Search results for "Tacrolimus Binding Proteins"

showing 4 items of 4 documents

Mitochondria during sea urchin oogenesis.

2017

SummarySea urchin represents an ideal model for studies on fertilization and early development, but the achievement of egg competence and mitochondrial behaviour during oogenesis remain to be enlightened. Oocytes of echinoid, such as sea urchin, unlike other echinoderms and other systems, complete meiotic maturation before fertilization. Mitochondria, the powerhouse of eukaryotic cells, contain a multi-copy of the maternally inherited genome, and are involved directly at several levels in the reproductive processes, as their functional status influences the quality of oocytes and contributes to fertilization and embryogenesis. In the present paper, we report our latest data on mitochondrial…

0301 basic medicineMitochondrial DNAEmbryo NonmammalianMitoTrackerHsp56MitochondrionOogenesisDNA MitochondrialParacentrotus lividusOxidative PhosphorylationTacrolimus Binding Proteins03 medical and health sciencesOogenesisMeiosisbiology.animalPicoGreenAnimalsConfocal laser scanning microscopySettore BIO/06 - Anatomia Comparata E CitologiaSea urchinGerminal vesiclebiologymtDNAAnatomyCell Biologybiology.organism_classificationCell biologyMitochondria030104 developmental biologySea UrchinsOocytesFemaleDevelopmental biologyDevelopmental BiologyZygote (Cambridge, England)
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Suppression of allograft rejection in the sponge Suberites domuncula by FK506 and expression of genes encoding FK506-binding proteins in allografts.

2001

SUMMARY Porifera (sponges) are, evolutionarily, the oldest metazoan phylum. Recent molecular data suggest that these animals possess molecules similar to and homologous with those of the innate and adaptive immune systems of higher Metazoa. Applying the biological system of parabiosis and the technique of differential display of mRNA, two cDNAs encoding putative FK506-binding proteins were isolated. FK506 is successfully used in clinics as a drug to prevent allograft rejection and is toxic to Suberites domuncula cells in vitro at doses above 100ng ml−1. Autograft fusion of transplants from S. domuncula was not affected by FK506. Allograft non-fusion was not affected by FK506 at toxic doses;…

Graft RejectionDNA ComplementaryPhysiologyParabiosisMolecular Sequence DataGene ExpressionSequence HomologyAquatic SciencePolymerase Chain ReactionTacrolimusTacrolimus Binding ProteinsImmune systempolycyclic compoundsHomologous chromosomeAnimalsTransplantation HomologousAmino Acid SequenceCloning MolecularMolecular BiologyGeneEcology Evolution Behavior and SystematicsGene LibraryMessenger RNADifferential displaybiologyAnatomybiology.organism_classificationIn vitroCell biologyPoriferaSuberites domunculaInsect ScienceAnimal Science and ZoologyThe Journal of experimental biology
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Localization of mitochondrial Hsp56 chaperonin during sea urchin development.

2001

We have previously demonstrated that Paracentrotus lividus nuclear genome encodes for the heat shock inducible chaperonin homolog Hsp 56 (1) and that the mature protein is localized in the mitochondrial matrix (2). In this paper we report that constitutive Hsp56 is maternally inherited, in fact it is present in the in unfertilized eggs, and that it has a perinuclear specific localization during cleavage. In the later stages both the constitutive and the heat shock inducible chaperonin has a specific territorial distribution. Moreover following heat shock, the Hsp56 appears in the cytoplasm and in the postmitochondrial supernatant beside the mitochondrial fraction.

Nuclear geneEmbryo NonmammalianBlotting WesternBiophysicsMitochondrionCell FractionationBiochemistryParacentrotus lividusChaperoninTacrolimus Binding Proteinsbiology.animalAnimalsMolecular BiologySea urchinbiologyCell Biologybiology.organism_classificationMolecular biologyImmunohistochemistryCell biologyMitochondriaMitochondrial matrixCytoplasmSea UrchinsHSP60Molecular ChaperonesBiochemical and biophysical research communications
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Hsp 56 mRNA in Paracentrotus lividus embryos binds to a mitochondrial protein

2007

We previously demonstrated that Paracentrotus lividus Hsp56 mitochondrial chaperonin is constitutively expressed during development, that it has a specific territorial distribution, both in normal and heat-shocked embryos, and that its amount increases after heat shock [Roccheri MC, Patti M, Agnello M, Gianguzza F, Carra E, Rinaldi AM. Localization of mitochondrial Hsp56 chaperonin during sea urchin development. Biochem Biophys Res Commun 2001;287:1093-98] and cadmium treatment [Roccheri MC, Agnello M, Boneventura R, Matranga V. Cadmium induces the expression of specific stress proteins in sea urchin embryos. Biochem Biophys Res Commun 2004;321:80-7]. In this study, we looked at Hsp56 mRNA …

chaperoninEmbryo NonmammaliancadmiumBiologyMitochondrionheat-shockParacentrotus lividusChaperoninMitochondrial ProteinsTacrolimus Binding Proteinsbiology.animalOrganelleAnimalsRNA MessengerSea urchinMessenger RNANuclease protection assayembryo developmentCell BiologyGeneral Medicinebiology.organism_classificationMolecular biologymitochondriaGene Expression RegulationParacentrotusBacterial outer membraneHeat-Shock Response
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