Search results for "Galectins"

showing 10 items of 20 documents

Histochemical and electron microscopic analysis of spiculogenesis in the demosponge Suberites domuncula.

2006

The skeleton of demosponges is built of spicules consisting of biosilica. Using the primmorph system from Suberites domuncula, we demonstrate that silicatein, the biosilica-synthesizing enzyme, and silicase, the catabolic enzyme, are colocalized at the surface of growing spicules as well as in the axial filament located in the axial canal. It is assumed that these two enzymes are responsible for the deposition of biosilica. In search of additional potential structural molecules that might guide the mineralization process during spiculogenesis to species-specific spicules, electron microscopic studies with antibodies against galectin and silicatein were performed. These studies showed that …

HistologybiologyHistocytochemistryGalectinsMolecular Sequence DataFlagellumbiology.organism_classificationSilicon DioxideMineralization (biology)CathepsinsMicrobiologySilica depositionSuberites domunculaMicroscopy ElectronDemospongeSponge spiculeBiophysicsAnimalsAmino Acid SequenceCollagenAnatomySuberitesElectron microscopicGalectinThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
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Inducible lectins with galectin properties and human IL1alpha epitopes opsonize yeast during the inflammatory response of the ascidian Ciona intestin…

2007

Studies on inducible ascidian lectins may shed light on the evolutionary emergence of cytokine functions. Here, we show that the levels of opsonins, with IL1alpha-epitopes, increase in Ciona intestinalis hemolymph as a response to an inflammatory stimulus and, in particular, to intratunic injection of lipopolysaccharide (LPS). The inflammatory agent promptly (within 4 h) enhances Ca(2+)-independent serum hemagglutinating and opsonizing activities, which are both inhibited by D-galactose and D-galactosides (alpha-lactose, N-acetyl-D-lactosamine, thio-digalactoside), suggesting that anti-rabbit erythrocyte lectins with galectin properties are involved as opsonins. Inducible galectin molecules…

LipopolysaccharidesHistologyLipopolysaccharideGalectinsSaccharomyces cerevisiaeCross ReactionsEpitopeEvolution . Inflammatory response . Phagocytosis . Opsonins . Lectins . IL1α-like galectins . Ascidian Ciona intestinalis (Tunicata)AntibodiesPathology and Forensic Medicinelaw.inventionchemistry.chemical_compoundEpitopesWestern blotPhagocytosisOpsonin ProteinslawHemolymphInterleukin-1alphaLectinsmedicineAnimalsHumansCiona intestinalisGalectinbiologymedicine.diagnostic_testGalactoseGalactosidesCell BiologyBlood ProteinsOpsonin Proteinsbiology.organism_classificationMolecular biologyBlood proteinsRecombinant ProteinsCiona intestinalisHemagglutininsBiochemistrychemistryRecombinant DNACalciumRabbitsCell and tissue research
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Inducible galectins are expressed in the inflamed pharynx of the ascidian Ciona intestinalis

2011

Although ascidians belong to a key group in chordate phylogenesis, amino acid sequences of Ciona intestinalis galectin-CRDs (CiLgals-a and -b) have been retained too divergent from vertebrate galectins. In the present paper, to contribute in disclosing Bi-CRD galectin evolution a novel attempt was carried out on CiLgals-a and -b CRDs phylogenetic analysis, and their involvement in ascidian inflammatory responses was shown. CiLgals resulted aligned with Bi-CRD galectins from vertebrates (Xenopus tropicalis, Gallus gallus, Mus musculus, Homo sapiens), cephalochordates (Branchiostoma floridae), echinoderms (Strongylocentrotus purpuratus) and a mono-CRD galectin from the ascidian Clavelina pict…

LipopolysaccharidesModels Molecularanimal structuresHemocytesTime FactorsGalectinsBlotting WesternMolecular Sequence DataCiona intestinalis galectinsSettore BIO/05 - ZoologiaSequence alignmentChordateAquatic ScienceAdjuvants ImmunologicPhylogeneticsBranchiostoma floridaeEnvironmental ChemistryAnimalsCiona intestinalisAmino Acid SequencePeptide sequencePhylogenyGalectinbiologyGeneral MedicineAnatomybiology.organism_classificationMolecular biologyStrongylocentrotus purpuratuseye diseasesCiona intestinalisProtein Structure TertiaryUp-Regulationembryonic structuresPharynxSequence Alignment
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Ciona intestinalis galectin (CiLgals-a and CiLgals-b) genes are differentially expressed in endostyle zones and challenged by LPS

2015

Abstract Immunohistochemical and in situ hybridization assays were performed to answer the question whether the endostyle, that is the initial gastro-intestinal trait of Ciona intestinalis pharynx, is involved in galectin (CiLgals-a and CiLgals-b) production during the pharynx inflammatory response to LPS inoculation. Specific anti-CiLgal-a and anti-CiLgals-b antibodies, and oligonucleotide probes, that mark inflammatory hemocytes inside the pharynx vessels and vessel epithelium as shown by a previous paper, were assayed on endostyle histological sections. For the first time, we show that galectins are produced by endostyle zones, and both CiLgals-a and –b genes are upregulated by LPS. CiLg…

LipopolysaccharidesSignal peptideLPSAscidianGalectinsOligonucleotidesSettore BIO/05 - ZoologiaIn situ hybridizationAquatic ScienceBiologyendostyleDownregulation and upregulationotorhinolaryngologic diseasesmedicineExtracellularAnimalsEnvironmental ChemistryCiona intestinalisIn Situ HybridizationGalectinAscidian Galectin Endostyle Inflammation Ciona intestinalisgalectinGeneral Medicinebiology.organism_classificationImmunohistochemistryMolecular biologyEpitheliumCiona intestinalismedicine.anatomical_structureItalyinflammationImmunologyPharynxEndostyle
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Prognostic value of the interaction between galectin-3 and antigen carbohydrate 125 in acute heart failure

2015

AIM:Galectin-3 (Gal-3) and carbohydrate antigen 125 (CA125) have emerged as robust prognostic biomarkers in heart failure. Experimental data have also suggested a potential molecular interaction between CA125 and Gal-3; however, the biological and clinical relevance of this interaction is still uncertain. We sought to evaluate, in patients admitted for acute heart failure, the association between plasma Gal-3 with all-cause mortality and the risk for rehospitalizations among high and low levels of CA125. METHODS AND RESULTS: We included 264 consecutive patients admitted for acute heart failure to the Cardiology Department in a third-level center. Both biomarkers were measured on admission. …

Maleendocrine system diseasesGalectin 3lcsh:MedicineRisk FactorsBlood plasmaANTIGEN CARBOHYDRATE 125lcsh:ScienceAged 80 and overMultidisciplinaryca125Mortality rateBlood Proteins//purl.org/becyt/ford/3.1 [https]Middle AgedPrognosisMedicina BásicaGalectin-3Female//purl.org/becyt/ford/3 [https]Research Articlemedicine.medical_specialtyCIENCIAS MÉDICAS Y DE LA SALUDcontributesGalectinsInmunologíaPatient ReadmissionAntigenInternal medicinemedicineHumanssurfaceClinical significanceIn patientIntensive care medicineAgedProportional Hazards ModelsHeart FailureGALECTIN-3business.industryProportional hazards modellcsh:Rassociationmedicine.diseaseACUTE HEART FAILUREstatin therapyinflammationCA-125 AntigenHeart failurecellslcsh:QbusinessBiomarkersFollow-Up Studies
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Molecular evolution: Evidence for the monophyletic origin of multicellular animals

1995

Multicellular animalsGalectinsMolecular Sequence DataEukaryotaProteinsZoologyGeneral MedicineBiologyBiological EvolutionInvertebratesPoriferaMonophylyHemagglutininsEvolutionary biologyMolecular evolutionVertebratesAnimalsAmino Acid SequencePhylogenyEcology Evolution Behavior and SystematicsNaturwissenschaften
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Human CD4+CD25+ regulatory T cells: proteome analysis identifies galectin-10 as a novel marker essential for their anergy and suppressive function.

2007

AbstractCD4+CD25+Foxp3+ regulatory T cells (CD25+ Treg cells) direct the maintenance of immunological self-tolerance by active suppression of autoaggressive T-cell populations. However, the molecules mediating the anergic state and regulatory function of CD25+ Treg cells are still elusive. Using differential proteomics, we identified galectin-10, a member of the lectin family, as constitutively expressed in human CD25+ Treg cells, while they are nearly absent in resting and activated CD4+ T cells. These data were confirmed on the mRNA and protein levels. Single-cell staining and flow cytometry showed a strictly intracellular expression of galectin-10 in CD25+ Treg cells. Specific inhibition…

ProteomeGalectinsImmunologychemical and pharmacologic phenomenaBiologyBiochemistryT-Lymphocytes RegulatoryFlow cytometrymedicineHumansIL-2 receptorCells CulturedGalectinCell ProliferationClonal AnergyMessenger RNAmedicine.diagnostic_testFOXP3Antibodies Monoclonalhemic and immune systemsForkhead Transcription FactorsCell BiologyHematologyCell biologySelf ToleranceGene Expression RegulationProteomeImmunologyIntracellularFunction (biology)BiomarkersBlood
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Proteomics of Galápagos Marine Iguanas Links Function of Femoral Gland Proteins to the Immune System

2020

Femoral glands secrete a wax-like substance on the inner side of lizard hind legs, which is thought to function as a mode of chemical communication. Though the minor volatile fraction is well studied, the major protein fraction remains enigmatic. Here, we use proteomics to analyze proteins in femoral gland secretions of the Galápagos marine iguana. Although we found no evidence for proteins and peptides involved in chemical communication, we found several immune-regulatory proteins which also demonstrate anti-microbial functions. Accordingly, we show that femoral gland proteins and peptides function as a barrier against microbial infection and may prevent the rapid degradation of volatile s…

ProteomicsProteomeProteomicsBiochemistryAnalytical ChemistryAnti-Infective AgentsTandem Mass Spectrometrydatabase designprotease inhibitor protein identificationLungSkin0303 health sciencesMuscles030302 biochemistry & molecular biologyBrainHigh-Throughput Nucleotide SequencingHeartBlood proteinsanimal modelsmarine iguanaBiochemistryOrgan SpecificityProteomeEcuadorBacillus subtilisPulmonary Surfactant-Associated ProteinsGalectinsAntileukoproteinaseBiologyprotease inhibitor03 medical and health sciencesproteomicsImmune systemfemoral glandsevolutionEndopeptidasesEscherichia coliAnimalsHumanstissuesMolecular Biology030304 developmental biologyGalectinInnate immune systemChemotactic FactorsResearchMyocardiumImmunity Innateimmune systemIguanasMuramidaseApoproteinsTranscriptomeFunction (biology)Molecular & Cellular Proteomics
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A galectin links the aggregation factor to cells in the sponge (Geodia cydonium) system.

1996

The cDNA for the full-length lectin from the marine sponge Geodia cydonium was cloned. Analysis of the deduced aa sequence revealed that this lectin belongs to the group of galectins. The full-length galectin, which was obtained also in a recombinant form, has an M(r) of 20,877; in the processed form it is a 15 kDa polypeptide. The enriched aggregation factor from G.cydonium also was determined to contain, besides minimal amounts of the galectin, a 140 kDa polypeptide which is involved in cell-cell adhesion. Monoclonal antibodies have been raised against this protein; Fab' fragments prepared from them abolished cell-cell reaggregation. Cell reaggregation experiments revealed that the aggreg…

animal structuresDNA Complementarymedicine.drug_classGalectinsCellMolecular Sequence DataMonoclonal antibodyBiochemistrylaw.inventionlawComplementary DNALectinsotorhinolaryngologic diseasesmedicineAnimalsAmino Acid SequenceCloning MolecularCell adhesionGalectinCell AggregationbiologyBase SequenceChemistryLectinAntibodies MonoclonalPoriferastomatognathic diseasesmedicine.anatomical_structureBiochemistrybiology.proteinRecombinant DNAAntibodyCell Adhesion MoleculesProtein BindingGlycobiology
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S-type lectins occur also in invertebrates: high conservation of the carbohydrate recognition domain in the lectin genes from the marine sponge Geodi…

1993

The marine sponge Geodia cydonium contains several lectins. The main component, called lectin-1, is composed of three to four identical subunits. The subunits of the lectins were cloned from a cDNA library; two clones were obtained. From the deduced aa sequence of one clone, LECT-1, a mol. wt of 15,313 Da is calculated; this value is in good agreement with mass spectrometric analysis of 15,453 +/- 25 Da. The sequence of another clone, LECT-2, was analysed and the aa sequence was deduced (15,433 Da). The two subunits have a framework sequence of 38 conserved aa which are characteristic for the carbohydrate-binding site of vertebrate S-type lectins. Clustering of lectin sequences of various s…

clone (Java method)GalectinsBlotting WesternMolecular Sequence DataBiochemistryChromatography AffinityMass SpectrometryLectinsAnimalsAmino Acid SequenceCloning MolecularPeptide sequenceGeneGalectinCloningbiologyBase SequencecDNA libraryLectinDNAbiology.organism_classificationPoriferaSuberites domunculaBiochemistrybiology.proteinElectrophoresis Polyacrylamide GelGlycobiology
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