Search results for "Ezrin"

showing 4 items of 4 documents

Identification and relevance of the CD95-binding domain in the N-terminal region of ezrin.

2003

The CD95 (Fas/APO-1) linkage to the actin cytoskeleton through ezrin is an essential requirement for susceptibility to the CD95-mediated apoptosis in CD4+ T cells. We have previously shown that moesin was not involved in the binding to CD95. Here we further support the specificity of the ezrin/CD95 binding, showing that radixin did not bind CD95. The ezrin region specifically and directly involved in the binding to CD95 was located in the middle lobe of the ezrin FERM domain, between amino acids 149 and 168. In this region, ezrin, radixin, and moesin show 60-65% identity, as compared with the 86% identity in the whole FERM domain. Transfection of two different human cell lines with a green …

Moesinchemical and pharmacologic phenomenaApoptosismacromolecular substancesBiologyBiochemistryEzrinRadixinhemic and lymphatic diseasesHumansfas ReceptorMolecular BiologyActinBinding SitesFERM domainhemic and immune systemsCell BiologyTransfectionActin cytoskeletonPhosphoproteinsActinsCell biologyProtein Structure TertiaryCytoskeletal ProteinsMutationbiological phenomena cell phenomena and immunityBinding domainHeLa CellsProtein BindingSignal TransductionThe Journal of biological chemistry
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Immunodetection of the microvillous cytoskeleton molecules villin and ezrin in the parasitophorous vacuole wall of Cryptosporidium parvum (Protozoa: …

1999

Microvilli - actin - villin - ezrin - Cryptosporidium parvum The sporozoites and merozoites of the Apicomplexan protozoan Cryptosporidium parvum (C. parvum) invade the apical side of enterocytes and induce the formation of a parasitophorous vacuole which stays in the brush border area and disturbs the distribution of microvilli. The vacuole is separated from the apical cytoplasm of the cell by an electron-dense layer of undetermined composition. In order to characterize the enterocyte cytoskeleton changes that occur during C. parvum invasion and development, we used both confocal immunofluorescence and immunoelectron microscopy to examine at the C.parvum-enterocyte interface the distributio…

Feces/microbiologyIntestines/parasitologyMicrofilament Proteins/ analysisVacuoleddc:616.07Actins/analysisRats Sprague-DawleyFecesMiceEzrinCarrier Proteins/ analysisCryptosporidium/ chemistry/pathogenicity/ultrastructureCytoskeletonMicroscopy ImmunoelectronCytoskeletonMice Inbred BALB CMicroscopy ConfocalbiologyMicrovilliMicrofilament ProteinsCytoskeleton/ chemistryGeneral MedicineCell biologyIntestinesCryptosporidium parvumFemaleVillinHistologyImmunoelectron microscopyVacuoles/ultrastructurePhosphoproteins/ analysisCryptosporidiummacromolecular substancesPathology and Forensic Medicineparasitic diseasesAnimalsApical cytoplasmActinCell Biologybiology.organism_classificationPhosphoproteinsActinsRatsMicrovilli/ chemistryCytoskeletal ProteinsMicroscopy ElectronVacuolesbiology.proteinCarrier ProteinsEuropean journal of cell biology
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Proprotein convertase 5/6 is critical for embryo implantation in women: regulating receptivity by cleaving ebp50, modulating ezrin binding, and membr…

2011

Establishment of endometrial receptivity is vital for successful embryo implantation; its failure causes infertility. Epithelial receptivity acquisition involves dramatic structural changes in the plasma membrane and cytoskeleton. Proprotein convertase 5/6 (PC6), a serine protease of the proprotein convertase (PC) family, is up-regulated in the human endometrium specifically at the time of epithelial receptivity and stromal cell decidualization. PC6 is the only PC member tightly regulated in this manner. The current study addressed the importance and mechanisms of PC6 action in regulating receptivity in women. PC6 was dysregulated in the endometrial epithelium during the window of implantat…

Scaffold proteinmedicine.medical_specialtySodium-Hydrogen ExchangersPlasma protein bindingBiologyEndometriumMiceEndocrinologyEzrinInternal medicinemedicineAnimalsHumansEmbryo ImplantationCytoskeletonCytoskeletonCellular localizationBinding proteinDecidualizationEpithelial CellsPhosphoproteinsProprotein convertaseCytoskeletal ProteinsEndocrinologyProprotein Convertase 5FemaleProtein Binding
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TRAIL signalling regulation by ezrin

2011

Background and Aim: TRAIL has sparked a growing interest in oncology due to its ability to selectively trigger cancer cell death while sparing normal cells. The Fas/actin association through ezrin, a member of the ERM protein family, has been reported to regulate early steps of Fas-mediated apoptosis. In this project, we addressed the role of ezrin regarding TRAIL-induced cell death in B lymphoma cell lines, or adherent cancer cell lines (HeLa WT, HCT116, SW480). Methods: Molecular and biochemical approaches were employed to study the relevance of ezrin and its phosphorylation status in TRAIL signaling. Results: We found that ezrin displays a negative function towards TRAIL- and Fas-mediate…

[SDV.SA]Life Sciences [q-bio]/Agricultural sciences[SDV.SA] Life Sciences [q-bio]/Agricultural sciences[SDV.MHEP] Life Sciences [q-bio]/Human health and pathologyTRAIL-RTRAILmacromolecular substancesEzrinenvironment and public healthEzrineCytosquelette[ SDV.MHEP ] Life Sciences [q-bio]/Human health and pathologyChemotherapyPhosphorylationActine[ SDV.SA ] Life Sciences [q-bio]/Agricultural sciences[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyActinCytoskeletonChimiothérapieCancer
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