbiology.proteinProtein quaternary structureHoloenzymesOxidation-ReductionProtein Processing Post-TranslationalChlamydomonas reinhardtiiCysteineBiochemistry
researchProduct

Oxidative modification and breakdown of ribulose-1,5-bisphosphate carboxylase/oxygenase induced in Euglena gracitis by nitrogen starvation

1994

When photoheterotrophic Euglena gracilis Z Pringsheim was subjected to nitrogen (N)-deprivation, the abundant photosynthetic enzyme ribulose-1,5-bis-phosphate carboxylase/oxygenase (Rubisco; EC 4.1.1.39) was rapidly and selectively degraded. The breakdown began after a 4-h lag period and continued for a further 8 h at a steady rate. After 12 h of starvation, when the amount of Rubisco was reduced to 40%, the proteolysis of this enzyme slowed down while degradation of other proteins started at a similar pace. This resulted in a decline of culture growth, chloroplast disassembly — as witnessed by chlorophyll (Chl) loss — and cell bleaching. Experiments with spectinomycin, an inhibitor of chlo…

OxygenaseRibulose 15-bisphosphateEuglena gracilisbiologyved/biologyved/biology.organism_classification_rank.speciesRuBisCOfood and beveragesPlant Sciencebiology.organism_classificationPhotosynthesisEuglenaChloroplastchemistry.chemical_compoundBiochemistrychemistryChloroplast disassemblyGeneticsbiology.proteinPlanta
researchProduct