0000000000026664

AUTHOR

Giovanna Barbieri

0000-0002-5895-1795

showing 7 related works from this author

Diorganotin(IV) and triorganotin(IV) complexes of meso-tetra(4-sulfonatophenyl) porphine induce apoptosis in A375 human melanoma cells

2006

The cytotoxic effect of several diorganotin(IV) and triorganotin(IV)-meso-tetra(4-sulfonatophenyl)porphine derivatives was tested and only the (Bu(2)Sn)(2)TPPS and the (Bu(3)Sn)(4)TPPS showed cytotoxicity on A375 human melanoma cells. To examine the pathway of (Bu(2)Sn)(2)TPPS or (Bu(3)Sn)(4)TPPS induced A375 cell death, DNA fragmentation analysis, Annexin V binding and PI uptake as well as caspases activation analysis by Western blot were carried out. A375 cells treated exhibited several typical characteristics of apoptosis. Both the (Bu(2)Sn)(2)TPPS and the (Bu(3)Sn)(4)TPPS compounds activate caspase-8 and caspase-9 leading to caspase-3 activation. Thus, we propose that these two porphiri…

Cancer ResearchPorphyrinsCytotoxicityMelamoma cellAntineoplastic AgentsApoptosisDNA FragmentationWestern blotAnnexinCell Line TumorOrganotin CompoundsPimedicineHumansCytotoxic T cellCytotoxicityMelanomaCaspasebiologymedicine.diagnostic_testTriorganotin(IV)ApoptosiFlow CytometryMolecular biologyMicroscopy FluorescenceOncologyApoptosisCaspasesbiology.proteinDNA fragmentationDiorganotin(IV)
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Effects of two organotin(IV)(sulfonato phenyl)porphynates on the MAPKs and on the growth of A375 human melanoma cells

2009

Previously we showed apoptotic induction in A375 human melanoma cells using two complexes of the meso-tetra(4-sulfonatophenyl)porphinate (TPPS), (Bu 2 Sn) 2 TPPS and (Bu 3 Sn) 4 TPPS. To understand how these compounds activate apoptosis in melanoma cells we studied MAPKs and the (Bu 2 Sn) 2 TPPS and (Bu 3 Sn) 4 TPPS cellular uptake. Western blotting experiments showed activated protein kinases ERK 1/2, JNK and p38 in 10 μM (Bu 2 Sn) 2 TPPS- and 1 μM (Bu 3 Sn) 4 TPPS-treated melanoma cells, which suggests that the three MAP kinases are involved in the apoptotic death of A375-treated cells. By taking advantage of the porphyrin fluorescence, we found a fast concentration of (Bu 2 Sn) 2 TPPS an…

MAPK/ERK pathwayCancer ResearchPorphyrinsp38 mitogen-activated protein kinasesBlotting WesternAntineoplastic AgentsApoptosischemistry.chemical_compoundCell Line TumorOrganotin CompoundsHumansMelanomaCell ProliferationbiologyKinaseCell growthGeneral MedicineA375 melamoma cells meso-tetra(4-sulfonato phenyl)porphinate MAPKs FAK cell growthMolecular biologyPorphyrinIn vitroMicroscopy Fluorescence MultiphotonOncologyBiochemistrychemistryApoptosisSettore CHIM/03 - Chimica Generale E InorganicaMitogen-activated protein kinasebiology.proteinMitogen-Activated Protein Kinases
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The Odyssey of Hsp60 from Tumor Cells to Other Destinations Includes Plasma Membrane-Associated Stages and Golgi and Exosomal Protein-Trafficking Mod…

2012

BACKGROUND: In a previous work we showed for the first time that human tumor cells secrete Hsp60 via exosomes, which are considered immunologically active microvesicles involved in tumor progression. This finding raised questions concerning the route followed by Hsp60 to reach the exosomes, its location in them, and whether Hsp60 can be secreted also via other mechanisms, e.g., by the Golgi. We addressed these issues in the work presented here. PRINCIPAL FINDINGS: We found that Hsp60 localizes in the tumor cell plasma membrane, is associated with lipid rafts, and ends up in the exosomal membrane. We also found evidence that Hsp60 localizes in the Golgi apparatus and its secretion is prevent…

Cell Physiologyanimal structuresAnatomy and PhysiologyHistologylcsh:MedicineGolgi ApparatusBiologyExosomesBiochemistrysymbols.namesakeCytosolMembrane MicrodomainsDiagnostic MedicineCell Line TumorOrganelleMolecular Cell BiologyPathologyHumansSecretionlcsh:ScienceLipid raftBiologyhsp60 exosomeOrganellesMultidisciplinarylcsh:RfungiChaperonin 60Golgi apparatusMicrovesiclesCellular StructuresTransport proteinCell biologyProtein TransportMembrane proteinSubcellular OrganellesTumor progressionsymbolsCytochemistryMedicinelcsh:QMembranes and SortingExtracellular SpaceBiomarkersResearch ArticleGeneral PathologyPLoS ONE
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Supramolecular Assemblies Based on Complexes of Nonionic Amphiphilic Cyclodextrins and a meso-Tetra(4- sulfonatophenyl)porphine Tributyltin(IV) Deriv…

2013

Amphiphilic cyclodextrin (ACyD) provides water-soluble and adaptable nanovectors by modulating the balance between the hydrophobic and hydrophilic chains at both CyD sides. This work aimed to design nanoassemblies based on nonionic and hydrophilic ACyD (SC6OH) for the delivery of a poor-water-soluble organotin(IV)-porphyrin derivative [(Bu3Sn)4TPPS] to melanoma cancer cells. To characterize the porphyrin derivatives under simulated physiological conditions, a speciation was performed using complementary techniques. In aqueous solution (≤ 20 μM), (Bu3Sn)4TPPS primarily exists as a monomer (2 in Figure 1), as suggested by the low static anisotropy (ρ ≈ 0.02) with a negligible formation of por…

Polymers and PlasticsCell SurvivalSurface PropertiesPotentiometric titrationSupramolecular chemistryAntineoplastic AgentsBioengineeringBiomaterialsStructure-Activity RelationshipSurface-Active Agentschemistry.chemical_compoundDrug Delivery SystemsAmphiphilePolymer chemistryTumor Cells CulturedMaterials ChemistryHumansOrganic chemistryParticle SizeMelanomaMELANOMA porphyrins organotin(IV)Cell Proliferationchemistry.chemical_classificationCyclodextrinsAqueous solutionCell DeathDose-Response Relationship DrugMolecular StructureCyclodextrinPorphyrinNanomedicineMonomerchemistrySettore CHIM/03 - Chimica Generale E InorganicaDrug Screening Assays AntitumorTrialkyltin CompoundsDrug carrier
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Apoptosis and cell growth arrest in A375 human melanoma cells by diorganotin(IV) and triorganotin(IV) complexes of [meso-Tetra(4-sulfonatophenyl)porp…

2011

In previous studies we have demonstrated that two derivatives of meso-Tetra(4-sulfonatophenyl)porphine (TPPS), (Bu2Sn)2TPPS and (Bu3Sn)4TPPS, cause apoptotic death of A375 melanoma cells and, at lower concentrations, arrest of cell proliferation. In the present study, we examined if the manganese metal inside the porphyrin cavity could improve the efficacy of this class of compounds. Thus, [meso- Tetra(4-sulfonatophenyl)porphine]Mn(III)Cl (=MnTPPS) derivatives, namely (Me2Sn)2MnTPPS, (Bu2Sn)2MnTPPS, (Me3Sn)4MnTPPS and (Bu3Sn)4MnTPPS, were tested on the A375 human melanoma cell line. A cytotoxicity assay showed that (Bu2Sn)2MnTPPS and (Bu3Sn)4MnTPPS were highly cytotoxic by inducing apoptosi…

HoechstCancer ResearchPorphyrinsSkin NeoplasmsMetalloporphyrinsDrug Evaluation PreclinicalAntineoplastic AgentsApoptosisDNA Fragmentationß-cateninBiology010402 general chemistry01 natural sciencesChloridesc-mycCell Line TumorsnailOrganotin CompoundsHumansCytotoxic T cellViability assayCytotoxicityMelanomacell viabilityCell Proliferation010405 organic chemistryCell growthCell cycleMolecular biology0104 chemical sciences3. Good healthManganese CompoundsOncologyCell cultureApoptosisDNA fragmentationcell viability; ß-catenin; c-myc; snail; HoechstInternational Journal of Oncology
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Dibutyltin(IV) and Tributyltin(IV) Derivatives of meso-Tetra(4 sulfonatophenyl)porphine Inhibit the Growth and the Migration of Human Melanoma Cells.

2019

Melanoma is the most aggressive and deadly form of skin cancer, which is largely due to its propensity to metastasize. Therefore, with the aim to inhibit the growth and the metastatic dissemination of melanoma cells and to provide a novel treatment option, we studied the effects of the melanoma treatment with two organotin(IV) complexes of the meso-tetra(4-sulfonato-phenyl)porphine, namely (Bu2Sn)2TPPS and (Bu3Sn)4TPPS. In particular, we showed that nanomolar concentrations of (Bu2Sn)2TPPS and (Bu3Sn)4TPPS are sufficient to inhibit melanoma cell growth, to increase the expression of the full-length poly (ADP-ribose) polymerase (PARP-1), to induce the cell cycle arrest respectively at G2/M a…

0301 basic medicinePorphyrinsCellAntineoplastic AgentsApoptosisorganotin(IV)migrationArticleBRAF03 medical and health sciences0302 clinical medicineCyclin D1Cell MovementCell Line Tumormelanoma; organotin(IV); cellular growth; BRAF; cell cycle; migrationmedicinemelanomaHumansSTAT3Cell ProliferationDose-Response Relationship DrugMolecular StructurebiologyCell growthChemistryMelanomaCell migrationCell Cycle CheckpointsGeneral Medicinecellular growthCell cyclemedicine.disease030104 developmental biologymedicine.anatomical_structureFocal Adhesion Kinase 1030220 oncology & carcinogenesisbiology.proteinCancer researchcell cycleSkin cancerSignal Transduction
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Negative Regulation of β Enolase Gene Transcription in Embryonic Muscle Is Dependent upon a Zinc Finger Factor That Binds to the G-rich Box within th…

1998

We have previously identified a muscle-specific enhancer within the first intron of the human beta enolase gene. Present in this enhancer are an A/T-rich box that binds MEF-2 protein(s) and a G-rich box (AGTGGGGGAGGGGGCTGCG) that interacts with ubiquitously expressed factors. Both elements are required for tissue-specific expression of the gene in skeletal muscle cells. Here, we report the identification and characterization of a Kruppel-like zinc finger protein, termed beta enolase repressor factor 1, that binds in a sequence-specific manner to the G-rich box and functions as a repressor of the beta enolase gene transcription in transient transfection assays. Using fusion polypeptides of b…

AgingTranscription GeneticMolecular Sequence DataDown-RegulationRepressorRegulatory Sequences Nucleic AcidBiologyBiochemistryDNA-binding proteinGene Expression Regulation EnzymologicMiceGene expressionAnimalsHumansAmino Acid SequenceCloning MolecularMuscle SkeletalEnhancerMolecular BiologyCell NucleusRegulation of gene expressionZinc fingerSp1 transcription factorBinding SitesSequence Homology Amino AcidZinc FingersCell BiologyMolecular biologyDNA-Binding ProteinsEnhancer Elements GeneticRegulatory sequencePhosphopyruvate HydrataseJournal of Biological Chemistry
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