Search results for "plasma protein"

showing 10 items of 193 documents

TIMP-3 facilitates binding of target metalloproteinases to the endocytic receptor LRP-1 and promotes scavenging of MMP-1.

2020

AbstractMatrix metalloproteinases (MMPs) and the related families of disintegrin metalloproteinases (ADAMs) and ADAMs with thrombospondin repeats (ADAMTSs) play a crucial role in extracellular matrix (ECM) turnover and shedding of cell-surface molecules. The proteolytic activity of metalloproteinases is post-translationally regulated by their endogenous inhibitors, known as tissue inhibitors of metalloproteinases (TIMPs). Several MMPs, ADAMTSs and TIMPs have been reported to be endocytosed by the low-density lipoprotein receptor-related protein-1 (LRP-1). Different binding affinities of these proteins for the endocytic receptor correlate with different turnover rates which, together with di…

Cell biologyTIMP-3 LRP-1 MMP-1 extracellular matrix endocytosis metalloproteinases endocytic receptorlcsh:MedicinePlasma protein bindingMatrix metalloproteinaseBiochemistryArticleExtracellular matrixDisintegrinHumanslcsh:ScienceReceptorTissue Inhibitor of Metalloproteinase-3MetalloproteinaseThrombospondinMultidisciplinarybiologyChemistrylcsh:RLigand (biochemistry)EndocytosisMatrix MetalloproteinasesCell biologyKineticsMultiprotein Complexesbiology.proteinlcsh:Qlipids (amino acids peptides and proteins)Matrix Metalloproteinase 1Low Density Lipoprotein Receptor-Related Protein-1Protein BindingScientific reports
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Down-regulation of nuclear binding activities of OXBOX-REBOX transcription factors during cellular senescence.

1996

Functional capacity of mitochondria declines during aging and this impairment may have a major role in aging process. Several observations indicate that transcriptional efficiency is reduced during aging. Our purpose was to find out whether aging and cellular senescence affect the nuclear binding activities of transcription factors which bind to OXBOX-REBOX sequence present in promoter regions of numerous nuclear genes encoding mitochondrial proteins. These factors regulate and coordinate the expression of mitochondrial proteins. We observed a strong down-regulation in the nuclear binding activities of OXBOX-REBOX factors in replicatively senesced human WI-38 and IMR-90 fibroblasts. On the …

Cell cycle checkpointNuclear genePhotoagingMolecular Sequence DataBiophysicsDown-RegulationPlasma protein bindingBiologyMitochondrionBiochemistryDownregulation and upregulationmedicineAnimalsHumansRats WistarMolecular BiologyTranscription factorCellular SenescenceCell Line TransformedBase SequenceNuclear ProteinsCell BiologyDNAmedicine.diseaseCell biologyRatsCell cultureProtein BindingTranscription FactorsBiochemical and biophysical research communications
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Computational identification of cell-specific variable regions in ChIP-seq data.

2019

ABSTRACT Chromatin immunoprecipitation followed by sequencing (ChIP-seq) is used to identify genome-wide DNA regions bound by proteins. Several sources of variation can affect the reproducibility of a particular ChIP-seq assay, which can lead to a misinterpretation of where the protein under investigation binds to the genome in a particular cell type. Given one ChIP-seq experiment with replicates, binding sites not observed in all the replicates will usually be interpreted as noise and discarded. However, the recent discovery of high-occupancy target (HOT) regions suggests that there are regions where binding of multiple transcription factors can be identified. To investigate these regions,…

Cell typeAcademicSubjects/SCI00010Computational biologyPlasma protein bindingBiologyGenomeCell LineEvolution Molecular03 medical and health scienceschemistry.chemical_compoundMice0302 clinical medicineNarese/3Cell Line TumorGeneticsAnimalsHumansEpigeneticsBinding sitePromoter Regions GeneticTranscription factorEmbryonic Stem Cells030304 developmental biology0303 health sciencesPrincipal Component AnalysisBinding SitesNucleotidesGenetic VariationPromoterGenomicsChromatinchemistryCpG siteMCF-7 CellsChromatin Immunoprecipitation SequencingMethods OnlineR-Loop StructuresK562 CellsChromatin immunoprecipitation030217 neurology & neurosurgeryFunction (biology)DNATranscription FactorsNucleic acids research
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Transport of resveratrol, a cancer chemopreventive agent, to cellular targets: plasmatic protein binding and cell uptake

2004

Resveratrol produced by several plants, berries and fruits, including grapes, is one of the best known natural food microcomponents with potent chemopreventive properties towards the most severe contemporary human diseases: cardiovascular sickness, cancer and neurodegenerative pathologies. Demonstration of its mechanism of action also implies the elucidation of the steps of bioavailability and bioabsorption in cells and tissues. In order to estimate the relationships between the amounts of resveratrol taken up by food or drink intake, and the several possible benefits illustrated from in vitro/in vivo experiments and from epidemiological studies, it is essential to demonstrate step by step …

CellPlasma protein bindingPharmacologyResveratrolBiologyBiochemistrychemistry.chemical_compoundIn vivoStilbenesTumor Cells CulturedmedicineAnimalsAnticarcinogenic AgentsHumansAnticarcinogenSerum AlbuminPharmacologyFatty Acidsfood and beveragesBiological TransportBlood ProteinsIn vitromedicine.anatomical_structureBiochemistryMechanism of actionchemistryResveratrolmedicine.symptomIntracellularProtein BindingBiochemical Pharmacology
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Albumin binding and hydrophobic character of promazine and chlorpromazine metabolites.

1972

1. The binding of didesmethylpromazine, promazine N-oxide, 2-hydroxypromazine, promazine sulfoxide, monodesmethylpromazine sulfoxide, didesmethylchlorpromazine, chlorpromazine N-oxide, and chlorpromazine sulfoxide to bovine serum albumin was determined by means of sephadex gel filtration. 2. The albumin binding of these substances was characterized by the following parameters: the percentage α of free substance, the percentage β of bound substance, the binding constants K1, k+ and m, the number of binding sites per albumin molecule, and the free binding energy ΔFo. 3. The partition coefficients between n-octanol and buffer solution, pH 7.40, were measured for the above mentioned metabolites…

Chemical PhenomenaChlorpromazineStatistics as TopicPlasma protein bindingchemistry.chemical_compoundmedicineAnimalsBovine serum albuminChlorpromazinePromazinePromazinePharmacologyChromatographyBinding SitesbiologyAlbuminSulfoxideSerum Albumin BovineGeneral MedicineBuffer solutionChemistrychemistrySolubilitySephadexSulfoxidesbiology.proteinChromatography GelCattleNitrogen OxidesChlorinemedicine.drugProtein BindingNaunyn-Schmiedeberg's archives of pharmacology
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Zur Plasmaproteinbindung von Arzneimitteln

1969

1. Auf Dialyse, Ultrazentrifugation und Sephadexgelfiltration als die gebrauchlichsten Methoden zur quantitativen Bestimmung der Eiweisbindung von Pharmaka wird hingewiesen. 2. Die Wechselwirkung von niedermolekularen Substanzen mit Proteinen folgt dem Massenwirkungsgesetz. Darauf beruht die Formulierung der Ergebnisse von Eiweisbindungsversuchen. Die Darstellung der Ergebnisse nach Scatchard (1949) wird als die wichtigste Methode angesehen. Daneben sind Darstellungsmethoden nach Scholtan (1962) und Kruger-Thiemer (1961) gebrauchlich, die fur bestimmte Fragestellungen Vorteile bieten. 3. Die Bindung von Pharmaka an Plasmaproteine scheint vorwiegend hydrophoben Charakter zu besitzen. Dabei s…

ChemistryDrug DiscoveryMolecular MedicineGeneral MedicinePlasma protein bindingMolecular biologyGenetics (clinical)Klinische Wochenschrift
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Photobinding of Tiaprofenic Acid and Subprofen to Proteins and Cells: A Combined Study Using Radiolabeling, Antibodies and Laser Flash Photolysis of …

1998

Drug photoallergy is a matter of current concern. It involves the formation of drug-protein photoadducts (photoantigens) that may ultimately trigger an immunological response. Tyrosine residues appear to be key binding sites in proteins. The present work has investigated the photobinding of tiaprofenic and (TPA) and the closely related isomer suprofen (SUP) to proteins and cells by means of radioactive labeling and drug-directed antibodies. To ascertain whether preassociation with the protein may play a role in photoreactivity, two model bichromophoric compounds (TPA-Tyr and SUP-Tyr) have been prepared and studied by laser flash photolysis. The results of this work show that (a) TPA and SUP…

ChemistryStereochemistrySuprofenGeneral MedicinePlasma protein bindingPhotochemistryBiochemistryCell membranemedicine.anatomical_structureLabellingmedicineFlash photolysisPhysical and Theoretical ChemistryBinding siteTyrosineTiaprofenic acidmedicine.drug
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Evaluation of enantioselective binding of antihistamines to human serum albumin by ACE.

2007

The drug binding to plasma and tissue proteins is a fundamental factor in determining the overall pharmacological activity of a drug. HSA, together with alpha(1)-acid glycoprotein, are the most important plasma proteins, which act as drug carriers, with implications on the pharmacokinetic of drugs. Among plasma proteins, HSA possesses the highest enantioselectivity. In this paper, a new methodology for the study of enantiodifferentiation of chiral drugs with HSA is developed and applied to evaluate the possible enantioselective binding of four antihistamines: brompheniramine, chlorpheniramine, hydroxyzine and orphenadrine to HSA. This study includes the determination of affinity constants o…

ChlorpheniramineClinical BiochemistryPlasma protein bindingPharmacologyBiochemistryAnalytical ChemistryPharmacokineticsOrphenadrinemedicineOrphenadrineHumansSerum AlbuminDrug CarriersChromatographyBinding SitesChemistryBiological activityStereoisomerismBrompheniramineHuman serum albuminBrompheniraminebody regionsHydroxyzineembryonic structuresHistamine H1 AntagonistsEnantiomerDrug carriermedicine.drugProtein BindingElectrophoresis
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Characterization of antihistamine–human serum protein interactions by capillary electrophoresis

2007

An important topic in the drug discovery and development process is the role of drug binding to plasma proteins. In this paper the characterization of the interaction between antihistamines (cationic drugs) towards human serum albumin (HSA) and alpha(1)-acid glycoprotein (AGP) under physiological conditions by capillary electrophoresis-frontal analysis is presented. Furthermore, the binding of these drugs to all plasma proteins is evaluated by using ultrafiltration and capillary electrophoresis. Antihistamines present a wide-ranging behaviour with respect to their affinities towards plasma proteins. Orphenadrine, phenindamine, tripelenamine and tripolidine principally bind to HSA; carbinoxa…

ChromatographyPhenindamineChemistryOrganic ChemistryElectrophoresis CapillaryBlood ProteinsGeneral MedicinePlasma protein bindingBrompheniramineHuman serum albuminBiochemistryBlood proteinsAnalytical Chemistrychemistry.chemical_compoundChlorcyclizineBiochemistryDimetindeneHistamine H1 AntagonistsmedicineHumansCarbinoxamineProtein Bindingmedicine.drugJournal of Chromatography A
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Role of Seroalbumin in the Cytotoxicity of cis-Dichloro Pt(II) Complexes with (N^N)-Donor Ligands Bearing Functionalized Tails

2018

Given the potent anticancer properties of cisdiamminedichloroplatinum( II) and knowing its mode of action, we synthesized four new cis-[PtCl2(N^N)] organoplatinum complexes, two with N-substituted pbi ligands (pbiR = 1-R-2-(2-pyridyl)benzimidazole) (namely, 1 and 2) and two more with 4,4′-disubstituted bpy ligands (bpy = 2,2′-bipyridine) (namely, 3 and 4). We explored their cytotoxicity and ability to bind to deoxyguanosine monophosphate (dGMP), DNA, and albumin models. By 1H NMR and UV−vis spectroscopies, circular dichroism, agarose gel electrophoresis, differential scanning calorimetry measurements, and density functional theory calculations, we verified that only 3 can form aquacomplex s…

Circular dichroismCell SurvivalStereochemistryLigandPlasma protein bindingHeLa CellLigands010402 general chemistry01 natural sciencesChemistry Physical and theoreticalInorganic ChemistryHeLaBipyridinechemistry.chemical_compoundDrug StabilityCoordination ComplexesQuímica físicaHumansPhysical and Theoretical ChemistryCytotoxicityA549 CellOrganoplatinumPlatinumCoordination ComplexeCalorimetry Differential ScanningMolecular Structurebiology010405 organic chemistryChemistryRational designDeoxyguanine NucleotidesSerum Albumin BovineDNAbiology.organism_classification0104 chemical sciencesSettore CHIM/03 - Chimica Generale E InorganicaA549 CellsAgarose gel electrophoresisDeoxyguanine NucleotideHumanHeLa CellsProtein BindingInorganic Chemistry
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