Search results for "rites"

showing 10 items of 427 documents

Biologically-induced transition of bio-silica sol to mesoscopic gelatinous flocs: a biomimetic approach to a controlled fabrication of bio-silica str…

2012

Siliceous sponges form their skeletal elements, the spicules, enzymatically via the sponge-specific enzyme silicatein. The enzymatic product of silicatein in vitro is a bio-silica polymer that is not processed/hardened by phase separation. In the present study we applied a two-phase system to investigate the transition of bio-silica, formed by silicatein, from the lucid state to the opaque/turbid state. We report for the first time that the polyether polyethylene glycol [PEG] causes a rapid transition of the lucid bio-silica to the opaque/turbid state. For the experiments the recombinant silicatein from the demosponge Suberites domuncula had been used. This process is rapid (1 h) and procee…

chemistry.chemical_classification0303 health sciencesbiologyNanoparticle02 engineering and technologyGeneral ChemistryPolyethylene glycolPolymer021001 nanoscience & nanotechnologyCondensed Matter Physicsbiology.organism_classificationSuberites domuncula03 medical and health scienceschemistry.chemical_compoundSpongechemistryChemical engineeringPEG ratioMicroscopyOrganic chemistrySurface charge0210 nano-technology030304 developmental biologySoft Matter
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Silintaphin-1 - interaction with silicatein during structure-guiding bio-silica formation

2011

Silicateins are unique enzymes of sponges (phylum Porifera) that template and catalyze the polymerization of nanoscale silicate to siliceous skeletal elements. These multifunctional spicules are often elaborately shaped, with complex symmetries. They carry an axial proteinaceous filament, consisting of silicatein and the scaffold protein silintaphin-1, which guides silica deposition and subsequent spicular morphogenesis. In vivo, the synthesis of the axial filament very likely proceeds in three steps: (a) assembly of silicatein monomers to form one pentamer; (b) assembly of pentamers to form fractal-like structures; and finally (c) assembly of fractal-like structures to form filaments. The …

chemistry.chemical_classification0303 health sciencesbiologyStereochemistryPentamerSubstrate (chemistry)02 engineering and technologyCell BiologyPolymer021001 nanoscience & nanotechnologybiology.organism_classificationBiochemistryTetraethyl orthosilicateSuberites domunculaProtein filament03 medical and health scienceschemistry.chemical_compoundMonomerchemistryPolymerizationBiophysics0210 nano-technologyMolecular Biology030304 developmental biologyFEBS Journal
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Molecular/chemical ecology in sponges. Evidence for an adaptive antibacterial response in Suberites domuncola

2004

Sponges (Porifera) represent the evolutionary oldest metazoan phylum still extant today. They have developed a complex Bauplan, based on the existence of structural and regulatory molecules; many of these have been cloned and analyzed in the past years. The demosponge Suberites domuncula has been used as a suitable model to demonstrate that these animals not only possess an adaptive immune response on the level of cytokines, but also, as pointed out here, on the level of synthesis of bioactive alkyl-lipid derivatives. From specimens of S. domuncula the two lyso-PAF (platelet-activating factor) compounds, 1-O-hexadecyl-sn-glycero-3-phosphocholine and 1-O-octadecyl-sn-glycero-3-phosphocholine…

chemistry.chemical_classificationEcologyATP synthasebiologyAntibacterial ResponseAquatic Sciencebiology.organism_classificationAcquired immune systemMicrobiologySuberites domunculaSpongeEnzymeDemospongechemistryBiochemistrybiology.proteinlipids (amino acids peptides and proteins)Ecology Evolution Behavior and SystematicsFunction (biology)
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Biochemistry and cell biology of silica formation in sponges

2003

The main inorganic material forming the skeletal elements in Demospongiae as well as in Hexactinellida, the spicules, is amorphous silica. The spicules occur in the cytoplasm and the extracellular space and also in the nucleus (as silicate crystals) of some sponge cells; the function in the latter compartment is unknown. Recent evidence shows that the formation of spicules is mediated by the enzyme silicatein. The cDNA as well as the gene encoding this enzyme was cloned from Suberites domuncula. The recombinant silicatein catalyzes the syn- thesis of amorphous silicate using tetraethoxysilane as substrate. The enzyme is dependent on ferric iron. Silicatein also has proteolytic (cathepsin-li…

chemistry.chemical_classificationHistologyBiologybiology.organism_classificationSilicateCell biologySuberites domunculaMedical Laboratory Technologychemistry.chemical_compoundSpongeSponge spiculeEnzymechemistryBiochemistryCytoplasmGene expressionExtracellularAnatomyInstrumentationMicroscopy Research and Technique
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Synthesis of the neurotoxin quinolinic acid in apoptotic tissue from Suberites domuncula: cell biological, molecular biological and chemical analyses

2002

Sessile marine animals, such as sponges, are prone to infection by prokaryotic as well as by eukaryotic attacking organisms. In the present study we document for the first time that in tissue from sponges which underwent apoptosis, a toxic compound is produced which very likely controls the elimination of the dying tissue. The marine sponge Suberites domuncula develops in the field occasionally apoptotic tissue areas which are rapidly eliminated. In the present study apoptosis was induced in S. domuncula by exposing the specimens in aquaria to 5 µg/ml Dip or by maintaining the sponges for 3 - 5 days under non-aeration conditions. After that treatment only one eukaryotic epibiont, the mollus…

chemistry.chemical_classificationbiologyCell growthCellbiology.organism_classificationApplied Microbiology and BiotechnologyBioactive compoundMicrobiologySuberites domunculachemistry.chemical_compoundSpongemedicine.anatomical_structureEnzymechemistryBiochemistryApoptosismedicineQuinolinic acid
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Immediate early response of the marine sponge Suberites domuncula to heat stress: Reduction of trehalose and glutathione concentrations and glutathio…

1997

The marine sponge Suberites domuncula was used to identify early markers for thermal stress. Cubes from sponges have been kept for 30 min at 31°C (10 °C higher than the ambient temperature). After this treatment the sponge cubes were kept again at 21°C. To demonstrate that the animals reacted to the elevated temperature, the expression of heat shock protein (HSP) was determined. Using an antibody raised against HSP70, it was found by Western blotting that the animals specifically express a 45 kDa polypeptide after heat treatment. It was shown that even after 10 min of heat treatment the steady-state concentration of trehalose drops by 40% from a base level of 13 nmol/mg protein. The activit…

chemistry.chemical_classificationbiologyGlutathioneAquatic Sciencebiology.organism_classificationTrehaloseEnzyme assayHsp70Suberites domunculachemistry.chemical_compoundEnzymechemistryBiochemistryHeat shock proteinbiology.proteinTrehalasesponge; Suberites domuncula; heat shock; trehalose; glutathione; S-transferaseEcology Evolution Behavior and Systematics
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Molecular response to TBT stress in marine sponge Suberites domuncula: proteolytical cleavage and phosphorylation of KRS_SD protein kinase

2003

Abstract Marine sponges as sessile filter feeders are inevitably under a constant influence of changes in their environment. Mediation of extracellular signals and regulation of cellular response to environmental stress is a key function of cellular protein kinases. Expression, proteolytical cleavage and phosphorylation of stress-responsive KRS_SD protein kinase, in control and tributyl-tin (TBT) treated sponges were investigated. In control sponge, two KRS_SD proteins were expressed: KRS_SD1 (54 kDa) corresponding to KRS_SD calculated molecular weight, and KRS_SD2 (50 kDa). Exposure of sponges to TBT resulted in alteration of KRS_SD1 and KRS_SD2 expression levels and their phosphorylation …

chemistry.chemical_classificationbiologymedicine.diagnostic_testKinaseProteolysisKRS_SD; marine sponge; protein kinase; stress; Tributyl-tinAquatic Sciencebiology.organism_classificationCleavage (embryo)Molecular biologySuberites domunculaEnzymeBiochemistrychemistrymedicineExtracellularPhosphorylationProtein kinase AEcology Evolution Behavior and SystematicsJournal of Experimental Marine Biology and Ecology
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Expression of silicatein and collagen genes in the marine sponge Suberites domuncula is controlled by silicate and myotrophin

2000

The major skeletal elements in the (Porifera) sponges, are spicules formed from inorganic material. The spicules in the Demospongiae class are composed of hydrated, amorphous silica. Recently an enzyme, silicatein, which polymerizes alkoxide substrates to silica was described from the sponge Tethya aurantia. In the present study the cDNA encoding silicatein was isolated from the sponge Suberites domuncula. The deduced polypeptide comprises 331 amino acids and has a calculated size of Mr 36 306. This cDNA was used as a probe to study the potential role of silicate on the expression of the silicatein gene. For these studies, primmorphs, a special form of aggregates composed of proliferating c…

chemistry.chemical_classificationeducation.field_of_studyBiologybiology.organism_classificationBiochemistrySilicateMicrobiologyAmino acidSuberites domunculaMyotrophinSpongechemistry.chemical_compoundSponge spiculechemistryBiochemistryComplementary DNAeducationSuberitesEuropean Journal of Biochemistry
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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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Fabry Disease With Concomitant Lewy Body Disease

2019

AbstractAlthough Gaucher disease can be accompanied by Lewy pathology (LP) and extrapyramidal symptoms, it is unknown if LP exists in Fabry disease (FD), another progressive multisystem lysosomal storage disorder. We aimed to elucidate the distribution patterns of FD-related inclusions and LP in the brain of a 58-year-old cognitively unimpaired male FD patient suffering from predominant hypokinesia. Immunohistochemistry (CD77, α-synuclein, collagen IV) and neuropathological staging were performed on 100-µm sections. Tissue from the enteric or peripheral nervous system was unavailable. As controls, a second cognitively unimpaired 50-year-old male FD patient without LP or motor symptoms and 3…

complications [Lewy Body Disease]MalePathologyAutopsyDisease0302 clinical medicineHypokinesiapathology [Brain]Lysosomal storage diseasespathology [Neurons]metabolism [alpha-Synuclein]metabolism [Fabry Disease]pathology [Astrocytes]Neuronsα-Synuclein0303 health sciencesParkinsonismTrihexosylceramidesBrainGeneral MedicineMiddle AgedParkinson diseasecomplications [Fabry Disease]Neurologymetabolism [Neurons]alpha-Synucleinmedicine.symptomLewy Body Diseasemedicine.medical_specialtymetabolism [Lewy Body Disease]Context (language use)Substantia nigrametabolism [Trihexosylceramides]Pathology and Forensic Medicineblood supply [Brain]03 medical and health sciencesCellular and Molecular Neuroscienceα-Galactosidase AmedicineHumansddc:610030304 developmental biologypathology [Lewy Bodies]Fabry diseasebusiness.industryPars compactapathology [Lewy Body Disease]Lewy bodies/neuritesOriginal Articlesmetabolism [Lewy Bodies]medicine.diseaseFabry diseasemetabolism [Brain]AstrocytesLewy BodiesNeurology (clinical)CD77pathology [Fabry Disease]business030217 neurology & neurosurgeryJournal of Neuropathology and Experimental Neurology
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