Search results for "transporters"

showing 10 items of 203 documents

Coordinated induction of drug transporters and phase I and II metabolism in human liver slices

2008

Although regulation of phase I drug metabolism in human liver is relatively well studied, the regulation of phase II enzymes and of drug transporters is incompletely characterized. Therefore, we used human liver slices to investigate the PXR, CAR and AhR-mediated induction of drug transporters and phase I and II metabolic enzymes. Precision-cut human liver slices were incubated for 5 or 24 h with prototypical inducers: phenobarbital (PB) (50 mu M) for CAR, beta-naphthoflavone (BNF) (25 mu M) for AhR, and rifampicin (RIF) (10 mu M) for PXR, and gene expression of the phase I enzymes CYP1A1, 1A2, 3A4, 3A5, 2136, 2A6, the phase II enzymes UGT1A1 and 1A6, and the transporters MRP2, MDR1, BSEP, …

DIFFERENTIAL REGULATIONQUANTITATIVE RT-PCRRAT-LIVERGene ExpressionPharmaceutical Sciencedrug transportersIn Vitro TechniquesPharmacologydigestive systemCytochrome P-450 Enzyme SystemUDP-GLUCURONOSYLTRANSFERASE 1A1Constitutive androstane receptorHumansSTELLATE CELL ACTIVATIONEnzyme inducerinductionliver slicesCONSTITUTIVE ANDROSTANE RECEPTORchemistry.chemical_classificationPregnane X receptorbiologyCYP3A4Multidrug resistance-associated protein 2TransporterPRIMARY HUMAN HEPATOCYTESMetabolic Detoxication Phase IIdrug metabolismEnzymeLiverPharmaceutical PreparationsBiochemistrychemistryEnzyme Inductionbiology.proteinMetabolic Detoxication Phase IPREGNANE-X-RECEPTORCarrier ProteinsPROTOTYPICAL INDUCERSDrug metabolismBILE-ACIDEuropean Journal of Pharmaceutical Sciences
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Cloning and characterization of the genes encoding the malolactic enzyme and the malate permease of Leuconostoc oenos

1996

Using degenerated primers from conserved regions of the protein sequences of malic enzymes, we amplified a 324-bp DNA fragment by PCR from Leuconostoc oenos and used this fragment as a probe for screening a Leuconostoc oenos genomic bank. Of the 2,990 clones in the genomic bank examined, 7 with overlapping fragments were isolated by performing colony hybridization experiments. Sequencing 3,453 bp from overlapping fragments revealed two open reading frames that were 1,623 and 942 nucleotides long and were followed by a putative terminator structure. The first deduced protein (molecular weight, 59,118) is very similar (level of similarity, 66%) to the malolactic enzyme of Lactococcus lactis; …

DNA BacterialMalolactic enzymeLeuconostoc oenosMolecular Sequence DataRestriction MappingMalatesBiological Transport ActiveOrganic Anion TransportersSaccharomyces cerevisiaeBiologyPolymerase Chain ReactionApplied Microbiology and BiotechnologyMalate dehydrogenaseOpen Reading FramesBacterial ProteinsMalate DehydrogenaseGene cluster[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyEscherichia coliLeuconostocAmino Acid SequenceCloning MolecularMalate transportDNA PrimersGenomic organizationBase SequenceSequence Homology Amino AcidEcologyLactococcus lactisNucleic acid sequenceMembrane Transport Proteinsbiology.organism_classificationMolecular biologymalate permeaseMolecular WeightOpen reading frameBiochemistryGenes BacterialLeuconostocResearch ArticleFood ScienceBiotechnologyApplied and Environmental Microbiology
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Identification of a third secondary carrier (DcuC) for anaerobic C4-dicarboxylate transport in Escherichia coli: roles of the three Dcu carriers in u…

1996

In Escherichia coli, two carriers (DcuA and DcuB) for the transport of C4 dicarboxylates in anaerobic growth were known. Here a novel gene dcuC was identified encoding a secondary carrier (DcuC) for C4 dicarboxylates which is functional in anaerobic growth. The dcuC gene is located at min 14.1 of the E. coli map in the counterclockwise orientation. The dcuC gene combines two open reading frames found in other strains of E. coli K-12. The gene product (DcuC) is responsible for the transport of C4 dicarboxylates in DcuA-DcuB-deficient cells. The triple mutant (dcuA dcuB dcuC) is completely devoid of C4-dicarboxylate transport (exchange and uptake) during anaerobic growth, and the bacteria are…

DNA BacterialMutantMolecular Sequence DataBiologymedicine.disease_causeMicrobiologyGene productBacterial ProteinsmedicineEscherichia coliDicarboxylic AcidsAmino Acid SequenceAnaerobiosisMolecular BiologyEscherichia coliPeptide sequenceGeneDicarboxylic Acid TransportersBase SequenceSequence Homology Amino AcidEscherichia coli ProteinsChromosome MappingBiological Transportbiology.organism_classificationIsoenzymesOpen reading frameMutagenesis InsertionalBiochemistryC4-dicarboxylate transportCarrier ProteinsBacteriaResearch ArticleJournal of bacteriology
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Definition of the single integration site of the pathogenicity locus in Clostridium difficile.

1996

We determined the nucleotide sequence 3.8 kb upstream and 5.2 kb downstream of the toxin genes A and B of Clostridium difficile. Nine ORFs were discovered. Based on PCR-directed approaches, two were attributed to the pathogenicity locus (PaLoc). The other seven were found in every C. difficile isolate obtained from the human gastrointestinal tract, respectless of their toxinogenicity. The ORFs cdu1 and cdu2/2' upstream of the PaLoc displayed similarity to repressors of Gram-positive bacteria (cdu1), and to an Na+/H+ antiporter described for Enterococcus hirae (cdu2/2'). Downstream of the locus a putative ABC transporter (cdd2-4) was identified. With a set of three paired primers used in pol…

DNA BacterialSequence analysisBacterial ToxinsMolecular Sequence DataVirulenceLocus (genetics)BiologyEnterotoxinsOpen Reading FramesBacterial ProteinsSpecies SpecificityGeneticsHumansAmino Acid SequenceORFSGeneGeneticsBase SequenceSequence Homology Amino AcidVirulenceClostridioides difficileNucleic acid sequenceGeneral MedicineMolecular biologyIntestinesTerminator (genetics)DNA Transposable ElementsATP-Binding Cassette TransportersMobile genetic elementsGene
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Pseudomonas corrugata crpCDE is part of the cyclic lipopeptide corpeptin biosynthetic gene cluster and is involved in bacterial virulence in tomato a…

2014

Summary: Pseudomonas corrugataCFBP 5454 produces two kinds of cyclic lipopeptides (CLPs), cormycin A and corpeptins, both of which possess surfactant, antimicrobial and phytotoxic activities. In this study, we identified genes coding for a putative non-ribosomal peptide synthetase and an ABC-type transport system involved in corpeptin production. These genes belong to the same transcriptional unit, designated crpCDE. The genetic organization of this locus is highly similar to other PseudomonasCLP biosynthetic clusters. Matrix-assisted laser desorption ionization-time of flight-mass spectrometry (MALDI-TOF-MS) analysis revealed that transporter and synthetase genomic knock-out mutants were u…

DNA BacteriallipodepsipeptidesABC transporters corpeptins Lux R transcriptional regulators non-ribosomal peptide synthetase Pseudomonas.chromobacterium-violaceumcloningPeptides CyclicLipopeptidesSolanum lycopersicumPseudomonasABC transporters Lux R transcriptional regulators non-ribosomal peptide synthetaseTobaccoPeptide SynthasesLux R transcriptional regulatorsnon-ribosomal peptide synthetasePhylogenyVLAGPlant DiseasesCell-Free SystemVirulenceputisolvin-iisyringae pv.-syringaeSettore AGR/12 - Patologia VegetaleOriginal Articlesgram-negative bacteriapeptideBiosynthetic PathwayssyringomycinRepressor ProteinssyringopeptinFood Quality and DesignABC transportersGenesGenes BacterialMultigene FamilyHost-Pathogen InteractionsMutationTrans-ActivatorsATP-Binding Cassette Transportersquorum-sensing system
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Rat adrenoleukodystrophy-related (ALDR) gene: full-length cDNA sequence and new insight in expression.

2001

X-linked adrenoleukodystrophy (X-ALD) is an inherited demyelinating disorder due to mutations in the ALD gene, which encodes a peroxisomal ABC half-transporter (ALDP). It has been suggested that ALDP assembles with ALDRP (adrenoleukodystrophy-related protein), a close homologous half-transporter, to form a functional heterodimer. For the first time full-length ALDRP cDNA (5.5 kb) was cloned, and 5' and 3' RACE analysis revealed that alternative usage of polyadenylation sites generates the two transcripts of 3.0 and 5.5 kb observed in the rat in Northern blot analysis. Southern blotting and chromosomal mapping demonstrated one ALDR locus in the rat genome. Characterisation of the 3' flanking…

DNA ComplementaryPolyadenylationMolecular Sequence DataBiophysicsLocus (genetics)BiologyATP Binding Cassette Transporter Subfamily DBiochemistryMiceFenofibrateStructural BiologyComplementary DNAGene expressionGeneticsmedicineAnimalsNorthern blotAmino Acid SequenceCloning MolecularRats WistarAdrenoleukodystrophyGene3' Untranslated RegionsSouthern blotGene LibraryGeneticsBase SequenceBrainChromosome MappingGene Expression Regulation DevelopmentalProteinsmedicine.diseaseMolecular biologyRatsProtein BiosynthesisAdrenoleukodystrophyATP-Binding Cassette Transporters5' Untranslated RegionsBiochimica et biophysica acta
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The sensor kinase DcuS of Escherichia coli: two stimulus input sites and a merged signal pathway in the DctA/DcuS sensor unit

2012

Abstract The membrane-integral sensor kinase DcuS of Escherichia coli consists of a periplasmically located sensory PASP domain, transmembrane helices TM1 and TM2, a cytoplasmic PASC domain and the kinase domain. Stimulus (C4-dicarboxylate) binding at PASP is required to stimulate phosphorylation of the kinase domain, resulting in phosphoryl transfer to the response regulator DcuR. PASC functions as a signaling device or a relay in signal transfer from TM2 to the kinase. Phosphorylated DcuR induces the expression of the target genes. Sensing by DcuS requires the presence of the C4-dicarboxylate transporter DctA during aerobic growth. DctA forms a sensor unit with DcuS, and a short C-termina…

Dicarboxylic Acid TransportersChemistryKinaseEscherichia coli ProteinsAntiporterClinical Biochemistrymedicine.disease_causeModels BiologicalBiochemistryCell biologyResponse regulatorTransmembrane domainBiochemistryProtein kinase domainPAS domainmedicinePhosphorylationProtein KinasesMolecular BiologyEscherichia coliSignal Transductionbchm
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Biowaiver Monographs for Immediate Release Solid Oral Dosage Forms: Metformin Hydrochloride.

2021

Abstract Data are examined regarding possible waiver of in vivo bioequivalence testing (i.e. biowaiver) for approval of metformin hydrochloride (metformin) immediate-release solid oral dosage forms. Data include metformin's Biopharmaceutics Classification System (BCS) properties, including potential excipient interactions. Metformin is a prototypical transporter-mediated drug and is highly soluble, but only 50% of an orally administered dose is absorbed from the gut. Therefore, metformin is a BCS Class III substance. A BCS-based approval approach for major changes to marketed products and new generics is admissible if test and reference dosage forms have the identical active pharmaceutical …

Drugendocrine system diseasesmedia_common.quotation_subjectPharmaceutical ScienceExcipientAdministration OralBiological Availabilitytransporters02 engineering and technologyPharmacologyBioequivalence030226 pharmacology & pharmacyDosage formPermeabilityBiopharmaceutics03 medical and health sciencesMetformin hydrochloride0302 clinical medicinePharmacokineticsmedicineBiopharmaceutics Classification System (BCS)media_commonActive ingredientDosage FormsbioequivalenceexcipientsChemistry021001 nanoscience & nanotechnologyBiopharmaceutics Classification SystembiowaiverMetforminMetforminSolubilityTherapeutic Equivalencyregulatory science0210 nano-technologypharmacokineticsmedicine.drugJournal of pharmaceutical sciences
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Intracellular retention of ABL kinase inhibitors determines commitment to apoptosis in CML cells

2012

PLoS one 7(7), e40853 (2012). doi:10.1371/journal.pone.0040853

Drugs and DevicesDrug Research and DevelopmentTime Factorsmedicine.drug_classChronic Myeloid LeukemiaIntracellular Spacelcsh:MedicineApoptosisPharmacologyPiperazinesTyrosine-kinase inhibitorHematologic Cancers and Related DisordersCell Line TumorLeukemia Myelogenous Chronic BCR-ABL Positivehemic and lymphatic diseasesLeukemiasmedicineHumansAnnexin A5Proto-Oncogene Proteins c-abllcsh:ScienceProtein Kinase InhibitorsMyeloproliferative DisordersMultidisciplinaryABLDose-Response Relationship DrugCaspase 3Chemistrylcsh:RBiological activityImatinibHematologyrespiratory tract diseasesDasatinibKineticsPyrimidinesImatinib mesylatePharmacodynamicsBenzamidesImatinib MesylateMedicineATP-Binding Cassette Transporterslcsh:QDrug Screening Assays AntitumorSignal transductionIntracellularResearch ArticleSignal Transductionmedicine.drug
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Expression of Active Streptolysin O in Escherichia coli as a Maltose-Binding-Protein-Streptolysin-O Fusion Protein. The N-Terminal 70 Amino Acids are…

1996

Streptolysin 0 (SLO) is the prototype of a family of cytolysins that consists of proteins which bind to cholesterol and form very large transmembrane pores. Structure/function studies on the pore-forming cytolysin SLO have been complicated by the proteolytic inactivation of a substantial portion of recombinant SLO (rSLO) expressed in Escherichia coli. To overcome this problem, translational fusions between the E. coli maltose-binding protein (MBP) gene and SLO were constructed, using the vectors pMAL-p2 and pMAL-c2. MBP-SLO fusion proteins were degraded if secreted into the E. coli periplasm, but intact, soluble MBP-SLO fusion proteins were produced at high levels in the cytoplasm. Active S…

ErythrocytesMonosaccharide Transport Proteinsgenetic structuresProtein ConformationStreptococcus pyogenesRecombinant Fusion ProteinsMolecular Sequence Datamedicine.disease_causeHemolysisBiochemistryMaltose-Binding ProteinsStructure-Activity RelationshipMaltose-binding proteinProtein structureBacterial ProteinsEscherichia colimedicineHumansCloning MolecularEscherichia coliSequence DeletionPore-forming toxinBase SequencebiologyEscherichia coli ProteinsFluoresceinsFusion proteineye diseasesTransmembrane proteinBiochemistryLiposomesStreptolysinsbiology.proteinATP-Binding Cassette TransportersStreptolysinsense organsCytolysinCarrier ProteinsSequence AnalysisEuropean Journal of Biochemistry
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