Search results for "binding"

showing 10 items of 3896 documents

Preliminary approach to elucidate the role of pigment as a binding site for drugs and chemicals in anagen hair: differential uptake of 3 H-haloperido…

2002

A striking difference was observed for cellular-bound drug in HaCaT and Sk-Mel-1 cells for a fixed drug exposure time of 72 h and varying 3H-haloperidol concentrations in the culture media. Drug uptake was dependent on drug concentration and linearly correlated for both the non-pigment- and the pigment-producing cells which however was different in magnitude. In an additional investigation the time course of drug uptake during 3H-haloperidol exposure (400 pmol/ml; 28 days) revealed increasing drug concentrations in the Sk-Mel-1 population, whereas drug concentrations in the keratinocytes reached a plateau within a short time period. In contrast to the HaCaT cells no tendency to saturation w…

KeratinocytesDrugmedia_common.quotation_subjectPopulationBiologyPharmacologyCell LinePathology and Forensic MedicineMelaninPigmentHaloperidolmedicineHumansTissue DistributionBinding siteeducationmedia_commonMelaninseducation.field_of_studyBinding SitesMelanosomesPigmentationHaCaTCell culturevisual_artvisual_art.visual_art_mediumHaloperidolHairmedicine.drugInternational Journal of Legal Medicine
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The cell adhesion domain of type XVII collagen promotes integrin-mediated cell spreading by a novel mechanism.

2001

Type XVII collagen (BP180) is a keratinocyte transmembrane protein that exists as the full-length protein in hemidesmosomes and as a 120-kDa shed ectodomain in the extracellular matrix. The largest collagenous domain of type XVII collagen, COL15, has been described previously as a cell adhesion domain (Tasanen, K., Eble, J. A., Aumailley, M., Schumann, H., Baetge, J, Tu, H., Bruckner, P., and Bruckner-Tuderman, L. (2000) J. Biol. Chem. 275, 3093-3099). In the present work, the integrin binding of triple helical, human recombinant COL15 was tested. Solid phase binding assays using recombinant integrin alpha(1)I, alpha(2)I, and alpha(10)I domains and cell spreading assays with alpha(1)beta(1)…

KeratinocytesIntegrinsDNA ComplementaryDystoninIntegrinAmino Acid MotifsNerve Tissue ProteinsCHO CellsBiochemistryAutoantigensCollagen receptorCell LineCell MovementCricetinaeCell AdhesionTumor Cells CulturedAnimalsHumansCloning MolecularCell adhesionMolecular BiologyIntegrin bindingbiologyDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionHemidesmosomeCell BiologyNon-Fibrillar CollagensMolecular biologyRecombinant ProteinsProtein Structure TertiaryFibronectinHaCaTCytoskeletal ProteinsEctodomainbiology.proteinCollagenCarrier ProteinsPeptidesProtein BindingThe Journal of biological chemistry
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Potential antipsoriatic effect of chondroitin sulfate through inhibition of NF-κB and STAT3 in human keratinocytes

2012

Abstract Chondroitin sulfate (CS) is a natural glycosaminoglycan, formed by the 1–3 linkage of d -glucuronic acid to N-acetylgalactosamine, present in the extracellular matrix. It is used as a slow acting disease modifying agent in the treatment of osteoarthritis, and part of its beneficial effects are due to its antiinflammatory properties that result from an inhibitory effect on NF-κB signaling pathway. This ability raises the hypothesis that CS might be effective in other chronic inflammatory processes such as psoriasis, in which a deregulation of NF-κB is a key feature. In addition, psoriasis is characterized by an upregulation of STAT3 signaling pathway that is related to the epidermal…

KeratinocytesSTAT3 Transcription FactorBlotting WesternPrimary Cell CultureAnti-Inflammatory AgentsDermoscopyElectrophoretic Mobility Shift AssayPharmacologyStat3 Signaling Pathwaychemistry.chemical_compoundDownregulation and upregulationPsoriasismedicineHumansPsoriasisChondroitin sulfateCells CulturedPharmacologyChemistryChondroitin SulfatesNF-kappa BNF-κBmedicine.diseaseMicroscopy FluorescenceImmunologyPhosphorylationTumor necrosis factor alphaSignal transductionProtein BindingPharmacological Research
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Preliminary approach to elucidate the role of pigment as a binding site for drugs and chemicals in anagen hairs: pigments as carriers for 3 H-haloper…

2002

In view of the melanin-binding characteristics of haloperidol and its differential uptake by pigment- and non-pigment-producing cells, a co-culture of HaCaT with Sk-Mel-1 cell lines was performed to investigate whether melanosomes act as carriers for drug molecules associated with the pigments. Initially, HaCaT and Sk-Mel-1 cells were separately cultivated in the presence of 3H-haloperidol (400 pmol/ml medium ) for 28 days followed by subsequent co-cultivation in the absence of 3H-haloperidol for 5 days. The transfer of pigments into the keratinocytes during co-culture was confirmed by transmission electron microscopy. After the co-culture experiments a striking increase (or = 50%) of 3H-ha…

KeratinocytesStereochemistryCellBiologyPathology and Forensic MedicineMelaninPigmentmedicineHumansTissue DistributionMelanosomeMelaninsBinding SitesMelanosomesintegumentary systemPigmentationHair follicleMolecular biologyCoculture TechniquesIn vitroMicroscopy ElectronHaCaTmedicine.anatomical_structureCell culturevisual_artvisual_art.visual_art_mediumHaloperidolsense organsHairInternational Journal of Legal Medicine
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Resistance of keratinocytes to TGFbeta-mediated growth restriction and apoptosis induction accelerates re-epithelialization in skin wounds.

2002

The pleiotropic growth factor TGFβ plays an important role in regulating responses to skin injury. TGFβ targets many different cell types and is involved in all aspects of wound healing entailing inflammation,re-epithelialization, matrix formation and remodeling. To elucidate the role of TGFβ signal transduction in keratinocytes during cutaneous wound healing, we have used transgenic mice expressing a dominant negative type II TGFβ receptor exclusively in keratinocytes. We could demonstrate that this loss of TGFβ signaling in keratinocytes led to an accelerated re-epithelialization of full thickness excisional wounds accompanied by an increased proliferation in keratinocytes at the wound ed…

Keratinocytesmedicine.medical_treatmentEGR1InflammationApoptosisMice TransgenicBiologyImmediate early proteinCell LineImmediate-Early ProteinsMiceDownregulation and upregulationTransforming Growth Factor betamedicineAnimalsTranscription factorEarly Growth Response Protein 1Wound Healingintegumentary systemGrowth factorGene Expression ProfilingCell BiologyCell biologyDNA-Binding ProteinsEpidermal CellsImmunologymedicine.symptomSignal transductionEpidermisWound healingCell DivisionTranscription FactorsJournal of cell science
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Inhibition Mechanism of SARS‐CoV‐2 Main Protease with Ketone‐Based Inhibitors Unveiled by Multiscale Simulations: Insights for Improved Designs**

2021

Abstract We present the results of classical and QM/MM simulations for the inhibition of SARS‐CoV‐2 3CL protease by a hydroxymethylketone inhibitor, PF‐00835231. In the noncovalent complex the carbonyl oxygen atom of the warhead is placed in the oxyanion hole formed by residues 143 to 145, while P1–P3 groups are accommodated in the active site with interactions similar to those observed for the peptide substrate. According to alchemical free energy calculations, the P1′ hydroxymethyl group also contributes to the binding free energy. Covalent inhibition of the enzyme is triggered by the proton transfer from Cys145 to His41. This step is followed by the nucleophilic attack of the Sγ atom on …

KetoneMolecular modelStereochemistrySubstituentMolecular Dynamics SimulationSARS‐CoV‐2 Inhibitors | Hot PaperCatalysisQM/MM3CL proteasechemistry.chemical_compoundCatalytic DomaininhibitorsHumansHydroxymethylProtease InhibitorsCoronavirus 3C ProteasesResearch Articleschemistry.chemical_classificationPF-00835231Binding SitesbiologySARS-CoV-2molecular modelingActive siteCOVID-19General ChemistryGeneral MedicineKetonesCOVID-19 Drug TreatmentKineticschemistryCovalent bondDrug Designbiology.proteinThermodynamicsOxyanion holeResearch ArticleAngewandte Chemie
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Thermal aggregation of bovine serum albumin at different pH: comparison with human serum albumin.

2007

We report here a study on thermal aggregation of BSA at two different pH values selected to be close to the isoelectric point (pI) of this protein. Our aim is to better understand the several steps and mechanisms accompanying the aggregation process. For this purpose we have performed kinetics of integrated intensity emission of intrinsic and extrinsic dyes, tryptophans and ANS respectively, kinetics of Rayleigh scattering and of turbidity. The results confirm the important role played by conformational changes in the tertiary structure, especially in the exposure of internal hydrophobic regions that promote intermolecular interactions. We also confirm that the absence of electrostatic repu…

KineticsBiophysicsSerum albuminPlasma protein bindingProtein structuremedicineAnimalsHumansScattering RadiationIsoelectric PointBovine serum albuminSerum AlbuminbiologyChemistryCircular DichroismTryptophanSerum Albumin BovineGeneral MedicineHuman serum albuminProtein tertiary structureProtein Structure TertiaryIsoelectric pointBiochemistrybiology.proteinBiophysicsCattlemedicine.drugProtein Binding
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The Expanding Spectrum of Mutations in Hereditary Angioedema.

2021

The evolution in the knowledge of rare genetic diseases such as hereditary angioedema (HAE) has increased at a parallel pace with the development of new molecular tools. The deficiency of C1 inhibitor (C1-INH) has been recognized as the main cause of HAE (HAE-C1-INH) since the 1960s, but the discovery of the wide spectrum of mutations affecting the C1-INH gene (SERPING1) was possible only from the late 1980s, when Sanger sequencing became available and more accessible worldwide. Nevertheless, the involvement of other genes in HAE was discovered only in 2006 with the description of mutations in the F12 gene in patients with HAE and normal C1-INH. In the last 3 years, advanced next-generation…

Kininogen 1Muscle ProteinsGenomicsSeverity of Illness IndexDNA sequencingC1-inhibitorPathogenesis03 medical and health sciencessymbols.namesake0302 clinical medicineImmunology and AllergyMedicineHumans030212 general & internal medicineGeneSanger sequencingGeneticsbiologybusiness.industryCalcium-Binding ProteinsAngioedemas HereditaryMembrane Proteinsmedicine.disease030228 respiratory systemHereditary angioedemaMutationbiology.proteinsymbolsbusinessComplement C1 Inhibitor ProteinThe journal of allergy and clinical immunology. In practice
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Identification of an endothelial cell binding site on kininogen domain D3

1995

High and low molecular mass kininogen, two multidomain plasma proteins, bind to endothelial cells, platelets, and neutrophils in the intravascular compartment. The specific cell attachment site on their common heavy chain is mediated by domain-3, a cystatin-like structure with inhibitory capacity for papain-like proteinases (Jiang, Y., Müller-Esterl, W., and Schmaier, A. H. (1992) J. Biol. Chem. 267, 3712-3717). In this report, the domain-3 cell binding site is determined by an antibody-directed strategy. The epitope of monoclonal antibody HKH15, which binds to domain-3 and blocks the binding of kininogens to platelets and endothelial cells, was mapped using seven synthetic peptides, which …

Kininogen bindingBlotting WesternMolecular Sequence DataBiotinBinding CompetitiveBiochemistryEpitopeEpitopesHumansAmino Acid SequenceBinding siteMolecular BiologyKininogenBinding SitesMolecular massKininogensChemistryAntibodies MonoclonalCell BiologyMolecular biologyEndothelial stem cellBiochemistryBiotinylationEndothelium VascularCystatinPeptidesJournal of Biological Chemistry
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Mapping of the H-Kininogen Binding Site Exposed by the Prekallikrein Heavy Chain

1992

Kininogen bindingHeavy chainProtein structureBiochemistrybiologyChemistryMonoclonalPrekallikreinbiology.proteinBinding siteAntibodyPeptide sequence
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