Search results for "recombinant"

showing 10 items of 1150 documents

Natural products as inhibitors of recombinant cathepsin L of Leishmania mexicana.

2015

Cysteine proteinases (cathepsins) from Leishmania spp. are promising molecular targets against leishmaniasis. Leishmania mexicana cathepsin L is essential in the parasite life cycle and a pivotal in virulence factor in mammals. Natural products that have been shown to display antileishmanial activity were screened as part of our ongoing efforts to design inhibitors against the L. mexicana cathepsin L-like rCPB2.8. Among them, agathisflavone (1), tetrahydrorobustaflavone (2), 3-oxo-urs-12-en-28-oic acid (3), and quercetin (4) showed significant inhibitory activity on rCPB2.8 with IC50 values ranging from 0.43 to 18.03 µM. The mechanisms of inhibition for compounds 1–3, which showed Ki values…

Cathepsin LImmunologyLeishmania mexicanaVirulence factorLeishmania mexicanaCathepsin BCathepsin LInhibitory Concentration 50Non-competitive inhibitionparasitic diseasesmedicineBiflavonoidsHumansCathepsinBiological ProductsbiologyGeneral Medicinebiology.organism_classificationLeishmaniaRecombinant ProteinsKineticsInfectious DiseasesMechanism of actionBiochemistrybiology.proteinParasitologyQuercetinmedicine.symptomUncompetitive inhibitorExperimental parasitology
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Expression of M-cadherin protein in myogenic cells during prenatal mouse development and differentiation of embryonic stem cells in culture.

1994

Molecules regulating morphogenesis by cell-cell interactions are the cadherins, a class of calcium-dependent adhesion molecules. One of its members, M-cadherin, has been isolated from a myoblast cell line (Donalies et al. [1991] Proc. Natl. Acad. Sci. U.S.A. 88:8024—8028). In mouse development, expression of M-cadherin mRNA first appears at day 8.5 of gestation (E8.5) in somites and has been postulated to be down-regulated in developing muscle masses (Moore and Walsh [1993] Development 117:1409—1420). Affinity-purified polyclonal M-cadherin antibodies, detecting a protein of approximately 120 kDa, were used to study the cell expression pattern of M-cadherin protein. It was first visualized …

Cell Adhesion Molecules NeuronalRecombinant Fusion ProteinsMolecular Sequence DataMorphogenesisFluorescent Antibody TechniqueGestational AgeBiologyEmbryonic and Fetal DevelopmentMiceLamininPregnancyMyocyteAnimalsAmino Acid SequenceRNA MessengerMuscle SkeletalCells CulturedDNA PrimersMice Inbred BALB CBase SequenceCadherinCell adhesion moleculeStem CellsCell MembraneGene Expression Regulation DevelopmentalCadherinsEmbryonic stem cellMolecular biologyCell culturebiology.proteinDesminFemaleDevelopmental BiologyDevelopmental dynamics : an official publication of the American Association of Anatomists
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Nuclear receptors modulate the interaction of Sp1 and GC-rich DNA via ternary complex formation

2000

Binding sites for transcription factor Sp1have been implicated in the transcriptional regulation of several genes by hormones or vitamins, and here we show that a GC-rich element contributes to the retinoic acid response of the interleukin 1β promoter. To explain such observations, it has been proposed that nuclear receptors can interact with Sp1 bound to GC-rich DNA. However, evidence supporting this model has remained indirect. So far, nuclear receptors have not been detected in a complex with Sp1 and GC-rich DNA, and the expected ternary complexes in non-denaturing gels were not seen. In search for these missing links we found that nuclear receptors [retinoic acid receptor (RAR), thyroid…

Cell ExtractsTranscriptional ActivationReceptors Retinoic AcidSp1 Transcription FactorRecombinant Fusion ProteinsReceptors Cytoplasmic and NuclearTretinoinRetinoic acid receptor betaBiologyRetinoid X receptorLigandsResponse ElementsTransfectionModels BiologicalBiochemistryAntibodiesCell LineSubstrate SpecificityAnimalsPromoter Regions GeneticMolecular BiologyNuclear receptor co-repressor 1Nuclear receptor co-repressor 2Binding SitesReceptors Thyroid HormoneDNACell BiologyRetinoic acid receptor gammaRetinoid X receptor gammaGC Rich SequenceProtein Structure TertiaryNuclear receptor coactivator 1Retinoic acid receptorDrosophila melanogasterEcdysteroneRetinoid X ReceptorsOligodeoxyribonucleotidesBiochemistryReceptors CalcitriolThermodynamicsResearch ArticleInterleukin-1Protein BindingTranscription FactorsBiochemical Journal
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Differential interaction of the two cholesterol-dependent, membrane-damaging toxins, streptolysin O and Vibrio cholerae cytolysin, with enantiomeric …

2003

AbstractMembrane cholesterol is essential to the activity of at least two structurally unrelated families of bacterial pore-forming toxins, represented by streptolysin O (SLO) and Vibrio cholerae cytolysin (VCC), respectively. Here, we report that SLO and VCC differ sharply in their interaction with liposome membranes containing enantiomeric cholesterol (ent-cholesterol). VCC had very low activity with ent-cholesterol, which is in line with a stereospecific mode of interaction of this toxin with cholesterol. In contrast, SLO was only slightly less active with ent-cholesterol than with cholesterol, suggesting a rather limited degree of structural specificity in the toxin–cholesterol interact…

Cell Membrane Permeabilitygenetic structuresBiophysicsBiologymedicine.disease_causeBiochemistrySubstrate Specificity03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsStructural Biologyotorhinolaryngologic diseasesGeneticsmedicineStreptolysin OMolecular BiologyVibrio cholerae030304 developmental biology0303 health sciencesLiposomeVibrio cholerae cytolysinCholesterolToxinCytotoxinsEnantiomeric cholesterol030302 biochemistry & molecular biologyMembranes ArtificialStereoisomerismCell BiologyFluoresceinseye diseasesRecombinant ProteinsCholesterol-binding cytolysinsMembraneCholesterolchemistryBiochemistryVibrio choleraeLiposomesStreptolysinsProtein–cholesterol interactionlipids (amino acids peptides and proteins)Streptolysinsense organsCytolysinEnantiomerProtein BindingFEBS letters
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Soluble N-ethylmaleimide-sensitive-factor attachment protein and N-ethylmaleimide-insensitive factors are required for Ca2+-stimulated exocytosis of …

1996

Ca2+ stimulates exocytosis in permeabilized insulin-secreting cells. To investigate the putative cytosolic components involved in the Ca2+ response, HIT-T15 cells (a pancreatic B-cell line) were permeabilized with streptolysin-O, a procedure that allows rapid exchange of soluble components including macromolecules. We found that in this cell preparation the secretory response to Ca2+ but not to guanosine 5'-[gamma-thio]triphosphate was lost as a function of time and could be restored by rat brain cytosol in a concentration-dependent manner. Reconstitutive activity of rat brain cytosol was found in a high-molecular-mass heat-labile partially N-ethylmaleimide(NEM)-sensitive fraction. The NEM-…

Cell Membrane Permeabilitymedicine.medical_treatmentBlotting WesternVesicular Transport ProteinsGuanosineBiologyBiochemistryExocytosisExocytosislaw.inventionCell Linechemistry.chemical_compoundIslets of LangerhansCytosolBacterial ProteinslawInsulin SecretionmedicineAnimalsInsulinheterocyclic compoundsAttachment proteinMolecular BiologyN-Ethylmaleimide-Sensitive ProteinsBrain ChemistryInsulinN-EthylmaleimideMembrane ProteinsCell BiologyRecombinant ProteinsCell biologyRatsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsCytosolchemistryEthylmaleimideGuanosine 5'-O-(3-Thiotriphosphate)StreptolysinsRecombinant DNACalciumSoluble NSF attachment proteinCarrier ProteinsResearch ArticleThe Biochemical journal
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A GFP-tagged Muscleblind C protein isoform reporter construct

2010

Drosophila muscleblind (mbl), the ortholog of human Muscleblind-like 1 (MBNL1) gene involved in Myotonic Dystrophy (DM), gives raise to protein isoforms MblA to G. The specific functions and subcellular distribution of isoforms are still largely unknown. To overcome the lack of isoform-specific antibodies we generated transgenic flies that express a GFP:MblC fusion protein under the control of the Gal4/UAS system. The reporter fusion protein was able to functionally complement mbl loss of function mutations, demonstrating activity, and accumulated predominantly in adult muscle nuclei. The fluorescent nature of the reporter makes it appropriate for live imaging detection of MblC protein isof…

Cell NucleusProtein isoformGene isoformMusclesRecombinant Fusion ProteinsTransgeneGreen Fluorescent ProteinsNuclear ProteinsBiologyMolecular biologyFusion proteinGreen fluorescent proteinAnimals Genetically Modifiedchemistry.chemical_compoundchemistryGenes ReporterLive cell imagingInsect ScienceAnimalsDrosophila ProteinsMBNL1DrosophilaGenetic EngineeringGeneFly
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PECAM-1 expression in human mesothelial cells: an in vitro study.

1996

Mesothelial cells are actively involved in inflammatory processes by expressing a set of cell adhesion molecules (CAMs). Transmigration of leukocytes into inflamed tissues requires a chemotactic stimulus and engagement of platelet-endothelial cell adhesion molecule-1 (PECAM-1). To investigate the kinetics involved in peritonitis, pure cultures of mesothelial cells are necessary. In previous studies, we have found that human mesothelial cells (HOMES) show a weak constitutive expression of PECAM-1, which cannot be further stimulated by cytokines. It is known that all serous cavities and body fluids contain numerous macrophages which strongly express this adhesion molecule. To identify the cel…

Cell SeparationIn Vitro TechniquesEpitheliumPathology and Forensic MedicineInterferon-gammaE-selectinmedicineHumansCell adhesionMolecular BiologyCells CulturedbiologyChemistryCell adhesion moleculeTumor Necrosis Factor-alphaMonocyteEpithelial CellsCell BiologyGeneral MedicineCell sortingMolecular biologyImmunohistochemistryRecombinant ProteinsCell biologyPlatelet Endothelial Cell Adhesion Molecule-1Microscopy Electronmedicine.anatomical_structureCell culturebiology.proteinNeural cell adhesion moleculeOmentumMesothelial CellInterleukin-1Pathobiology : journal of immunopathology, molecular and cellular biology
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Heterodimer formation of wild-type and amyotrophic lateral sclerosis-causing mutant Cu/Zn-superoxide dismutase induces toxicity independent of protei…

2008

Recent studies provide evidence that wild-type Cu/Zn-superoxide dismutase (SOD1(hWT)) might be an important factor in mutant SOD1-mediated amyotrophic lateral sclerosis (ALS). In order to investigate its functional role in the pathogenesis of ALS, we designed fusion proteins of two SOD1 monomers linked by a polypeptide. We demonstrated that wild-type-like mutants, but not SOD1(G85R) homodimers, as well as mutant heterodimers including SOD1(G85R)-SOD1(hWT) display dismutase activity. Mutant homodimers showed an increased aggregation compared with the corresponding heterodimers in cell cultures and transgenic Caenorhabditis elegans, although SOD1(G85R) heterodimers are more toxic in functiona…

Cell SurvivalRecombinant Fusion Proteinsanimal diseasesSOD1MutantProtein aggregationAnimals Genetically ModifiedProtein CarbonylationSuperoxide dismutaseMicechemistry.chemical_compoundSuperoxide Dismutase-1Cell Line TumorGeneticsAnimalsHumansAmino Acid SequenceCaenorhabditis elegansMolecular BiologyGenetics (clinical)Motor NeuronsbiologySuperoxide DismutaseSuperoxideAmyotrophic Lateral SclerosisWild typenutritional and metabolic diseasesHydrogen PeroxideGeneral MedicineFusion proteinProtein Structure Tertiarynervous system diseasesCell biologyAmino Acid Substitutionnervous systemchemistryBiochemistrybiology.proteinDismutaseDimerizationHuman Molecular Genetics
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Molecular evolution of the metazoan extracellular matrix: cloning and expression of structural proteins from the demosponges Suberites domuncula and …

2000

One crucial event during evolution to multicellularity was the development of either direct cell–cell contact or indirect interaction via extracellular matrix (ECM) molecules. The identification of those polypeptides provides conclusive data on the phylogenetic relationship of metazoan phyla and helps us to understand the position of the Metazoa among the other kingdoms. Recently it became evident that the ECM of sponges is amazingly complex; it is composed of fibrous molecules, e.g., collagen, and their corresponding receptors, which are highly similar to those existing in other metazoan phyla. While these data already support the view of monophyly of Metazoa, additional studies are requir…

Cell signalingDNA ComplementaryDermatopontinMolecular Sequence DataGene ExpressionBiologyBioinformaticsTransplantation AutologousExtracellular matrixEvolution MolecularMyotrophinGeneticsAnimalsAmino Acid SequenceCloning MoleculareducationGrowth SubstancesMolecular BiologyPeptide sequenceEcology Evolution Behavior and SystematicsPhylogenyCell Aggregationeducation.field_of_studyExtracellular Matrix ProteinsBase SequenceSequence Homology Amino AcidReceptor Protein-Tyrosine Kinasesbiology.organism_classificationRecombinant ProteinsCell biologyPoriferaSuberites domunculaTransplantationChondroitin Sulfate ProteoglycansIntercellular Signaling Peptides and ProteinsCollagenCarrier ProteinsCell Adhesion MoleculesFunction (biology)Journal of molecular evolution
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α-Secretase Activity of the Disintegrin Metalloprotease ADAM 10: Influences of Domain Structure

2001

Disintegrin metalloproteases from different organisms form the ADAM (a disintegrin and metalloprotease) family. All members display a common domain organization and possess four potential functions: proteolysis, cell adhesion, cell fusion, and cell signaling. Members of the ADAM family are responsible for the proteolytic cleavage of transmembrane proteins and release of their extracellular domain. The proteolytic process is referred to as ectodomain shedding, which is activated by phorbol esters and inhibited by hydroxamic acid-based inhibitors. We have shown that the disintegrin metalloprotease ADAM 10 has both constitutive and regulated alpha-secretase activity. Expression of a dominant n…

Cell signalingDisintegrinsMolecular Sequence DataProtein domainBiologyGeneral Biochemistry Genetics and Molecular BiologyADAM10 ProteinAmyloid beta-Protein PrecursorHistory and Philosophy of ScienceEndopeptidasesDisintegrinAnimalsAspartic Acid EndopeptidasesHumansProtease InhibitorsAmino Acid SequenceCell adhesionMetalloproteinaseGeneral NeuroscienceHEK 293 cellsMembrane ProteinsMetalloendopeptidasesRecombinant ProteinsTransmembrane proteincarbohydrates (lipids)ADAM ProteinsBiochemistryEctodomainbiology.proteinAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalAnnals of the New York Academy of Sciences
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