Search results for "Cortactin"

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Methylmercury-induced developmental toxicity is associated with oxidative stress and cofilin phosphorylation. Cellular and human studies

2017

Environmental exposure to methylmercury (MeHg) during development is of concern because it is easily incorporated in children’s body both pre- and post-natal, it acts at several levels of neural pathways (mitochondria, cytoskeleton, neurotransmission) and it causes behavioral impairment in child. We evaluated the effects of prolonged exposure to 10–600 nM MeHg on primary cultures of mouse cortical (CCN) and of cerebellar granule cells (CGC) during their differentiation period. In addition, it was studied if prenatal MeHg exposure correlated with altered antioxidant defenses and cofilin phosphorylation in human placentas (n = 12) from the INMA cohort (Spain). Exposure to MeHg for 9 days in v…

0301 basic medicineDevelopmental DisabilitiesGlutathione reductaseCiencias de la SaludMitochondrionMETHYLMERCURYToxicologymedicine.disease_causeProtein CarbonylationMiceCytosolMITOCHONDRIAPregnancyPhosphorylationOXIDATIVE STRESSCells Culturedchemistry.chemical_classificationNeuronsbiologyGeneral NeuroscienceGlutathione peroxidaseCOFILINBrainMethylmercuryEnvironmental exposureCofilinMethylmercury CompoundsMitochondrial Proton-Translocating ATPasesGlutathioneCell biologyMitochondriaGlutathione ReductaseActin Depolymerizing FactorsCofilinPhosphorylationFemaleHuman placentaactinCortactinCIENCIAS MÉDICAS Y DE LA SALUDmacromolecular substancesACTIN03 medical and health sciencesCultured neuronsmedicineAnimalsHumansCULTURED NEURONSGlutathione PeroxidaseSalud OcupacionalHUMAN PLACENTAMolecular biology030104 developmental biologychemistryAnimals NewbornOxidative stressbiology.proteinOxidative stress
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Alix protein is substrate of Ozz-E3 ligase and modulates actin remodeling in skeletal muscle

2012

Alix/AIP1 is a multifunctional adaptor protein that participates in basic cellular processes, including membrane trafficking and actin cytoskeleton assembly, by binding selectively to a variety of partner proteins. However, the mechanisms regulating Alix turnover, subcellular distribution, and function in muscle cells are unknown. We now report that Alix is expressed in skeletal muscle throughout myogenic differentiation. In myotubes, a specific pool of Alix colocalizes with Ozz, the substrate-binding component of the muscle-specific ubiquitin ligase complex Ozz-E3. We found that interaction of the two endogenous proteins in the differentiated muscle fibers changes Alix conformation and pro…

Ubiquitin-Protein LigasesMuscle Fibers Skeletalmacromolecular substancesBiochemistryCell LineMiceCell MovementTwo-Hybrid System TechniquesmedicineCell AdhesionAnimalsProtein Interaction Domains and MotifsPseudopodiaMuscle SkeletalMolecular BiologyActinMice KnockoutbiologyMyogenesisSettore BIO/16 - Anatomia UmanaCalcium-Binding ProteinsUbiquitinationActin remodelingSkeletal muscleUbiquitin-Protein Ligase ComplexesCell BiologyActin cytoskeletonUbiquitin ligaseCell biologyRepressor ProteinsActin CytoskeletonProtein Transportmedicine.anatomical_structureUbiquitin ligase complexbiology.proteinCell Migration Myogenesis Skeletal Muscle Ubiquitin Ligase Ubiquitination Alix F-actin Ozz-E3 Ubiquitin Ligase Skeletal Muscle CellsCortactinCortactinProtein Binding
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