Search results for "ATPases"

showing 10 items of 59 documents

An

2020

Intracellular acid stress inhibits plant growth by unknown mechanisms and it occurs in acidic soils and as consequence of other stresses. In order to identify mechanisms of acid toxicity, we screened activation-tagging lines of Arabidopsis thaliana for tolerance to intracellular acidification induced by organic acids. A dominant mutant, sbt4.13-1D, was isolated twice and shown to over-express subtilase SBT4.13, a protease secreted into endoplasmic reticulum. Activity measurements and immuno-detection indicate that the mutant contains less plasma membrane H+-ATPase (PMA) than wild type, explaining the small size, electrical depolarization and decreased cytosolic pH of the mutant but not orga…

NADPH oxidaseArabidopsis ProteinsArabidopsisNADPH OxidasesGerminationROSArticleOxidative StressProton-Translocating ATPasesMutationorganic acidsactivation-taggingH+-ATPaseSubtilisinsProtonsInternational journal of molecular sciences
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Photoaffinity cross-linking of F1ATPase from spinach chloroplasts by 3'-arylazido-beta-alanyl-8-azido ATP.

1994

UV irradiation of the ATPase (CF1) from spinach chloroplasts in the presence of 3'-arylazido-beta-alanyl-8-azido ATP (8,3'-DiN3ATP) results in a nucleotide-dependent inactivation of the enzyme and in a nucleotide-dependent formation of alpha-beta cross-links. The results demonstrate an interfacial localization of the nucleotide binding sites on CF1.

Nucleotide binding siteAzidesChloroplastsStereochemistryPhotochemistryAffinity labelATPaseBiophysicsBiochemistryChloroplastF1ATPasechemistry.chemical_compoundAdenosine TriphosphateStructural BiologyVegetablesGeneticsBinding siteChenopodiaceaeInterfacial localizationMolecular BiologyPhotoaffinity cross-linkingchemistry.chemical_classificationbiologyfood and beveragesAffinity LabelsCell Biologybiology.organism_classificationChloroplastProton-Translocating ATPasesEnzymeCross-Linking Reagentschemistrybiology.proteinSpinach chloroplastAdenosine triphosphateFEBS letters
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Progress in neuropathology of the neuronal ceroid lipofuscinoses.

1999

Abstract Since the last, 6th, International Congress on Neuronal Ceroid-Lipofuscinoses, neuropathological advances in neuronal ceroid lipofuscinoses (NCL) have been made in several areas: (1) In adult NCL (ANCL) lipopigments have now been repeatedly confirmed to contain subunit c of mitochondrial ATP synthase and even sphingolipid activators (saposins). ANCL lipopigments have also been confirmed in extracerebral tissues including skin, skeletal muscle, and spleen, but not yet lymphocytes (2). Among circulating blood cells not only B cells and subclasses of T lymphocytes, i.e., CD4 + , CD8 + , and CD56 cells, but also monocytes have been found to contain NCL lipopigments, indicating that thi…

Pathologymedicine.medical_specialtyEndocrinology Diabetes and MetabolismSpleenNeuropathologyBiologyBiochemistry03 medical and health sciences0302 clinical medicineEndocrinologyNeuronal Ceroid-LipofuscinosesPrecursor cellCyclinsGeneticsmedicineMacrophageHumansVitamin E DeficiencyKufs diseaseMolecular Biology030304 developmental biologySkinNeurons0303 health sciencesMicrogliaBrainmedicine.diseaseSphingolipid3. Good healthProton-Translocating ATPasesmedicine.anatomical_structureSpinal CordMicroglia030217 neurology & neurosurgeryCD8Molecular genetics and metabolism
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Mode of cell death induction by pharmacological Vacuolar H+-ATPase (V-ATPase) inhibition.

2012

The vacuolar H+-ATPase (V-ATPase), a multisubunit proton pump, has come into focus as an attractive target in cancer invasion. However, little is known about the role of V-ATPase in cell death, and especially the underlying mechanisms remain mostly unknown. We used the myxobacterial macrolide archazolid B, a potent inhibitor of the V-ATPase, as an experimental drug as well as a chemical tool to decipher V-ATPase-related cell death signaling. We found that archazolid induced apoptosis in highly invasive tumor cells at nanomolar concentrations which was executed by the mitochondrial pathway. Prior to apoptosis induction archazolid led to the activation of a cellular stress response including …

Programmed cell deathVacuolar Proton-Translocating ATPasesCellBiologyBiochemistryCellular stress responseCell Line TumormedicineAutophagyV-ATPaseHumansEnzyme InhibitorsMolecular BiologyCell ProliferationMembrane Potential MitochondrialMicroscopy ConfocalCell DeathCell growthAutophagyCytochromes cCell BiologyCell biologymedicine.anatomical_structureApoptosisSignal transductionSignal Transduction
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Polar/Ionizable Residues in Transmembrane Segments: Effects on Helix-Helix Packing

2012

The vast majority of membrane proteins are anchored to biological membranes through hydrophobic alpha-helices. Sequence analysis of high-resolution membrane protein structures show that ionizable amino acid residues are present in transmembrane (TM) helices, often with a functional and/or structural role. Here, using as scaffold the hydrophobic TM domain of the model membrane protein glycophorin A (GpA), we address the consequences of replacing specific residues by ionizable amino acids on TM helix insertion and packing, both in detergent micelles and in biological membranes. Our findings demonstrate that ionizable residues are stably inserted in hydrophobic environments, and tolerated in t…

Protein Foldinglcsh:MedicineBiochemistryBiotecnologiaProtein Structure SecondaryCell membraneGlycophorinsAmino Acidslcsh:ScienceMicelleschemistry.chemical_classificationMultidisciplinarybiologySodium Dodecyl SulfateLipidsTransmembrane proteinAmino acidmedicine.anatomical_structureBiochemistryCytochemistryThermodynamicsResearch ArticleProtein StructureBiophysicsCalcium-Transporting ATPasesProtein ChemistryProtein–protein interactionMembranes (Biologia)MicrosomesEscherichia colimedicineGlycophorinProtein InteractionsBiologyCell Membranelcsh:RMembrane ProteinsProteinsComputational BiologyBiological membraneIntracellular MembranesProtein Structure TertiaryTransmembrane ProteinsMembrane proteinchemistryHelixbiology.proteinBiophysicslcsh:QProtein Multimerization
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Effects of sulindac sulfide on the membrane architecture and the activity of gamma-secretase.

2007

gamma-Secretase is a membrane-embedded multi-protein complex that catalyzes the final cut of the Alzheimer's disease-related amyloid precursor protein (APP) to amyloid-beta peptides of variable length (37-43 amino acids) via an unusual intramembrane cleavage. Recent findings propose that some commonly used non-steroidal anti-inflammatory drugs (NSAIDs) have the ability to modulate specifically gamma-secretase activity without inhibiting the enzyme as a whole. These drugs may shift the processing of APP from the longer amyloid-beta 42 peptide towards shorter, less fibrillogenic and less toxic amyloid-beta species. We hypothesize that gamma-secretase activity, as an enzyme that is strictly as…

Protein subunitBlotting WesternPeptideCHO CellsSarcoplasmic Reticulum Calcium-Transporting ATPasesCellular and Molecular NeuroscienceAmyloid beta-Protein PrecursorCricetulusMembrane MicrodomainsSulindacCricetinaemental disordersAmyloid precursor proteinPresenilin-1AnimalsHumansLipid raftCells CulturedPharmacologychemistry.chemical_classificationbiologyAnti-Inflammatory Agents Non-SteroidalCell MembraneP3 peptideAmino acidMembraneBiochemistrychemistrybiology.proteinBiophysicsAmyloid Precursor Protein SecretasesAmyloid precursor protein secretaseNeuropharmacology
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Cercospora beticola toxins. Part XVII. The role of the beticolin/Mg2+ complexes in their biological activity Study of plasma membrane H+-ATPase, vacu…

1996

Beticolin-1 and beticolin-2, yellow toxins produced by the phytopathogenic fungus Cercospora beticola, inhibit the plasma membrane H(+)-ATPase. Firstly, since beticolins are able to form complexes with Mg2+, the role of the beticolin/Mg2+ complexes in the inhibition of the plasma membrane proton pump has been investigated. Calculations indicate that beticolins could exist under several forms, in the H(+)-ATPase assay mixture, both free or complexed with Mg2+. However, the percentage inhibition of the H(+)-ATPase activity is correlated to the concentration of one single form of beticolin, the dimeric neutral complex Mg2H2B2, which appears to be the active form involved in the H(+)-ATPase inh…

Pyrophosphatase H+-StereochemistryATPaseAcid PhosphatasePhosphataseBiophysicsBiological Transport ActiveHeterocyclic Compounds 4 or More RingsZea maysBiochemistryMagnesium ion complexH+- PyrophosphataseMagnesiumEnzyme InhibitorsPyrophosphatasesInhibitionchemistry.chemical_classificationATPase H+-biologyChemistryVacuolar hCell MembraneSubstrate (chemistry)Biological activityCell BiologyMycotoxinsAlkaline PhosphataseCercospora beticolabiology.organism_classificationInorganic PyrophosphataseProton-Translocating ATPasesBeticolinMembraneEnzymeBiochemistryVacuolesbiology.proteinH+- ATPaseBiochimica et Biophysica Acta (BBA) - Biomembranes
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Structural dynamics in F1ATPase during the first reaction cycle of ATP hydrolysis

1991

Abstract The velocity of ATP hydrolysis, catalyzed by purified F 1 ATPase from Micrococcus luteus , was decelerated on decreasing the temperature. At 13′C one reaction cycle is completed after 20 s. Hydrolysis was triggered upon rapid mixing of the enzyme with ATP. During the first reaction cycle, succeeding structural alterations of the F 1 ATPase were traced by time resolved X-ray scattering. The scattering spectra obtained from consecutive intervals of 1 s, revealed the F 1 ATPase to pass a conformational state exhibiting an expanded (6%) molecular shape. The expanded state was observed between 45% and 65% of the time required to complete the reaction cycle. This pointx out a conformatio…

Reaction mechanismProtein ConformationStereochemistryATPaseBiophysicsTime resolved X-ray scatteringBiochemistryMicrococcusCatalysisF1ATPaseHydrolysisMolecular dynamicsAdenosine TriphosphateStructural BiologyATP hydrolysisGeneticsMolecular Biologychemistry.chemical_classificationbiologyHydrolysisX-RaysReaction cycleCell Biologybiology.organism_classificationKineticsProton-Translocating ATPasesEnzymechemistryDynamic structure transitionbiology.proteinMicrococcus luteusFEBS Letters
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Synthesis, computational docking and biological evaluation of celastrol derivatives as dual inhibitors of SERCA and P-glycoprotein in cancer therapy.

2021

Abstract A series of eleven celastrol derivatives was designed, synthesized, and evaluated for their in vitro cytotoxic activities against six human cancer cell lines (A549, HepG2, HepAD38, PC3, DLD-1 Bax-Bak WT and DKO) and three human normal cells (LO2, BEAS-2B, CCD19Lu). To our knowledge, six derivatives were the first example of dipeptide celastrol derivatives. Among them, compound 3 was the most promising derivative, as it exhibited a remarkable anti-proliferative activity and improved selectivity in liver cancer HepAD38 versus human normal hepatocytes, LO2. Compound 6 showed higher selectivity in liver cancer cells against human normal lung fibroblasts, CCD19Lu cell line. The Ca2+ mob…

SERCAAntineoplastic AgentsApoptosisPharmacologySarcoplasmic Reticulum Calcium-Transporting ATPaseschemistry.chemical_compoundStructure-Activity RelationshipCell Line TumorDrug DiscoverymedicineCytotoxic T cellHumansATP Binding Cassette Transporter Subfamily B Member 1P-glycoproteinCell ProliferationPharmacologyBinding SitesbiologyOrganic ChemistryCancerGeneral Medicinemedicine.diseaseMolecular Docking SimulationchemistryApoptosisDocking (molecular)CelastrolCell cultureDrug Resistance NeoplasmDrug Designbiology.proteinDrug Screening Assays AntitumorPentacyclic TriterpenesEuropean journal of medicinal chemistry
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Light-induced proton slip and proton leak at the thylakoid membrane

2005

A treatment of leaves of Spinacia oleracea L. with light or with the thiol reagent dithiothreitol in the dark led to partly uncoupled thylakoids. After induction in intact leaves, the partial uncoupling was irreversible at the level of isolated thylakoids. We distinguish between uncoupling by proton slip, which means a decrease of the H+/e(-) -ratio due to less efficient proton pumping, and proton leak as defined by enhanced kinetics of proton efflux. Proton slip and proton leak made about equal contributions to the total uncoupling. The enhanced proton efflux kinetics corresponded to reduction of subunit CF1-gamma of the ATP synthase as shown by fluorescence labeling of thylakoid proteins …

SpinaciaLightProtonPhysiologyKineticsAnalytical chemistryPlant ScienceThylakoidsDithiothreitolElectron Transportchemistry.chemical_compoundSpinacia oleraceaChloroplast Proton-Translocating ATPasesPhotosynthesisATP synthasebiologybiology.organism_classificationPlant LeavesDithiothreitolchemistryPhotophosphorylationThylakoidbiology.proteinBiophysicsProtonsThioredoxinAgronomy and Crop ScienceATP synthase alpha/beta subunitsJournal of Plant Physiology
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