Search results for "Thioacetamide"

showing 4 items of 4 documents

Optimized Mouse Models for Liver Fibrosis

2017

Fibrosis is the excessive accumulation of extracellular matrix components due to chronic injury, with collagens as predominant structural components. Liver fibrosis can progress to cirrhosis, which is characterized by a severe distortion of the delicate hepatic vascular architecture, the shunting of the blood supply away from hepatocytes and the resultant functional liver failure. Cirrhosis is associated with a highly increased morbidity and mortality and represents the major hard endpoint in clinical studies of chronic liver diseases. Moreover, cirrhosis is a strong cofactor of primary liver cancer. In vivo models are indispensable tools to study the cellular and molecular mechanisms of li…

0301 basic medicinePathologymedicine.medical_specialtyCirrhosisbusiness.industryLiver fibrosismedicine.diseaseVascular architectureExtracellular matrix03 medical and health scienceschemistry.chemical_compound030104 developmental biology0302 clinical medicinechemistryIn vivoFibrosisMedicine030211 gastroenterology & hepatologyThioacetamidebusinessPrimary liver cancer
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Increased hepatic fibrosis and JNK2-dependent liver injury in mice exhibiting hepatocyte-specific deletion of cFLIP.

2012

Chronic liver disease promotes hepatocellular injury involving apoptosis and triggers compensatory regeneration that leads to the activation of quiescent stellate cells in the liver. The deposition of extracellular matrix from activated myofibroblasts promotes hepatic fibrosis and the progression to cirrhosis with deleterious effects on liver physiology. The role of apoptosis signaling pathways in the development of fibrosis remains undefined. The aim of the current study was to determine the involvement of the caspase-8 homologue cellular FLICE-inhibitory protein (cFLIP) during the initiation and progression of fibrosis. Liver injury and fibrosis from carbon tetrachloride (CCl4) and thioa…

Liver CirrhosisMalePathologymedicine.medical_specialtyTime FactorsGenotypePhysiologyCASP8 and FADD-Like Apoptosis Regulating ProteinApoptosisBiologyThioacetamideChronic liver diseaseMicePhysiology (medical)medicineAnimalsMitogen-Activated Protein Kinase 9PhosphorylationExtracellular Signal-Regulated MAP KinasesCarbon TetrachlorideCompensatory regenerationLiver injuryMice KnockoutHepatologyCaspase 3Gastroenterologymedicine.diseaseCaspase 9Enzyme ActivationDisease Models Animalmedicine.anatomical_structurePhenotypeLiverApoptosisHepatocyteHepatic stellate cellCancer researchDisease ProgressionHepatocytesHepatocellular injuryChemical and Drug Induced Liver InjuryHepatic fibrosisSignal TransductionAmerican journal of physiology. Gastrointestinal and liver physiology
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Liver regeneration induced by a designer human IL‐6/ sIL‐6R fusion protein reverses severe hepatocellular injury

2000

The cytokine IL-6 plays a significant role in liver regeneration in conjunction with additional growth factors (HGF, TNF-α, and TGF-α). Many IL-6 effects depend on a naturally occurring soluble IL-6 receptor (sIL-6R). Here, the chimeric protein hyper-IL-6, constructed from the human IL-6 protein fused to a truncated form of its receptor, was found to have superagonistic IL-6 properties, and as such, enhanced liver cell regeneration. Hyper-IL-6 reversed the state of hepatotoxicity and enhanced the survival rates of rats suffering from fulminant hepatic failure after D-galactosamine administration. The hyper-IL-6 protein has a significant potential for use in the treatment of severe human liv…

MalePathologymedicine.medical_specialtyRecombinant Fusion Proteinsmedicine.medical_treatmentApoptosisGalactosamineThioacetamideBiochemistryFulminant hepatic failureGeneticsmedicineAnimalsHumansReceptorInterleukin 6Molecular BiologybiologyInterleukin-6ChemistryLiver cellRegeneration (biology)Receptors InterleukinReceptors Interleukin-6Fusion proteinRats Inbred F344Liver regenerationLiver RegenerationRatsDisease Models AnimalCytokineCancer researchbiology.proteinCell DivisionLiver FailureBiotechnologyThe FASEB Journal
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Discovery and validation of small-molecule heat-shock protein 90 inhibitors through multimodality molecular imaging in living subjects.

2012

Up-regulation of the folding machinery of the heat-shock protein 90 (Hsp90) chaperone protein is crucial for cancer progression. The two Hsp90 isoforms (α and β) play different roles in response to chemotherapy. To identify isoform-selective inhibitors of Hsp90(α/β)/cochaperone p23 interactions, we developed a dual-luciferase (Renilla and Firefly) reporter system for high-throughput screening (HTS) and monitoring the efficacy of Hsp90 inhibitors in cell culture and live mice. HTS of a 30,176 small-molecule chemical library in cell culture identified a compound, N -(5-methylisoxazol-3-yl)-2-[4-(thiophen-2-yl)-6-(trifluoromethyl)pyrimidin-2-ylthio]acetamide (CP9), that binds to Hsp90(α/β) an…

Thymidine kinase activityProtein FoldingImmunoprecipitationLactams MacrocyclicBlotting WesternMice NudeThiophenesBiologyThioacetamideTritiumSmall Molecule LibrariesMiceco-chaperone p23Luciferases FireflyHeat shock proteinCell Line TumorNeoplasmsAcetamidesDrug DiscoveryBenzoquinonesAnimalsHumansImmunoprecipitationProtein IsoformsLuciferaseHSP90 Heat-Shock ProteinsLuciferases RenillaProstaglandin-E SynthasesMultidisciplinaryCell growthImidazolesbioluminescence imagingHsp90Small moleculeMolecular biologydrug developmentHigh-Throughput Screening Assayssmall-molecule inhibitorsIntramolecular OxidoreductasesLeadPNAS PlusCell culturePositron-Emission TomographyPyrazinesbiology.proteinPET/computed tomography imagingTomography X-Ray ComputedProceedings of the National Academy of Sciences of the United States of America
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