0000000000210520

AUTHOR

D. Cascino

showing 10 related works from this author

Sea Urchin Mitochondrial Matrix Contains a 56-kDa Chaperonine-like Protein

1997

Abstract Paracentrotus lividus mitochondrial matrix contains a constitutive hsp of 56-KDa which cross reacts with a serum anti-hsp-60 chaperonine from yeast mitochondria. The localization of hsps preexisting or newly synthesized in different subcellular fractions of gastrula embryos is also analyzed by two-dimensional electrophoresis.

animal structuresChaperoninsBlotting WesternBiophysicsMitochondrionBiochemistryParacentrotus lividusbiology.animalAnimalsElectrophoresis Gel Two-DimensionalImmunoelectrophoresisMolecular BiologySea urchinbiologyEmbryoCell Biologybiology.organism_classificationMolecular biologyYeastMitochondriaGastrulationBiochemistryMitochondrial matrixSea Urchinsbiological sciencesembryonic structuresBiochemical and Biophysical Research Communications
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Achievement of thermotolerance through hsps phosphorylation in sea urchin embryos.

1995

TPA treatment of sea urchin embryos is able to induce thermotolerance. Evidence is provided that TPA treatment induces phosphorylation of a constitutive stress protein of 38 KDa.

animal structuresHot Temperatureintegumentary systemTrough (geology)Cell BiologyGeneral MedicineSea urchin embryoBiologyCell biologySea Urchinsembryonic structuresBotanyPhosphorylationAnimalsTetradecanoylphorbol AcetateElectrophoresis Gel Two-DimensionalFemalePhosphorylationHeat-Shock ProteinsBody Temperature RegulationCell biology international
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Constitutive hsp70 is essential to mitosis during early cleavage of Paracentrotus lividus embryos: The blockage of constitutive hsp70 impairs mitosis

1999

Localization of constitutive hsp70 in eggs and early embryos of sea urchin Paracentrotus lividus is shown by means of in situ immunostaining. An accumulation of this protein is shown in the mitotic structures (asters, spindles and centrosomes). Microinjection of anti-hsp70 antibodies into eggs causes impairment of formation of mitotic structures and of cell division. This impairment goes from a complete mitotic block, to irregular mitotic apparatus formation with irregular cleavage, depending upon the antibody concentration. The localization of hsp70 after antibody microinjection is also described. Blockage of mitotic apparatus formation by nocodazole also blocks the concentration of hsp70 …

Time FactorsGrowth InhibitorMicroinjectionsCell divisionTime FactorSea UrchinCleavage Stage OvumBiophysicsMitosisCleavage (embryo)BiochemistryParacentrotus lividuschemistry.chemical_compoundbiology.animalAnimalsHSP70 Heat-Shock ProteinsSea urchin embryoMitosisMicroinjectionSea urchinMolecular BiologyConstitutive hsp70HSP70 Heat-Shock ProteinbiologyDose-Response Relationship DrugAnimalNocodazoleCell Biologybiology.organism_classificationMitosiGrowth InhibitorsMicroinjectionCell biologyNocodazolechemistryBiophysicCentrosomeSea UrchinsFertilizationembryonic structures
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Identification and characterization of a constitutive HSP75 in sea urchin embryos.

1997

Abstract An antiserum against a hsp of the 70-kDa family was prepared, by means of a fusion protein, which was able to detect a constitutive 75-kDa hsc in the sea urchinP. lividus.This hsc was present both during oogenesis and at all developmental stages. A two-dimensional electrophoresis has revealed four isolectric forms of this 75-kDa hsc. The amino acid sequence of the fragment used to prepare the anti-hsp70 antibodies revealed a 43% identity with the corresponding part of sea urchin sperm receptor, and in mature eggs a brighter immunofluorescence was seen all around the cell cortex where the receptor for sea urchin sperm is localized. In oocytes the hsp75 was localized in the cytoplasm…

MaleCytoplasmEmbryo NonmammalianRecombinant Fusion ProteinsBlotting WesternMolecular Sequence DataBiophysicsEmbryonic DevelopmentReceptors Cell SurfaceHSP sea urchin embryosBiologyBiochemistryOogenesisbiology.animalCell cortexAnimalsHSP70 Heat-Shock ProteinsAmino Acid SequenceIsoelectric PointeducationMolecular BiologySea urchinPeptide sequenceeducation.field_of_studySequence Homology Amino AcidOvaryEmbryoCell BiologySperm receptorImmunohistochemistrySpermatozoaMolecular biologySpermFusion proteinMolecular WeightGastrulationSea UrchinsOocytesElectrophoresis Polyacrylamide GelFemalePlasmids
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Sea urchin HSF activity in vitro and in transgenic embryos.

1997

Evidence is provided for the presence at the physiological temperature of 20 degrees C of a heat shock transcriptor factor, HSF, in the nuclei of P.lividus embryos. This HSF is able to specifically bind in vitro the heat shock element, HSE, of the promoter of the hsp70 gene i.v., as suggested by DNA-protein binding reactions and DNAse I protection assays. Upon heat-shock, at the temperature of 31 degrees C, its ability to bind the HSE units becomes much higher. The HSF activated by heat-shock drives in vivo the transcription of the beta-galactosidase reporter gene in transgenic sea urchin gastrulae. An ATF-like transcription factor, widely described in other organisms but not at all in sea …

Embryo NonmammalianHot TemperatureSea UrchinTranscription FactorTransgeneRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsTransfectionBiochemistryAnimals Genetically ModifiedTranscription (biology)Genes Reporterbiology.animalHeat shock proteinAnimalsHSP70 Heat-Shock ProteinsCell NucleuPromoter Regions GeneticMolecular BiologySea urchinTranscription factorHeat-Shock ProteinsCell NucleusHSP70 Heat-Shock ProteinReporter genebiologyBase SequenceAnimalTemperatureHeat-Shock ProteinPromoterCell BiologyGastrulabeta-GalactosidaseMolecular biologyCell biologyHsp70BiophysicSea UrchinsRecombinant Fusion ProteinTranscription FactorsBiochemical and biophysical research communications
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Deciliation: A stressful event for Paracentrotus lividus embryos.

1998

In this report, by using mono- and two-dimensional electrophoretic analysis, we demonstrate that deciliation on sea urchin embryos induces a stress response. Deciliation indeed causes not only the activation of ciliary subroutine, but also a transient decrease of bulk protein synthesis. This decrease is in agreement with our previous results on heat shock response in sea urchin, although deciliation does not induce the expression of the same main hsp set. We were able to characterize one main deciliation-stress protein of 40 kDa whose expression is transiently induced by deciliation and whose localisation is likely to be nuclear.

CytoplasmEmbryo NonmammalianBiophysicsBiochemistryParacentrotus lividusFight-or-flight responseMethionineStress Physiologicalbiology.animalProtein biosynthesisAnimalsRegenerationElectrophoresis Gel Two-DimensionalCiliaHeat shockMolecular BiologySea urchinCell NucleusSaline Solution HypertonicbiologyProteinsEmbryoCell BiologyGastrulaSea urchin embryobiology.organism_classificationMolecular biologyCell biologyProtein BiosynthesisSea UrchinsElectrophoresis Polyacrylamide GelBiochemical and biophysical research communications
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Apoptosis in sea urchin embryos.

1997

Abstract It is demonstrated by DNA electrophoresis analysis, morphological observations and TdT in situ reaction, that Paracentrotus embryos if treated with TPA plus heat undergo an apoptotic reaction. Indication is also obtained that non treated embryos undergo spontaneous apoptosis at the early pluteus stage, expecially in the districts of arms and intestine. The possible meaning of this latter observation is discussed.

animal structuresfood.ingredientEmbryo NonmammalianGel electrophoresis of nucleic acidsBiophysicsApoptosisDNA FragmentationBiologySpontaneous apoptosisBiochemistryfoodParacentrotusAnimalsPluteusMolecular BiologyEmbryonic InductionIn situ reactionEmbryoCell BiologyAnatomyGastrulaSea urchin embryobiology.organism_classificationCell biologyApoptosisSea Urchinsembryonic structuresTetradecanoylphorbol AcetateBiochemical and biophysical research communications
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EFFECT OF THE IMPase INHIBITOR L690,330 ON SEA URCHIN DEVELOPMENT

1998

Abstract A variety of concentrations of the IMPase inhibitor L690,330 were added to sea urchin embryos. Immediate arrest of development was obtained for concentrations from 7.5 m m on. Concentrations lower than 3.5 m m permitted gastrulation but inhibited skeletogenesis and disturbed elongation along the animal–vegetal axis. The latter results are similar to those obtained by counteracting lithium effect with myoinositol, which are suggested to be due to partial relief of IMPase inhibition.

Embryo NonmammalianSea UrchinCalcium-Calmodulin-Dependent Protein KinaseLithiumMorulaGlycogen Synthase Kinase 3biology.animalMorphogenesisEnzyme InhibitorMorphogenesiAnimalsIMPaseEnzyme InhibitorsSea urchin embryo5'-NucleotidaseSea urchinDiphosphonatesbiologyAnimalAbnormalities Drug-InducedCell BiologyGeneral MedicineAnatomySea urchin embryoCell biologyGastrulationDiphosphonateSea UrchinsCalcium-Calmodulin-Dependent Protein KinasesElongationLithium ChlorideInositolCell Biology International
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Myo-inositol counteracts the vegetalizing effect of lithium on P.lividus embryos

1992

Abstract The vegetalizing effect of LiCl on sea urchins embryos can be counteracted by the addition of myo-inositol. This observation is discussed in connection with similar results recently reported for amphibian embryos.

animal structuresbiologyLithium (medication)Embryogenesisfood and beveragesEmbryoCell Biologybiology.organism_classificationParacentrotus lividusTeratologyCell biologychemistry.chemical_compoundBiochemistryAmphibian embryosMechanism of actionchemistryembryonic structuresmedicineInositolmedicine.symptommedicine.drugCell Biology International Reports
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A constitutive 70 kDa heat-shock protein is localized on the fibres of spindles and asters at metaphase in an ATP-dependent manner: A new chaperone r…

2001

In the present study, double immunofluorescence and immunoblot analysis have been used to show that centrosomes, isolated from Paracentrotus lividus sea urchin embryos at the first mitotic metaphase, contain the constitutive chaperone, heat-shock protein (HSP) 70. More specifically, we demonstrate that centrosomes contain only the HSP70-d isoform, which is one of the four isoforms identified in P. lividus . We also provide evidence that p34(cell division control kinase-2) and t complex polypeptide-1 (TCP-1) α, a subunit of the TCP-1 complex, are localized on the centrosomes. Furthermore, inhibition of TCP-1 in vivo, via microinjecting an anti-(TCP-1α) antibody into P. lividus eggs before fe…

Constitutive HSP70Chaperone activityParacentrotus lividus sea urchinCell BiologyMitosiBiochemistryMolecular Biology
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