Search results for "binding site"

showing 10 items of 856 documents

Demonstration of High-Affinity Binding Sites for C3a Anaphylatoxin on Guinea-Pig Platelets

1978

3H-serotonin release from guinea-pig platelets was demonstrated to be the consequence of C3a binding to these cells. A Scatchard analysis of dose-response data of the 125I-C3a binding pattern to guinea-pig platelets pointed to the existence of binding sites with high and low affinity for the C3a molecule (HA and LA receptors). HA receptors are specific for C3a with intact C-terminal arginine. whereas C3adesarg only interacts with LA receptors. The release of serotonin may be induced by a combined reaction of C3a with HA receptors and LA receptors on the platelet membrane.

Blood PlateletsAnaphylatoxinsSerotoninBinding SitesArginineChemistryGuinea PigsImmunologyTemperaturechemical and pharmacologic phenomenaCarboxypeptidasesComplement C3General MedicineGuinea pigBiochemistryAnimalsProtease-activated receptorPlateletAnaphylatoxinSerotoninBinding sitePeptidesReceptorScandinavian Journal of Immunology
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Novel α2β1 integrin inhibitors reveal that integrin binding to collagen under shear stress conditions does not require receptor preactivation.

2012

The interaction between α2β1 integrin (GPIa/IIa, VLA-2) and vascular collagen is one of the initiating events in thrombus formation. Here, we describe two structurally similar sulfonamide derivatives, BTT-3033 and BTT-3034, and show that, under static conditions, they have an almost identical effect on α2-expressing CHO cell adhesion to collagen I, but only BTT-3033 blocks platelet attachment under flow (90 dynes/cm(2)). Differential scanning fluorimetry showed that both molecules bind to the α2I domain of the recombinant α2 subunit. To further study integrin binding mechanism(s) of the two sulfonamides, we created an α2 Y285F mutant containing a substitution near the metal ion-dependent ad…

Blood PlateletsIntegrinPlatelet Membrane GlycoproteinsBiochemistryCD49cCollagen Type ICollagen receptorCell LineMiceCell AdhesionAnimalsHumansBinding siteReceptorMolecular BiologyIntegrin bindingSulfonamidesbiologyMolecular StructureChemistryta1182Cell BiologyMice Inbred C57BLBiochemistryIntegrin alpha Mbiology.proteinBiophysicsIntegrin beta 6Stress MechanicalIntegrin alpha2beta1Protein BindingThe Journal of biological chemistry
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Resolving Binding Events on the Multifunctional Human Serum Albumin

2020

Abstract Physiological processes rely on initial recognition events between cellular components and other molecules or modalities. Biomolecules can have multiple sites or mode of interaction with other molecular entities, so that a resolution of the individual binding events in terms of spatial localization as well as association and dissociation kinetics is required for a meaningful description. Here we describe a trichromatic fluorescent binding‐ and displacement assay for simultaneous monitoring of three individual binding sites in the important transporter and binding protein human serum albumin. Independent investigations of binding events by X‐ray crystallography and time‐resolved dyn…

Boron Compounds540 Chemistry and allied sciencesalbumin bindingIbuprofenSerum Albumin HumanMolecular Dynamics SimulationCrystallography X-Ray01 natural sciencesBiochemistryFluorescenceDrug DiscoverymedicineHumansSpatial localizationmulticolor assayskinetics investigationsGeneral Pharmacology Toxicology and PharmaceuticsBinding sitePharmacologychemistry.chemical_classificationBinding SitesMolecular Structure010405 organic chemistryBinding proteinBiomoleculeCommunicationOrganic ChemistryLauric AcidsTransporterdrug interactionsHuman serum albuminFluorescenceCommunications0104 chemical sciences010404 medicinal & biomolecular chemistry4-Chloro-7-nitrobenzofurazanchemistry540 ChemieBiophysicsMolecular MedicineDissociation kineticsswitchSENSE technologyWarfarinmedicine.drugChemmedchem
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Shared Binding Sites for the Bacillus thuringiensis Proteins Cry3Bb, Cry3Ca, and Cry7Aa in the African Sweet Potato Pest Cylas puncticollis (Brentida…

2014

ABSTRACT Bacillus thuringiensis Cry3Bb, Cry3Ca, and Cry7Aa have been reported to be toxic against larvae of the genus Cylas , which are important pests of sweet potato worldwide and particularly in sub-Saharan Africa. However, relatively little is known about the processing and binding interactions of these coleopteran-specific Cry proteins. The aim of the present study was to determine whether Cry3Bb, Cry3Ca, and Cry7Aa proteins have shared binding sites in Cylas puncticollis to orient the pest resistance strategy by genetic transformation. Interestingly, processing of the 129-kDa Cry7Aa protoxin using commercial trypsin or chymotrypsin rendered two fragments of about 70 kDa and 65 kDa. N-…

Brush borderBacillus thuringiensisBiological pest controlHemolysin ProteinsApplied Microbiology and BiotechnologyMicrobiologyHemolysin ProteinsBacterial ProteinsBacillus thuringiensisEnvironmental MicrobiologymedicineAnimalsIpomoea batatasBinding sitePlant DiseasesBinding SitesChymotrypsinBacillus thuringiensis ToxinsEcologybiologyfungiTrypsinbiology.organism_classificationColeopteraEndotoxinsLarvabiology.proteinPEST analysisFood ScienceBiotechnologymedicine.drugApplied and Environmental Microbiology
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Lyophilization of lepidopteran midguts: a preserving method for Bacillus thuringiensis toxin binding studies

2004

Binding assays with brush border membrane vesicles (BBMV) from insect midguts are commonly used in the study of the interactions between Bacillus thuringiensis Cry toxins and their receptors. Collaboration between laboratories often require that frozen insect samples are sent in dry ice. Because of customs restrictions and delays, sample thawing is always a risk and often the biological material becomes ruined during shipping. We have tested lyophilization as an alternative method for preserving insect midguts for binding studies with B. thuringiensis Cry toxins. For this purpose, BBMV were prepared from both frozen and lyophilized midguts from three lepidopteran species: Spodoptera exigua,…

Brush borderBacillus thuringiensisReceptors Cell SurfaceHelicoverpa armigeraSpodopteramedicine.disease_causeHost-Parasite InteractionsMicrobiologyBacterial ProteinsBacillus thuringiensisExiguamedicineAnimalsBinding sitePest Control BiologicalEcology Evolution Behavior and SystematicsCryopreservationMicrovillibiologyToxinfungibiology.organism_classificationLepidopteraFreeze DryingBiochemistryManduca sextaInsect ProteinsDigestive SystemJournal of Invertebrate Pathology
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Binding of Bacillus thuringiensis toxins in resistant and susceptible strains of pink bollworm (Pectinophora gossypiella)

2003

Abstract Evolution of resistance by pests could cut short the success of transgenic plants producing toxins from Bacillus thuringiensis, such as Bt cotton. The most common mechanism of insect resistance to B. thuringiensis is reduced binding of toxins to target sites in the brush border membrane of the larval midgut. We compared toxin binding in resistant and susceptible strains of Pectinophora gossypiella, a major pest of cotton worldwide. Using Cry1Ab and Cry1Ac labeled with 125I and brush border membrane vesicles (BBMV), competition experiments were performed with unlabeled Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca, Cry1Ja, Cry2Aa, and Cry9Ca. In the susceptible strain, Cry1Aa, Cry1Ab, Cry1…

Brush borderBacterial ToxinsBacillus thuringiensisGenetically modified cropsBinding CompetitiveBiochemistryMicrobiologyIodine RadioisotopesRadioligand AssayBacillus thuringiensisBotanyAnimalsPest Control BiologicalMolecular BiologyBinding SitesMicrovillibiologyHeliothis virescensCytoplasmic Vesiclesfungifood and beveragesPlutellabiology.organism_classificationRecombinant ProteinsLepidopteraKineticsBt cottonCry1AcLarvaInsect ScienceProtein BindingPink bollwormInsect Biochemistry and Molecular Biology
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Bacillus thuringiensis crystal proteins CRY1Ab and CRY1Fa share a high affinity binding site in Plutella xylostella (L.).

1996

The future success of Bacillus thuringiensis based insecticides depends in part on our ability to prevent insects from developing resistance against their insecticidal crystal proteins. Two recent papers indicated cross-resistance between Cry1A proteins and Cry1Fa in two different insect species (Tabashnik et al., 1994, Appl. Environ. Microbiol. 60, 4627-4629; Gould et al., 1995, J. Econ. Entomol. 88, 1545-1559). Brush border membrane vesicles were prepared from Plutella xylostella and used in binding assays with 125I-labeled trypsin-activated crystal proteins. Competition experiments showed that Cry1Fa competed with Cry1Ab for a same binding site, though the latter still bound to a differe…

Brush borderBacterial ToxinsBiophysicsBacillus thuringiensisMothsHemolysin ProteinsBiochemistryCell membraneIodine RadioisotopesHemolysin ProteinsBacterial ProteinsBacillus thuringiensismedicineAnimalsBinding siteReceptorPest Control BiologicalMolecular BiologyBinding SitesbiologyBacillus thuringiensis ToxinsVesiclefungiCell MembranePlutellaCell Biologybiology.organism_classificationMolecular biologyEndotoxinsmedicine.anatomical_structureBiochemistryBiochemical and biophysical research communications
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Development and Characterization of Diamondback Moth Resistance to Transgenic Broccoli Expressing High Levels of Cry1C

2000

ABSTRACT A field-collected colony of the diamondback moth, Plutella xylostella , had 31-fold resistance to Cry1C protoxin of Bacillus thuringiensis . After 24 generations of selection with Cry1C protoxin and transgenic broccoli expressing a Cry1C protein, the resistance that developed was high enough that neonates of the resistant strain could complete their entire life cycle on transgenic broccoli expressing high levels of Cry1C. After 26 generations of selection, the resistance ratios of this strain to Cry1C protoxin were 12,400- and 63,100-fold, respectively, for the neonates and second instars by a leaf dip assay. The resistance remained stable until generation 38 (G38) under continuous…

Brush borderBacterial ToxinsBrassicaGenetically modified cropsBrassicaMothsApplied Microbiology and BiotechnologyInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsBinding sitePest Control BiologicalDiamondback mothEcologybiologyStrain (chemistry)Bacillus thuringiensis ToxinsMicrovilliParasporal bodyfungibiology.organism_classificationPlants Genetically ModifiedMolecular biologyEndotoxinsFood ScienceBiotechnology
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In Vivo and In Vitro Binding of Vip3Aa to Spodoptera frugiperda Midgut and Characterization of Binding Sites by 125 I Radiolabeling

2014

ABSTRACT Bacillus thuringiensis vegetative insecticidal proteins (Vip3A) have been recently introduced in important crops as a strategy to delay the emerging resistance to the existing Cry toxins. The mode of action of Vip3A proteins has been studied in Spodoptera frugiperda with the aim of characterizing their binding to the insect midgut. Immunofluorescence histological localization of Vip3Aa in the midgut of intoxicated larvae showed that Vip3Aa bound to the brush border membrane along the entire apical surface. The presence of fluorescence in the cytoplasm of epithelial cells seems to suggest internalization of Vip3Aa or a fragment of it. Successful radiolabeling and optimization of the…

Brush bordermedia_common.quotation_subjectSpodopteraSpodopteraHemolysin ProteinsBinding CompetitiveApplied Microbiology and BiotechnologyIodine RadioisotopesHemolysin ProteinsBacterial ProteinsBacillus thuringiensisInvertebrate MicrobiologyAnimalsTrypsinBinding siteInternalizationmedia_commonBinding SitesBacillus thuringiensis ToxinsMicrovilliEcologybiologyfungiEpithelial CellsMidgutHydrogen-Ion Concentrationbiology.organism_classificationEndotoxinsBiochemistryCytoplasmIsotope LabelingLarvaDigestive SystemFood ScienceBiotechnologyApplied and Environmental Microbiology
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CTCF and BORIS Regulate Rb2/p130 Gene Transcription: A Novel Mechanism and a New Paradigm for Understanding the Biology of Lung Cancer

2011

Abstract Although innumerable investigations regarding the biology of lung cancer have been carried out, many aspects thereof remain to be addressed, including the role played by the retinoblastoma-related protein Rb2/p130 during the evolution of this disease. Here we report novel findings on the mechanisms that control Rb2/p130 gene expression in lung fibroblasts and characterize the effects of Rb2/p130 deregulation on the proliferative features of lung cancer cells. We revealed for the first time that in lung fibroblasts the expression of Rb2/p130 gene is directly controlled by the chromatin insulator CCCTC-binding factor, CTCF, which by binding to the Rb2/p130 gene promoter induces, and/…

CCCTC-Binding FactorChromatin ImmunoprecipitationCancer ResearchLung NeoplasmsTranscription GeneticSettore MED/06 - Oncologia MedicaBiologyInsulator (genetics)Open Reading FramesTranscription (biology)Carcinoma Non-Small-Cell LungCell Line TumorGene expressionmedicineHumansCarcinoma Small CellPromoter Regions GeneticLung cancerChromosome PositioningMolecular BiologyGeneBinding SitesRetinoblastoma-Like Protein p130PromoterFibroblastsmedicine.diseaseChromatinDNA-Binding ProteinsGene Expression Regulation NeoplasticRepressor ProteinsGene transcriptionOncologyCTCFembryonic structuresCancer researchLung cancerLung cancer; Gene transcriptionbiological phenomena cell phenomena and immunityProtein BindingMolecular Cancer Research
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