Search results for "Cytotoxic"

showing 10 items of 1673 documents

2019

In photodynamic therapy (PDT), photosensitizers and light are used to cause photochemically induced cell death. The selectivity and the effectiveness of the phototoxicity in cancer can be increased by a specific uptake of the photosensitizer into tumor cells. A promising target for this goal is the folic acid receptor α (FRα), which is overexpressed on the surface of many tumor cells and mediates an endocytotic uptake. Here, we describe a polysaccharide-based nanoparticle system suitable for targeted uptake and its photochemical and photobiological characterization. The photosensitizer 5, 10, 15, 20-tetraphenyl-21H, 23H-porphyrine (TPP) was encapsulated in spermine- and acetal-modified dext…

Polymers and Plasticsmedicine.medical_treatmentSperminePhotodynamic therapyGeneral ChemistryReceptor-mediated endocytosischemistry.chemical_compoundDextranchemistryDrug deliverymedicineCancer researchPhotosensitizerCytotoxicityPhototoxicityPolymers
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Polynuclear complexes of Pt(II) with polypyridyl ligands.II.Synthesis, spectroscopic and structural characterization and cytotoxic activity

2007

Polynuclear complexes Platinum Synthesis Cytotoxic activity
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CD8+CD45RA+CD27-CD28-T-cell subset in PBL of cervical cancer patients representing CD8+T-cells being able to recognize cervical cancer associated ant…

2003

Objective In response to antigenic stimulation, naive MHC-class I restricted and antigen-specific CD8+CD45RA+CD28+T-cells undergo clonal expansion and differentiate into CD8+CD45RO+ memory T-cells. Upon re- encounter with the nominal antigen, CD45RO+ T-cells are able to convert to CD8+CD45RA+CD28-T-cells displaying potent immune effector functions, including TNF-alpha production. This T-cell subpopulation constitutes a minor population in healthy individuals. In the present study we are currently evaluating whether this particular T-cell subset in PBL represents CD8+T-cells which may be able to recognize cervical cancer associated antigens provided by HPV 16 E7. Material and methods Flow-cy…

PopulationUterine Cervical Neoplasmschemical and pharmacologic phenomenaCD8-Positive T-LymphocytesBiologyEpitopeImmune systemCD28 AntigensAntigenAntigens CDT-Lymphocyte SubsetsmedicineHumansCytotoxic T cellAmino Acid SequenceeducationAntigens ViralPapillomaviridaeNeoplasm Stagingeducation.field_of_studyHistocompatibility TestingObstetrics and GynecologyCD28Cancerhemic and immune systemsmedicine.diseasePeptide FragmentsTumor Necrosis Factor Receptor Superfamily Member 7Lymphatic MetastasisImmunologyCytokinesLeukocyte Common AntigensFemaleCD8Zentralblatt für Gynäkologie
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Zn-Enhanced Asp-Rich Antimicrobial Peptides N-Terminal Coordination by Zn(II) and Cu(II), Which Distinguishes Cu(II) Binding to Different Peptides

2021

The antimicrobial activity of surfactant-associated anionic peptides (SAAPs), which are isolated from the ovine pulmonary surfactant and are selective against the ovine pathogen Mannheimia haemolytica, is strongly enhanced in the presence of Zn(II) ions. Both calorimetry and ITC measurements show that the unique Asp-only peptide SAAP3 (DDDDDDD) and its analogs SAAP2 (GDDDDDD) and SAAP6 (GADDDDD) have a similar micromolar affinity for Zn(II), which binds to the N-terminal amine and Asp carboxylates in a net entropically-driven process. All three peptides also bind Cu(II) with a net entropically-driven process but with higher affinity than they bind Zn(II) and coordination that involves the N…

Pore Forming Cytotoxic Proteins0301 basic medicineStereochemistryQH301-705.5Metal ions in aqueous solutionAntimicrobial peptidesPeptide010402 general chemistry01 natural sciencesArticleCatalysisInorganic Chemistry03 medical and health scienceschemistry.chemical_compoundthermodynamicsDeprotonationZn(II) and Cu(II) bioinorganic chemistryPulmonary surfactantAmidePhysical and Theoretical ChemistryBiology (General)Mannheimia haemolyticaMolecular BiologyQD1-999Spectroscopychemistry.chemical_classificationOrganic ChemistryElectron Spin Resonance SpectroscopyGeneral Medicine0104 chemical sciencesComputer Science ApplicationsZincChemistry030104 developmental biologyMembranechemistryAmine gas treatingmetal-antimicrobial peptide interactionsPeptidesCopperInternational Journal of Molecular Sciences
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A lipocentric view of peptide-induced pores

2010

Although lipid membranes serve as effective sealing barriers for the passage of most polar solutes, nonmediated leakage is not completely improbable. A high activation energy normally keeps unassisted bilayer permeation at a very low frequency, but lipids are able to self-organize as pores even in peptide-free and protein-free membranes. The probability of leakage phenomena increases under conditions such as phase coexistence, external stress or perturbation associated to binding of nonlipidic molecules. Here, we argue that pore formation can be viewed as an intrinsic property of lipid bilayers, with strong similarities in the structure and mechanism between pores formed with participation …

Pore Forming Cytotoxic ProteinsCell Membrane PermeabilityMembrane permeabilityMembrane lipidsPore energeticsBiophysicsThermal fluctuationsReviewMolecular Dynamics SimulationSurface tensionMembrane LipidsAnti-Infective AgentsLipid bilayerChemistryBilayerLipidic poreGeneral MedicinePermeationCrystallographyMembrane permeabilityMembraneBiophysicsAntimicrobial peptidePore structurePorosityPore-forming proteinsEuropean Biophysics Journal
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Functional size of complement and perforin pores compared by confocal laser scanning microscopy and fluorescence microphotolysis

1991

Abstract Confocal laser scanning microscopy and fluorescence microphotolysis (also referred to as fluorescence photobleaching recovery) were employed to study the transport of hydrophilic fluorescent tracers through complement and perforin pores. By optimizing the confocal effect it was possible to determine the exclusion limit of the pores in situ, i.e. without separation of cells and tracer solution. Single-cell flux measurements by fluorescence microphotolysis yielded information on the sample population distribution of flux rates. By these means a direct comparison of complement and perforin pores was made in sheep erythrocyte membranes. In accordance with previous studies employing a v…

Pore Forming Cytotoxic ProteinsIn situCell Membrane PermeabilityConfocalBiophysicsAntigen-Antibody ComplexIn Vitro TechniquesBiologyBiochemistryTumor Cells CulturedmedicineAnimalsHumansMembrane GlycoproteinsSheepPerforinLasersCell MembraneErythrocyte MembraneMembrane ProteinsComplement System ProteinsCell BiologyFluorescencePhotobleachingCell biologyRed blood cellmedicine.anatomical_structureMembranePerforinMicroscopy Electron Scanningbiology.proteinCytolysinBiochimica et Biophysica Acta (BBA) - Biomembranes
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Pore-forming toxins activate MAPK p38 by causing loss of cellular potassium.

2009

Mitogen activated protein kinase (MAPK) p38 has emerged as a survival protein in cells that are attacked by bacterial toxins forming small membrane pores. Activation of p38 by pore forming toxins (PFT) has been attributed to osmotic stress, but here we show that loss of K+ is likely to be the critical parameter. Several lines of evidence support this conclusion: first, osmoprotection did not prevent p38-phosphorylation in alpha-toxin-loaded cells. Second, treatment of cells with a K+ ionophore, or simple incubation in K+-free medium sufficed to cause robust p38-phosphorylation. Third, media containing high [K+] prevented p38-activation by Staphylococcus aureus alpha-toxin, Vibrio cholerae c…

Pore Forming Cytotoxic ProteinsOsmotic shockp38 mitogen-activated protein kinasesBacterial ToxinsBiophysicsBiologyHemolysin ProteinsBiochemistryp38 Mitogen-Activated Protein KinasesCell LineCell membraneHemolysin ProteinsmedicineHumansPhosphorylationMolecular BiologyPore-forming toxinEscherichia coli ProteinsCell MembraneHemolysinEpithelial CellsCell BiologyCell biologyEnzyme Activationmedicine.anatomical_structureBiochemistryPotassiumStreptolysinCalciumCytolysinBiochemical and biophysical research communications
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Pore formation by Vibrio cholerae cytolysin requires cholesterol in both monolayers of the target membrane

2007

Vibrio cholerae cytolysin (VCC) forms oligomeric transmembrane pores in cholesterol-rich membranes. To better understand this process, we used planar bilayer membranes. In symmetric membranes, the rate of the channel formation by VCC has a superlinear dependency on the cholesterol membrane fraction. Thus, more than one cholesterol molecule can facilitate VCC-pore formation. In asymmetric membranes, the rate of pore formation is limited by the leaflet with the lower cholesterol content. Methyl-beta-cyclodextrin, which removes cholesterol from membranes, rapidly inhibits VCC pore formation, even when it is added to the side opposite that of VCC addition. The results suggest that cholesterol i…

Pore Forming Cytotoxic Proteinsgenetic structuresLipid BilayersBiologymedicine.disease_causeBiochemistrychemistry.chemical_compoundMonolayermedicineAnimalsMoleculeVibrio choleraePore-forming toxinMembrane GlycoproteinsPerforinCholesterolbeta-CyclodextrinsGeneral Medicineeye diseasesTransmembrane proteinCholesterolMembraneBiochemistrychemistryVibrio choleraeBiophysicsCattlelipids (amino acids peptides and proteins)sense organsCytolysinBiochimie
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EFFECT OF EXTRACTS FROM LEAVES AND RHIZOMES OF THE SEAGRASS POSIDONIA OCEANICA ON HEPG2 HEPATOCARCINOMA (HCC) CELLS

2022

Posidonia oceanica Hepg2 cells cytotoxicity liver cancer apoptosis autophagy ROS productionSettore BIO/05 - ZoologiaSettore BIO/06 - Anatomia Comparata E Citologia
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Effect of flupirtine on Bcl-2 and glutathione level in neuronal cells treated in vitro with the prion protein fragment (PrP106-126).

1997

Flupirtine, trade name Katadolon, is a centrally acting nonopioid analgesic that has recently been found to display cytoprotective activity in vitro and in vivo on neurons induced to undergo apoptosis. This report shows that the PrP106-126 fragment of the prion protein, which is the likely etiological agent for a series of encephalopathies, is toxic to cortical neurons in vitro. Simultaneously, PrP106-126 influences the molecular GSH content and the bcl-2 expression in neurons. Significant toxicity (32% reduction in cell viability) was observed at a concentration of 50 microM of the peptide after 9 days of incubation, while at higher concentrations toxicity increased to 70%. Neurotoxicity w…

PrionsMolecular Sequence DataAminopyridinesApoptosisPharmacologyBiologychemistry.chemical_compoundDevelopmental NeurosciencemedicineAnimalsAmino Acid SequenceRats WistarCytotoxicityCells CulturedNeuronsNeurotoxicityGlutathioneAnalgesics Non-Narcoticmedicine.diseaseGlutathioneIn vitroPeptide FragmentsGenes bcl-2RatsOxidative StressNeuroprotective AgentsNeurologychemistryGene Expression RegulationProto-Oncogene Proteins c-bcl-2ApoptosisCell cultureImmunologyToxicityFlupirtineOxidation-Reductionmedicine.drugExperimental neurology
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