0000000000560486

AUTHOR

Cinzia Chinnici

0000-0001-9318-6606

showing 4 related works from this author

Phenoloxidases in ascidian hemocytes: characterization of the pro-phenoloxidase activating system.

2003

The phenoloxidase (PO) activity of the hemocytes lysate supernatant from three ascidians species, assayed by means of 3-methyl-2-benzothiazolinone hydrazone hydrochloride, have been compared. PO-containing hemocytes were identified by a cytochemical reaction and the enzymatic activity measured by a spectrophotometric assay of lysate supernatant from hemocyte populations separated on a discontinuous Percoll density gradient. In Styela plicata, the enzyme appeared to be contained in morula cells only. In Ciona intestinalis, PO activity was shown in univacuolar refractile granulocyte and granular hemocyte. In Phallusia mammillata both compartment cell and granular hemocytes were positive. Enzy…

LysisHemocytesCiona intestinaliCell separationPhysiologySettore BIO/05 - ZoologiaHemocyteBiologyTunicateBiochemistryEnzyme activatormedicineAnimalsCiona intestinalisPhallusia mammillataBenzothiazolesUrochordataMolecular BiologyPolyacrylamide gel electrophoresischemistry.chemical_classificationMonophenol MonooxygenaseImmunityHydrazonesTrypsinbiology.organism_classificationMolecular biologyEnzyme ActivationThiazolesEnzymeStyela plicatachemistryStyela plicataPhenoloxidasePercollmedicine.drugComparative biochemistry and physiology. Part B, Biochemistrymolecular biology
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Identification of Type I and IX Collagens in the Ascidian Ciona intestinalis

2001

Immunohistochemical methods showed that a type I collagen is a component of the tunic of Ciona intestinalis, involved in the encapsulation process. Since the fibril-forming collagen types are characterized by triple helical domain with a highly preserved Gly-Xaa-Yaa repeated sequence, a probe coding the fibril-forming type I collagen of the echinoderm Paracentrotus lividus was used to identify ascidian cDNA clones. Northern blot hybridization established that P. lividus probe cross-hybridizes with a 6 Kb C. intestinalis mRNA isolated from the pharynx. Using the echinodermal type I collagen cDNA as a probe several positive clones were identified. Analysis of sequence and the deduced amino ac…

chemistry.chemical_classificationbiologychemistryComplementary DNACiona intestinalisNorthern blotbiology.organism_classificationRepeated sequenceMolecular biologyHomology (biology)Paracentrotus lividusType I collagenAmino acid
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CiC3-1a-Mediated Chemotaxis in the Deuterostome Invertebrate Ciona intestinalis (Urochordata)

2003

Abstract Deuterostome invertebrates possess complement genes, and in limited instances complement-mediated functions have been reported in these organisms. However, the organization of the complement pathway(s), as well as the functions exerted by the cloned gene products, are largely unknown. To address the issue of the presence of an inflammatory pathway in ascidians, we expressed in Escherichia coli the fragment of Ciona intestinalis C3-1 corresponding to mammalian complement C3a (rCiC3-1a) and assessed its chemotactic activity on C. intestinalis hemocytes. We found that the migration of C. intestinalis hemocytes toward rCiC3-1a was dose dependent, peaking at 500 nM, and was specific for…

Lipopolysaccharidescomplement system ascidiansHemocytesMolecular Sequence DataIn situ hybridizationPertussis toxinimmunologyHemolymphEscherichia coliAnimalsImmunology and AllergyCiona intestinalisAmino Acid SequencePeptide sequenceinnate immunityInflammationCell-Free SystemChemotactic FactorsbiologyImmune SeraRiboprobeChemotaxisAnatomybiology.organism_classificationRecombinant ProteinsComplement systemCell biologyCiona intestinalisChemotaxis LeukocyteHemocyte migrationPertussis ToxinCell Migration InhibitionComplement C3a
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A serum fucolectin isolated and characterized from sea bass Dicentrarchus labrax

2001

A lectin specific for fucose and galactose was isolated by affinity chromatography on Sepharose CL-6B from the serum of Dicentrarchus labrax. The hemagglutinating activity against rabbit erythrocytes was calcium-independent, and reached its maximum at 37 degrees C. Two protein components were found in the hemagglutinating fractions eluted from the Sepharose column. Only the 34 kDa component (DLL2) eluted from the polyacrylamide gels (SDS-PAGE) showed agglutinating activity against rabbit erythrocytes. SDS-PAGE, in non-reducing conditions, revealed a single 66 kDa protein that reacted with antibodies to the 34 kDa component. Therefore, a dimeric structure stabilized by disulfide bonds can be…

SerumImmunoblottingCarbohydratesSettore BIO/05 - ZoologiaBiophysicsHemagglutinin (influenza)CentrifugationBiochemistryFucoseSepharosechemistry.chemical_compoundAffinity chromatographyLectinsAnimalsDicentrarchus labraxHemagglutininSea bassMolecular BiologybiologyLectinHemagglutination Testsbiology.organism_classificationFishchemistryBiochemistryGalactosebiology.proteinBassElectrophoresis Polyacrylamide GelDicentrarchusFucolectinBiochimica et Biophysica Acta (BBA) - General Subjects
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