0000000000335849

AUTHOR

Daniele P. Romancino

0000-0003-2041-0122

showing 11 related works from this author

Spatial distribution of two maternal messengers encoding two sea urchin cell surface proteins

1993

We have localized, byin situ hybridization, two messengers, called bepl and bep4 (butanol extracted proteins), coding for cell surface proteins, involved in cell interaction, in sections of eggs of the sea urchinP. lividus. These maternal RNAs are spatially distributed in a gradient with a maximum at one pole of the egg. These results represent the first demonstration of the existence of a gradient of informational molecules in the sea urchin egg,i.e., the biological material for which the gradient theory was first proposed.

Polarity (international relations)biologyEcologyCell Surface ProteinsIn situ hybridizationSpatial distributionBiological materialsCell biologybiology.animalembryonic structuresGeneral Earth and Planetary SciencesGradient theoryGeneral Agricultural and Biological SciencesSea urchinGeneral Environmental ScienceRendiconti Lincei
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Palmitoylation is a post-translational modification of Alix regulating the membrane organization of exosome-like small extracellular vesicles.

2018

Abstract Background Virtually all cell types have the capacity to secrete nanometer-sized extracellular vesicles, which have emerged in recent years as potent signal transducers and cell-cell communicators. The multifunctional protein Alix is a bona fide exosomal regulator and skeletal muscle cells can release Alix-positive nano-sized extracellular vesicles, offering a new paradigm for understanding how myofibers communicate within skeletal muscle and with other organs. S-palmitoylation is a reversible lipid post-translational modification, involved in different biological processes, such as the trafficking of membrane proteins, achievement of stable protein conformations, and stabilization…

0301 basic medicineAlix (also known as PDCD6IP)Protein ConformationLipoylationLipid BilayersBiophysicsSkeletal muscle cellsCell Cycle ProteinsExosomesBiochemistryExosomeTetraspanin 29Cell Line03 medical and health sciencesExtracellular VesiclesPalmitoylationTetraspaninExtracellularHumansLipid bilayerMuscle SkeletalMolecular BiologyCells CulturedEndosomal Sorting Complexes Required for TransportChemistryVesicleCalcium-Binding ProteinsCell MembraneExtracellular vesicleTetraspaninSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Cell biologyExosomeProtein Transport030104 developmental biologyS-palmitoylationMembrane proteinextracellular vesicles (EVs)Skeletal muscle cellProtein Processing Post-TranslationalProtein BindingSignal TransductionBiochimica et biophysica acta. General subjects
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Identification and characterization of the nano-sized vesicles released by muscle cells

2013

AbstractSeveral cell types secrete small membranous vesicles that contain cell-specific collections of proteins, lipids, and genetic material. The function of these vesicles is to allow cell-to-cell signaling and the horizontal transfer of their cargo molecules. Here, we demonstrate that muscle cells secrete nano-sized vesicles and that their release increases during muscle differentiation. Analysis of these nanovesicles allowed us to characterize them as exosome-like particles and to define the potential role of the multifunctional protein Alix in their biogenesis.

Cell typeCellular differentiationBiophysicsBiologyExosomesBiochemistryExosomeExosome; Nanovesicle; Alix; Ozz-E3 ubiquitin ligase; Muscle cellArticleCell Line03 medical and health sciencesMice0302 clinical medicineOzz-E3 ubiquitin ligaseStructural BiologyGeneticsMyocyteAnimalsSecretionMolecular Biology030304 developmental biology0303 health sciencesMuscle CellsSettore BIO/16 - Anatomia UmanaVesicleCalcium-Binding ProteinsCell MembraneMuscle cellCell DifferentiationCell BiologyCell biologyNanostructuresExosomeAlixCell culture030220 oncology & carcinogenesisNanovesicleBiogenesisFEBS Letters
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Identification and characterization of PlAlix, the Alix homologue from the Mediterranean sea urchin Paracentrotus lividus.

2013

The sea urchin provides a relatively simple and tractable system for analyzing the early stages of embryo development. Here, we use the sea urchin species, Paracentrotus lividus, to investigate the role of Alix in key stages of embryogenesis, namely the egg fertilization and the first cleavage division. Alix is a multifunctional protein involved in different cellular processes including endocytic membrane trafficking, filamentous (F)-actin remodeling, and cytokinesis. Alix homologues have been identified in different metazoans; in these organisms, Alix is involved in oogenesis and in determination/differentiation events during embryo development. Herein, we describe the identification of th…

MaleBlastomeresanimal structuresDNA ComplementaryEmbryo Nonmammalian2-cell stage embryo; Alix/AIP1; F-actin; sea urchin embryoBlotting WesternMolecular Sequence DataParacentrotus lividusF-actinbiology.animalBotany2-cell stage embryoMediterranean SeaAnimalsAmino Acid SequenceCloning MolecularSea urchinPeptide sequenceActinsea urchin embryoMicroscopy ConfocalbiologySequence Homology Amino AcidReverse Transcriptase Polymerase Chain ReactionEmbryogenesisMicrofilament ProteinsGene Expression Regulation DevelopmentalEmbryoCell BiologySequence Analysis DNAbiology.organism_classificationAlix/AIP1Cell biologyCytoplasmFertilizationembryonic structuresParacentrotusFemaleCytokinesisDevelopmental Biology
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Identification of an Antigen Related to the Sea Urchin RNA-Binding Protein LP54 in Mammalian Central Nervous System

2001

LP54 is an RNA-binding protein involved in localization of maternal messengers in sea urchin egg and embryos. Using a polyclonal antibody directed against Paracentrotus lividus LP54 we detected a 66-kDa cross-reacting antigen in undifferentiated and differentiated SH-SY5Y human neuroblastoma cells. After treatment of undifferentiated cells with detergent, the 66-kDa antigen was found to be enriched in the cytoskeletal fraction. By Western blot the expression of this antigen was also analyzed in regions of the CNS and in tissues of the adult rat and its exclusive presence in the hippocampus and thalamus was revealed. The immunoreactivity with P. lividus antibody against LP54 in hippocampal l…

Central Nervous SystemRNA localizationOctoxynolBlotting WesternDetergentsRNA-binding proteinBinding CompetitiveHippocampusParacentrotus lividusThalamusWestern blotAntigenbiology.animalTumor Cells CulturedmedicineAnimalsHumansRNA MessengerMolecular BiologySea urchinCytoskeletonbiologymedicine.diagnostic_testRNA-Binding ProteinsCell Differentiationbiology.organism_classificationMolecular biologyRatsMicroscopy FluorescencePolyclonal antibodiesSea Urchinsbiology.proteinElectrophoresis Polyacrylamide GelAntibodyMicrotubule-Associated ProteinsMolecular Cell Biology Research Communications
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Centrifugation does not alter spatial distribution of `BEP4' mRNA in paracentrotus lividus EGG

1997

AbstractParacentrotus lividus unfertilized eggs were centrifuged in a sucrose gradient, so to split each into two parts: a nucleated light fragment and an anucleated heavy fragment. Northern blot analyses utilizing a bep4 probe as animal marker and H2A histone gene and 12S-mit RNA as controls indicate that the eggs are elongated along the animal-vegetal axis during centrifugation and thereafter split into an animal and a vegetal half. Treatment of the eggs with colchicine before centrifugation abolishes the animal localization of bep4 mRNA.

Localized mRNABiophysicsCentrifugationCell FractionationBiochemistryMicrotubulesParacentrotus lividuschemistry.chemical_compoundStructural BiologyBotanyA/V axisGeneticsCentrifugation Density GradientColchicineAnimalsCentrifugationNorthern blotRNA MessengerMolecular BiologyGeneIn Situ HybridizationOvumMessenger RNAbiologyUnfertilized EggsRNACell PolarityMembrane ProteinsCell Biologybiology.organism_classificationBlotting NorthernMolecular biologychemistrySea Urchinsembryonic structuresCortexColchicineFEBS Letters
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“BEP” RNAs and Proteins Are Situated in the Animal Side of Sea Urchin Unfertilized Egg, Which Can Be Recognized by Female Pronuclear Localization

1996

Microsurgery experiments demonstrate that the animal side of the unfertilized sea urchin Paracentrotus lividus egg coincides with the side of the egg pronucleus location. It is demonstrated by means of in situ hybridization and immunostaining of whole mounts of animal or vegetal halves that the previously identified bep 1 and bep4 RNAs and their proteins are located in the animal part of the unfertilized egg and much less in the vegetal part. The addition of Fabs against BEP1 and BEP4 causes exogastrulation.

BiophysicsIn situ hybridizationBiochemistryParacentrotus lividusbiology.animalBotanyMorphogenesismedicineAnimalsRNA MessengerMolecular BiologySea urchinOvumCell NucleusbiologyPronucleusMembrane ProteinsRNACell Biologybiology.organism_classificationCell biologyCell nucleusmedicine.anatomical_structureMembrane proteinSea Urchinsembryonic structuresRNAFemaleImmunostainingBiochemical and Biophysical Research Communications
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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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Characterization of bep1 and bep4 antigens involved in cell interactions during Paracentrotus lividus development

1992

Abstract We have identified and partially characterised two antigens, extracted with 3% butanol, from Paracentrotus lividus embryos dissociated at the blastula stage, and encoded by the cDNA clones previously described as bep1 and bep4 (bep-butanol extracted proteins). The cDNA fragments containing the specific central portions of bep1 and bep4 were expressed as MS2 polymerase fusion proteins in Escherichia coli. These two fusion proteins, called 1C1 (bep1) and 4A1 (bep4), were injected subcutaneously into rabbits and the corresponding polyclonal antibodies generated. Western blot analysis of proteins, extracted with 3% butanol, from sea urchin embryos at the blastula stage (b.e.p.), establ…

Cancer ResearchEmbryo Nonmammaliananimal structuresRecombinant Fusion ProteinsEmbryonic DevelopmentFluorescent Antibody TechniqueParacentrotus lividusCell–cell interactionWestern blotComplementary DNAbiology.animalmedicineAnimalsMolecular BiologySea urchinCell Aggregationbiologymedicine.diagnostic_testMembrane ProteinsCell Biologybiology.organism_classificationBlastulaMolecular biologyFusion proteinPolyclonal antibodiesSea Urchinsembryonic structuresbiology.proteinDevelopmental BiologyDifferentiation
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EGFR signalling is required for Paracentrotus lividus endomesoderm specification

2008

The EGFR pathway is critical for cell fate specification throughout the development of several organisms. Here we identified in sea urchin an EGFR-related antigen maternally expressed and showing a dynamic pattern of localization during development. To investigate the role played by the EGFR in Paracentrotus lividus development we blocked its activity by using the EGFR kinase inhibitor AG1478. This treatment produces decrease of EGFR phosphorylation, and embryos with various defects especially in the endomesoderm territory until to obtain an animalized phenotype. These effects are rescued by the addition of TGF-alpha, an EGFR ligand. The role played by EGFR-like along the animal/vegetal axi…

Embryo NonmammalianMAP Kinase Signaling SystemBlotting WesternBiophysicsCell fate determinationBiochemistryParacentrotus lividusMesodermEndomesodermbiology.animalBotanyAnimalsCell LineageExtracellular Signal-Regulated MAP KinasesMolecular BiologySea urchinbiologyKinaseEndodermEmbryoTyrphostinsbiology.organism_classificationImmunohistochemistryPhenotypeCell biologyErbB ReceptorsParacentrotusQuinazolinesPhosphorylationEGFR sea urchin AlzheimerSignal TransductionArchives of Biochemistry and Biophysics
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Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface

2017

AbstractCell surface expression of alpha-enolase, a glycolytic enzyme displaying moonlighting activities, has been shown to contribute to the motility and invasiveness of cancer cells through the protein non-enzymatic function of binding plasminogen and enhancing plasmin formation. Although a few recent records indicate the involvement of protein partners in the localization of alpha-enolase to the plasma membrane, the cellular mechanisms underlying surface exposure remain largely elusive. Searching for novel interactors and signalling pathways, we used low-metastatic breast cancer cells, a doxorubicin-resistant counterpart and a non-tumourigenic mammary epithelial cell line. Here, we demon…

Lipopolysaccharides0301 basic medicineAlpha-enolaseScienceCellPlasma protein bindingArticle03 medical and health sciencesCell MovementEpidermal growth factorCell Line TumormedicineHumansHSP70 Heat-Shock ProteinsRegulation of gene expressionMultidisciplinarybiologyQCell MembraneR3. Good healthCell biologyGene Expression Regulation NeoplasticSettore BIO/18 - Genetica030104 developmental biologymedicine.anatomical_structurePhosphopyruvate HydrataseChaperone (protein)Cancer cellbiology.proteinMedicineEnolase Hsp70 protein cell surface cancer biologyIntracellularProtein Binding
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