Search results for "Centrin"

showing 10 items of 12 documents

Communicative Method and Paradigms of Gender and (Post-)colonial Studies in the Foreign Language and Literature Class as Activators of Cognitive Dece…

2009

Communicative method gender studies postcolonial studies cognitive decentring
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Angular roughshark Oxynotus centrina (Squaliformes: Oxynotidae) in captivity feeding exclusively on elasmobranch eggs: an overlooked feeding niche or…

2015

A specimen of angular roughshark Oxynotus centrina has been kept successfully in captivity for the first time. Over a period of 24 months, the specimen preyed exclusively on the contents of elasmobranch egg cases, suggesting a specialized trophic niche.

Food chainTasteSqualiformesEcologyOxynotus centrinaNicheCaptivityAquatic ScienceBiologyTrophic nichebiology.organism_classificationOxynotidaeEcology Evolution Behavior and SystematicsJournal of Fish Biology
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Roles for ELMOD2 and Rootletin in ciliogenesis.

2021

AbstractELMOD2 is a GTPase activating protein (GAP) with uniquely broad specificity for ARF family GTPases. We previously showed that it acts with ARL2 in mitochondrial fusion and microtubule stability and with ARF6 during cytokinesis. Mouse embryonic fibroblasts deleted for ELMOD2 also displayed changes in cilia related processes including increased ciliation, multiciliation, ciliary morphology, ciliary signaling, centrin accumulation inside cilia, and loss of rootlets at centrosomes with loss of centrosome cohesion. Increasing ARL2 activity or overexpressing Rootletin reversed these defects, revealing close functional links between the three proteins. This was further supported by the fin…

GTPase-activating proteinBiologyMicrotubulesMitochondrial DynamicsCell Line03 medical and health sciencesMice0302 clinical medicineMicrotubuleGTP-Binding ProteinsCiliogenesisAnimalsHumansCiliaMolecular Biology030304 developmental biologyCytokinesisCentrosome0303 health sciencesADP-Ribosylation FactorsCiliumGTPase-Activating ProteinsCell BiologyArticlesFibroblastsCell biologyMitochondriaCytoskeletal Proteinsmitochondrial fusionCentrosomeCentrinRootletin030217 neurology & neurosurgeryCytokinesisSignal TransductionMolecular biology of the cell
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Centrins, gatekeepers for the light-dependent translocation of transducin through the photoreceptor cell connecting cilium

2006

Centrins are members of a highly conserved subgroup of the EF-hand superfamily of Ca(2+)-binding proteins commonly associated with centrosome-related structures. In the retina, centrins are also prominent components of the photoreceptor cell ciliary apparatus. Centrin isoforms are differentially localized at the basal body and in the lumen of the connecting cilium. All molecular exchanges between the inner and outer segments occur through this narrow connecting cilium. Ca(2+)-activated centrin isoforms bind to the visual heterotrimeric G-protein transducin via an interaction with the betagamma-subunit. Ca(2+)-dependent assemblies of centrin/G-protein complexes may regulate the transducin mo…

Gene isoformPhotoreceptorsgenetic structuresPhotoreceptor cellHeterotrimeric G proteinConnecting ciliummedicineCentrinBasal bodyAnimalsPhotoreceptor CellsCiliaTransducinPhosphorylationVision OcularCentrosomeRetinaChemistryLight-dependent translocationCiliumCalcium-Binding ProteinsSensory SystemsCell biologyProtein TransportOphthalmologymedicine.anatomical_structureCentrinVertebratesTransducinsense organsPhotic StimulationVision Research
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Centrins in retinal photoreceptor cells: regulators in the connecting cilium.

2008

Changes in the intracellular Ca2+ concentration regulate the visual signal transduction cascade directly or more often indirectly through Ca2+-binding proteins. Here we focus on centrins, which are members of a highly conserved subgroup of the EF-hand superfamily of Ca2+-binding proteins in photoreceptor cells of the vertebrate retina. Centrins are commonly associated with centrosome-related structures. In mammalian retinal photoreceptor cells, four centrin isoforms are expressed as prominent components in the connecting cilium linking the light-sensitive outer segment compartment with the metabolically active inner segment compartment. Our data indicate that Ca2+-activated centrin isoforms…

Gene isoformgenetic structuresChromosomal Proteins Non-HistoneBiologyContractile ProteinsHeterotrimeric G proteinmedicineCompartment (development)AnimalsHumansCiliaEye ProteinsVision OcularRetinaCalcium-Binding ProteinsSensory SystemsCell biologyOphthalmologymedicine.anatomical_structureCentrinCalciumsense organsTransducinSignal transductionIntracellularPhotoreceptor Cells VertebrateProgress in retinal and eye research
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Calcium-Dependent Assembly of Centrin-G-Protein Complex in Photoreceptor Cells

2002

Photoexcitation of rhodopsin activates a heterotrimeric G-protein cascade leading to cyclic GMP hydrolysis in vertebrate photoreceptors. Light-induced exchanges of the visual G-protein transducin between the outer and inner segment of rod photoreceptors occur through the narrow connecting cilium. Here we demonstrate that transducin colocalizes with the Ca(2+)-binding protein centrin 1 in a specific domain of this cilium. Coimmunoprecipitation, centrifugation, centrin overlay, size exclusion chromatography, and kinetic light-scattering experiments indicate that Ca(2+)-activated centrin 1 binds with high affinity and specificity to transducin. The assembly of centrin-G-protein complex is medi…

Lightgenetic structuresChromosomal Proteins Non-HistoneMacromolecular SubstancesImmunoprecipitationG proteinCentrifugationPlasma protein bindingBiologyRetinaSubstrate SpecificityRats Sprague-DawleyMiceHeterotrimeric G proteinCalcium-binding proteinAnimalsScattering RadiationTransducinMicroscopy ImmunoelectronCell Growth and DevelopmentMolecular BiologyCalcium-Binding ProteinsCell BiologyHeterotrimeric GTP-Binding ProteinsPrecipitin TestsRatsCell biologyMice Inbred C57BLMolecular WeightRhodopsinCentrinChromatography Gelbiology.proteinCalciumCattlesense organsTransducinPhotoreceptor Cells VertebrateProtein BindingSignal TransductionMolecular and Cellular Biology
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Patient centring and scan length: how inaccurate practice impacts on radiation dose in CT colonography (CTC).

2019

Objective: The aim of this study was to acknowledge errors in patients positioning in CT colonography (CTC) and their effect in radiation exposure. Materials and methods: CTC studies of a total of 199 patients coming from two different referral hospitals were retrospectively reviewed. Two parameters have been considered for the analysis: patient position in relation to gantry isocentre and scan length related to the area of interest. CTDI vol and DLP were extracted for each patient. In order to evaluate the estimated effective total dose and the dose to various organs, we used the CT-EXPO ® software version 2.2. This software provides estimates of effective dose and doses to the other vario…

MaleRadiology Nuclear Medicine and ImagingSupine positionTime FactorsEstimatedRadiotherapy Setup ErrorsRadiation DosageEffective dose (radiation)Patient Positioning030218 nuclear medicine & medical imagingCentringCohort Studies03 medical and health sciences0302 clinical medicineCT colonography; CTC; estimated; isocentre; positioning; scan length; radiology; nuclear nedicine and imagingnuclear nedicine and imagingCT colonographyProne PositionSupine PositionMedicineHumansIn patientAgedRetrospective StudiesMedical Errorsbusiness.industryUltrasoundRadiation doseAnal orificeScan lengthGeneral MedicineMiddle AgedRadiation ExposureCTCradiologyIsocentre030220 oncology & carcinogenesisTotal doseFemalebusinessNuclear medicineColonography Computed TomographicPositioningLa Radiologia medica
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Germline deletion of Cetn1 causes infertility in male mice

2013

Centrins are calmodulin-like Ca2+-binding proteins that can be found in all ciliated eukaryotic cells from yeast to mammals. Expressed in male germ cells and photoreceptors, centrin 1 (CETN1) resides in the photoreceptor transition zone and connecting cilium. To identify its function in mammals, we deleted Cetn1 by homologous recombination. Cetn1−/− mice were viable and showed no sign of retina degeneration suggesting that CETN1 is nonessential for photoreceptor ciliogenesis or structural maintenance. Phototransduction components localized normally to the Cetn1−/− photoreceptor outer segments, and loss of CETN1 had no effect on light-induced translocation of transducin to the inner segment.…

Maleendocrine systemLight Signal TransductionCentrioleChromosomal Proteins Non-HistoneSpermiogenesisBiologyMice03 medical and health sciencesRetinal Rod Photoreceptor CellsCiliogenesismedicineAnimalsBasal bodyTransducinSpermatogenesisGerm-Line MutationInfertility MaleCentriolesSequence Deletion030304 developmental biologyMice KnockoutGenetics0303 health sciencesSpermatidCalcium-Binding ProteinsCell Cycle030302 biochemistry & molecular biologyCell DifferentiationCell BiologySpermatidsCell biologyMice Inbred C57BLmedicine.anatomical_structureCentrinFemalesense organsTransducinResearch ArticleVisual phototransductionJournal of Cell Science
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Identification of Novel Molecular Components of the Photoreceptor Connecting Cilium by Immunoscreens

2002

Abstract The connecting cilium of photoreceptor cells is the only intracellular link between the morphologically, functionally and biochemically different compartments of the inner and outer segments. The non-motile modified cilium plays an important role in the organization and the function of photoreceptor cells, namely in delivery and turnover of enzymes and substrates of the visual transduction cascade, and the photosensitive membranes of the outer segment. The protein components of the cilium participate in the intracellular transport through the cilium, in the outer segment disk morphogenesis and in the maintenance of discrete membrane domains. In order to identify yet unknown cytoske…

Photoreceptor Connecting CiliumAdenomatous Polyposis Coli ProteinXenopus ProteinsBiologyPhotoreceptor cellRats Sprague-DawleyMiceCellular and Molecular NeurosciencemedicineAnimalsDrosophila ProteinsCiliaCloning MolecularCytoskeletonMicrotubule-Associated Protein 4CytoskeletonGene LibraryRetinaCiliumCalcium-Binding ProteinsDynactin ComplexSensory SystemsRatsCell biologyMice Inbred C57BLOphthalmologymedicine.anatomical_structureCentrinsense organsMicrotubule-Associated ProteinsPhotoreceptor Cells VertebrateVisual phototransductionExperimental Eye Research
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Insights into functional aspects of centrins from the structure of N-terminally extended mouse centrin 1

2006

AbstractCentrins are members of the family of Ca2+-binding EF-hand proteins. In photoreceptor cells, centrin isoform 1 is specifically localized in the non-motile cilium. This connecting cilium links the light-sensitive outer segment with the biosynthetic active inner segment of the photoreceptor cell. All intracellular exchanges between these compartments have to occur through this cilium. Three-dimensional structures of centrins from diverse organisms are known, showing that the EF-hand motifs of the N-terminal domains adopt closed conformations, while the C-terminal EF-hand motifs have open conformations. The crystal structure of an N-terminally extended mouse centrin 1 (MmCen1-L) resemb…

Protein ConformationAmino Acid MotifsSequence HomologyPlasma protein bindingEF-handTroponin CMiceStructure-Activity RelationshipProtein structureCalcium-binding proteinConnecting ciliumCentrinAnimalsHumansPhotoreceptor CellsCiliaEF Hand MotifsProtein Structure QuaternaryChemistryEF handCiliumCalcium-Binding ProteinsTerminal Repeat SequencesCalcium-binding proteinSensory SystemsProtein Structure TertiaryCell biologyOphthalmologyCentrinCalciumTransducinsense organsX-ray structureProtein BindingVision Research
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