Search results for "Cytosol"

showing 10 items of 265 documents

3H-1,2-benzoxathiepine 2,2-dioxides: a new class of isoform-selective carbonic anhydrase inhibitors

2017

Abstract A new chemotype with carbonic anhydrase (CA, EC 4.2.1.1) inhibitory action has been discovered, the homo-sulfocoumarins (3H-1,2-benzoxathiepine 2,2-dioxides) which have been designed considering the (sulfo)coumarins as lead molecules. An original synthetic strategy of a panel of such derivatives led to compounds with a unique inhibitory profile and very high selectivity for the inhibition of the tumour associated (CA IX/XII) over the cytosolic (CA I/II) isoforms. Although the CA inhibition mechanism with these new compounds is unknown for the moment, we hypothesize that it may be similar to that of the sulfocoumarins, i.e. hydrolysis to the corresponding sulfonic acids which therea…

Gene isoformStereochemistryHigh selectivityInhibitory postsynaptic potential01 natural sciencesStructure-Activity RelationshipHydrolysisCarbonic anhydraseDrug DiscoveryHumansMoleculeCarbonic Anhydrase InhibitorsCarbonic AnhydrasesPharmacologyCarbonic anhydraseDose-Response Relationship DrugMolecular Structurebiology010405 organic chemistryChemistrylcsh:RM1-950Active sitehomo-sulfocoumarinsGeneral MedicineCyclic S-Oxides0104 chemical sciencesinhibitor010404 medicinal & biomolecular chemistryCytosollcsh:Therapeutics. PharmacologyBiochemistrysulfocoumarinbiology.proteinResearch PaperJournal of Enzyme Inhibition and Medicinal Chemistry
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Glial Protection Against Neuronal Damage

1997

Glial homeostatic mechanisms are involved in neuronal protection during the early phase of cerebral ischemia. These protective effects include, among others, glutamate uptake and the regulation of pH in the extracellular space of the brain. Uptake of glutamate goes along with glial swelling, as does the elimination of protons from the glial cytosol. Five transport systems interact in order to maintain a normal intra- and extracellular pH in the brain.

Glutamate uptakeCytosolnervous systemChemistryNeuronal damageIschemiamedicineGlutamate receptorExtracellularNeuronal protectionmedicine.diseaseHomeostasisCell biology
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Role for calnexin and N-linked glycosylation in the assembly and secretion of hepatitis B virus middle envelope protein particles.

1998

ABSTRACT Unlike those of the S and the L envelope proteins, the functional role of the related M protein in the life cycle of the hepatitis B virus (HBV) is less understood. We now demonstrate that a single N glycan, specific for M, is required for efficient secretion of M empty envelope particles. Moreover, this glycan mediates specific association of M with the chaperone calnexin. Conversely, the N glycan, common to all three envelope proteins, is involved neither in calnexin binding nor in subviral particle release. As proper folding and trafficking of M need the assistance of the chaperone, the glycan-dependent association of M with calnexin may thus play a crucial role in the assembly …

GlycanHepatitis B virusGlycosylationGlycosylationCalnexinImmunologyBiologymedicine.disease_causeMicrobiologychemistry.chemical_compoundCytosolN-linked glycosylationViral Envelope ProteinsVirologyCalnexinmedicineAnimalsSecretionPeptide sequenceHepatitis B virusBase SequenceCalcium-Binding ProteinsVirus-Cell Interactionscarbohydrates (lipids)BiochemistrychemistryOligodeoxyribonucleotidesInsect ScienceChaperone (protein)COS Cellsbiology.proteinMutagenesis Site-DirectedJournal of virology
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The inhibition of glycerol permeation through aquaglyceroporin-3 induced by mercury(II)

2016

Mercurial compounds are known to inhibit water permeation through aquaporins (AQPs). Although in the last years some hypotheses were proposed, the exact mechanism of inhibition is still an open question and even less is known about the inhibition of the glycerol permeation through aquaglyceroporins. Molecular dynamics (MD) simulations of human aquaporin-3 (AQP3) have been performed up to 200 ns in the presence of Hg2+ ions. For the first time, we have observed the unbiased passage of a glycerol molecule from the extracellular to cytosolic side. Moreover, the presence of Hg2+ ions covalently bound to Cys40 leads to a collapse of the aromatic/arginine selectivity filter (ar/R SF), blocking th…

Glycerol0301 basic medicineMolecular dynamicCell Membrane PermeabilityBiochemistryProtein Structure Secondarychemistry.chemical_compoundGLPFCOORDINATIONCRYSTALEscherichia coli ProteinsPermeationBiochemistryCovalent bondSettore CHIM/03 - Chimica Generale E InorganicaPhosphatidylcholinesCOMPLEXESProtein BindingSTRUCTURAL BASISCations DivalentPlasmodium falciparumAquaporinCYSTEINE-189Molecular Dynamics SimulationMolecular dynamicsAquaporinsWATER CHANNELInorganic Chemistry03 medical and health sciencesEscherichia coliGlycerolExtracellularHumansMoleculePERMEABILITYProtein Structure QuaternaryAquaporin 3Binding SitesAQUAPORIN INHIBITIONWaterBiological TransportMembranes ArtificialAquaglyceroporinMercurySIMULATIONSProtein Structure TertiaryCytosolWater permeation030104 developmental biologyAquaglyceroporinschemistryStructural Homology ProteinBiophysicsGlycerol permeationJournal of Inorganic Biochemistry
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The catalytic activity of the endoplasmic reticulum-resident protein microsomal epoxide hydrolase towards carcinogens is retained on inversion of its…

1996

Diol epoxides formed by the sequential action of cytochrome P-450 and the microsomal epoxide hydrolase (mEH) in the endoplasmic reticulum (ER) represent an important class of ultimate carcinogenic metabolites of polycyclic aromatic hydrocarbons. The role of the membrane orientation of cytochrome P-450 and mEH relative to each other in this catalytic cascade is not known. Cytochrome P-450 is known to have a type I topology. According to the algorithm of Hartman, Rapoport and Lodish [(1989) Proc. Natl. Acad. Sci. U.S.A. 86, 5786–5790], which allows the prediction of the membrane topology of proteins, mEH should adopt a type II membrane topology. Experimentally, mEH membrane topology has been …

GlycosylationGlycosylation1303 BiochemistryCytochromeStereochemistryMolecular Sequence Data10050 Institute of Pharmacology and Toxicology610 Medicine & healthEndoplasmic ReticulumBiochemistryCatalysis1307 Cell Biologychemistry.chemical_compoundEndoglycosidase H1312 Molecular BiologyAnimalsAmino Acid SequenceBenzopyrenesMolecular BiologyEpoxide HydrolasesbiologyEndoplasmic reticulumCell BiologyIntracellular MembranesRecombinant ProteinsRatsCytosolMembranechemistryMicrosomal epoxide hydrolaseMembrane topologyCOS Cellsbiology.proteinCarcinogensMutagenesis Site-Directed570 Life sciences; biologyResearch Article
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Rat and human liver cytosolic epoxide hydrolases: evidence for multiple forms at level of protein and mRNA.

1990

Two forms of human liver cytosolic epoxide hydrolase (cEH) with diagnostic substrate specificity for trans-stilbene oxide (cEHTSO) and cis-stilbene oxide (cEHCSO) have been identified, and cEHCSO was purified to apparent homogeneity. The enzyme had a monomer molecular weight of 49 kDa and an isoelectric point of 9.2. Pure cEHCSO hydrolyzed CSO at a rate of 145 nmole/min/mg. TSO was not metabolized at a detectable level, and like cEHTSO, the enzyme was about three times more active at pH 7.4 than at pH 9.0. Unlike cEHTSO, cEHCSO was efficiently inhibited by 1 mM 1-trichloropropene oxide (90.5%) and 1 mM STO (92%). Similarly, liver cEH purified 541-fold from fenofibrate induced Fischer 344 ra…

Health Toxicology and MutagenesisBiologyCytosolSpecies SpecificityWestern blotmedicineAnimalsHumansRNA MessengerEpoxide hydrolaseEpoxide Hydrolaseschemistry.chemical_classificationmedicine.diagnostic_testImmunochemistryPublic Health Environmental and Occupational HealthDNAMolecular biologyRatsMolecular WeightBlotIsoelectric pointEnzymeLiverBiochemistrychemistryPolyclonal antibodiesMicrosomal epoxide hydrolaseEpoxide Hydrolasesbiology.proteinResearch ArticleEnvironmental Health Perspectives
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In vitro sulfonation of 7-hydroxycoumarin derivatives in liver cytosol of human and six animal species

2020

Sulfonation is an important high affinity elimination pathway for phenolic compounds.In this study sulfonation of 7-hydroxycoumarin and 13 its derivatives were evaluated in liver cytosols of human and six animal species. 7-hydroxycoumarin and its derivatives are strongly fluorescent, and their sulfate conjugates are nonfluorescent at excitation 405 nm and emission 460 nm. A convenient fluorescence based kinetic assay of sulfonation was established.The sulfonation rate of most of the 7-hydroxycoumarin derivatives was low in liver cytosol of human and pig, whereas it was high with most compounds in dog and intermediate in rat, mouse, rabbit, and sheep. Sulfonation of the 7-hydroxycoumarin der…

Health Toxicology and MutagenesisLiver cytosolToxicologyliver030226 pharmacology & pharmacyBiochemistryArticle03 medical and health sciences0302 clinical medicineanimalhumanAnimal specieskumariinitsulfonationPharmacologyChemistrymaksaGeneral MedicinelääkeaineetIn vitroBiochemistry7-hydroxycoumarinfarmakokinetiikka030220 oncology & carcinogenesiseläimetihmiset
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Sequence-Specific Repression of Cotranslational Translocation of the Hepatitis B Virus Envelope Proteins Coincides with Binding of Heat Shock Protein…

1997

AbstractThe large L envelope protein of the hepatitis B virus has the peculiar capacity to adopt two transmembrane topologies. The N-terminal preS domain of L initially remains in the cytosol while the S domain is cotranslationally inserted into the endoplasmic reticulum membrane. The preS region of about half of the L molecules is posttranslationally translocated to the lumenal space. We now demonstrate that the repression of cotranslational translocation of preS is conferred by a preS1-specific sequence. By analysis of L deletion mutants, the cytosolic anchorage determinant was mapped to amino acid sequence 70 to 94 of L. The intrinsic potential of this determinant to suppress cotranslati…

Hepatitis B virusHSC70 Heat-Shock ProteinsRecombinant Fusion ProteinsPlasma protein bindingBiologyGenes envCytosolViral Envelope ProteinsHeat shock proteinVirologyHumansHSP70 Heat-Shock ProteinsBinding sitePromoter Regions GeneticPeptide sequenceBinding SitesBase SequenceCell-Free SystemEndoplasmic reticulumHSC70 Heat-Shock ProteinsOligonucleotides AntisenseMolecular biologyTransmembrane proteinChaperone (protein)Protein Biosynthesisbiology.proteinMutagenesis Site-DirectedMetallothioneinCarrier ProteinsProtein BindingVirology
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Chaperones Involved in Hepatitis B Virus Morphogenesis

1999

Little is known about host cell factors necessary for hepatitis B virus (HBV) assembly which involves envelopment of cytosolic nucleocapsids by the S, M and L transmembrane viral envelope proteins and subsequent budding into intraluminal cisternae. Central to virogenesis is the L protein that mediates hepatocyte receptor binding and envelopment of capsids. To serve these topologically conflicting roles, L protein exhibits an unusual dual membrane topology, disposing its N-terminal preS domain inside and outside of the virion lipid envelope. The mixed topology is achieved by posttranslational preS translocation of about half of the L protein molecules across a post-endoplasmic reticulum memb…

Hepatitis B virusProtein FoldingCalnexinHSC70 Heat-Shock ProteinsClinical BiochemistryBiochemistryViral Matrix ProteinsCytosolViral Envelope ProteinsViral envelopeCalnexinMorphogenesisAnimalsHumansHSP70 Heat-Shock ProteinsProtein PrecursorsMolecular BiologyHepatitis B Surface AntigensViral matrix proteinbiologyChemistryCalcium-Binding ProteinsHSC70 Heat-Shock ProteinsBiological TransportVirologyTransmembrane proteinCell biologyProtein BiosynthesisMembrane topologyChaperone (protein)COS Cellsbiology.proteinProtein foldingCarrier ProteinsMolecular ChaperonesBiological Chemistry
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Hepatitis B virus assembly is sensitive to changes in the cytosolic S loop of the envelope proteins.

2000

Among the three related L, M, and S envelope proteins of the hepatitis B virus (HBV), the L and S polypeptides are required for virion production. Whereas the pivotal function of the pre-S region of L in nucleocapsid envelopment has been established, the contribution of its S domain and the S protein is less clear. In this study, we evaluated the role of the cytosolic S loop, common to L and S, in HBV assembly by performing mutagenesis experiments. To distinguish between the effect of the mutations on either envelope or virion formation, we investigated the ability of the mutants to assemble into secretable subviral empty envelopes and to replace the wild-type proteins in virion maturation,…

Hepatitis B virusRecombination GeneticMutationHepatitis B virusvirusesVirus AssemblyMutantMolecular Sequence DataMorphogenesisMutagenesis (molecular biology technique)Biologymedicine.disease_causeVirologyCell biologyLoop (topology)CytosolCytosolViral Envelope ProteinsSequence Analysis ProteinVirologymedicineMutagenesis Site-DirectedHumansAmino Acid SequenceFunction (biology)Virology
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