Search results for "Cattle"

showing 10 items of 608 documents

Ultrastructure, fractionation and biochemical analysis of Cryptosporidium parvum sporozoites.

1999

Abstract Sporozoites of the apicomplexan parasite Cryptosporidium parvum were subjected to cell disruption and subcellular fractionation using a sucrose density step gradient. With this procedure, highly enriched preparations of the parasite membrane, the micronemes, dense granules and amylopectin granules were produced. No separate fraction containing rhoptries was obtained, however this organelle was found in defined fractions of the gradient, still associated with the apical tip of the sporozoites. Using negative staining, the internal structure of the micronemes was revealed by transmission electron microscopy. Micronemes and dense granules showed characteristic protein compositions by …

Cryptosporidium parvumOrganellesRhoptryProtozoan ProteinsCattle DiseasesCryptosporidiosisBiologybiology.organism_classificationCell FractionationNegative stainApicomplexaMicronemeMicroscopy ElectronInfectious DiseasesCryptosporidium parvumBiochemistryOrganelleUltrastructureCentrifugation Density GradientAnimalsParasitologyCattleElectrophoresis Polyacrylamide GelCell fractionationInternational journal for parasitology
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Protective Effects of L- and D-Carnosine on R-Crystallin Amyloid Fibril Formation: Implications for Cataract Disease

2009

Mildly denaturing conditions induce bovine ?-crystallin, the major structural lens protein, to self-assemble into fibrillar structures in vitro. The natural dipeptide L-carnosine has been shown to have potential protective and therapeutic significance in many diseases. Carnosine derivatives have been proposed as potent agents for ophthalmic therapies of senile cataracts and diabetic ocular complications. Here we report the inhibitory effect induced by the peptide (L- and D-enantiomeric form) on ?-crystallin fibrillation and the almost complete restoration of the chaperone activity lost after denaturant and/or heat stress. Scanning force microscopy (SFM), thioflavin T, and a turbidimetry ass…

CrystallinCircular dichroismAmyloidCarnosinePeptideMicroscopy Atomic ForceBiochemistryCataractLens proteinRats Sprague-Dawleychemistry.chemical_compoundOrgan Culture TechniquesCrystallinChaperone activityAnimalsalpha-CrystallinsSFM Scanning Force Microscopychemistry.chemical_classificationDipeptideCD Circular DichroismThT Thioflavin TCalorimetry Differential ScanningDSC Differential Scanning CalorimetryCircular DichroismCarnosineStereoisomerismIn vitroeye diseasesRatsSpectrometry FluorescencechemistryBiochemistryHEPES 4-(2-Hydroxyethyl)piperazine-1-ethanesulfonic acidThioflavinCattleFemaleSpectrophotometry Ultravioletsense organsAmyloid fibrilMolecular Chaperones
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The efficient bovine insulin presentation capacity of bone marrow-derived macrophages activated by granulocyte-macrophage colony-stimulating factor c…

1993

Bone marrow-derived macrophages (BMM phi) were shown before to function as antigen-presenting cells. We show here, that the antigen presentation capacity of BMM phi depends on the nature of the antigen and is differently regulated by the lymphokines interferon-gamma (IFN-gamma) and granulocyte/macrophage-colony-stimulating factor (GM-CSF). When bovine insulin (BI) was employed as antigen, only BMM phi treated with GM-CSF (GM-CSF-M phi) were efficient presenters, but when presentation of the antigens ovalbumin and conalbumin was tested, IFN-gamma-pulsed BMM phi (IFN-gamma-M phi) proved superior to GM-CSF-M phi. The lack of efficient BI presentation function of IFN-gamma-M phi was only obviou…

CytoplasmImmunologyAntigen presentationAntigen-Presenting CellsBone Marrow CellsBiologyInterferon-gammachemistry.chemical_compoundAntigenmedicineAnimalsInsulinImmunology and AllergyCysteineSulfhydryl CompoundsAntigen-presenting cellAntigen processingMacrophagesLymphokineGranulocyte-Macrophage Colony-Stimulating FactorGlutathioneMacrophage ActivationGlutathioneCell biologyGranulocyte macrophage colony-stimulating factorBiochemistrychemistryCattleIntracellularmedicine.drugEuropean Journal of Immunology
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2'-O-methyl-5-formylcytidine (f5Cm), a new modified nucleotide at the 'wobble' of two cytoplasmic tRNAs Leu (NAA) from bovine liver.

1996

The nucleotide analysis of a cytoplasmic tRNA(Leu) isolated from bovine liver revealed the presence of an unknown modified nucleotide N. The corresponding N nucleoside was isolated by different enzymatic and chromatographic protocols from a partially purified preparation of this tRNA(Leu). Its chemical characterization was determined from its chromatographic properties, UV-absorption spectroscopy and mass spectrometric measurements, as well as from those of the borohydride reduced N nucleoside and its etheno-trimethylsilyl derivative. The structure of N was established as 2'-O-methyl-5-formylcytidine (f5CM), and its reduced derivative as 2'-O-methyl-5-hydroxy-methylcytidine (om5Cm). By sequ…

CytoplasmMolecular Sequence DataWobble base pairBorohydridesCytidineBiologyRNA Transfer Amino AcylGas Chromatography-Mass Spectrometrychemistry.chemical_compoundGeneticsAnimalsHumansNucleotidechemistry.chemical_classificationBase SequenceMolecular StructureNucleic acid sequenceCytidineUridinechemistryBiochemistryLiverTransfer RNANucleic Acid ConformationCattleLeucineNucleosideHeLa CellsResearch ArticleNucleic acids research
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Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1.

1999

AbstractThe interaction of cytoplasmic dynein with its cargoes is thought to be indirectly mediated by dynactin, a complex that binds to the dynein intermediate chain. However, the roles of other dynein subunits in cargo binding have been unknown. Here we demonstrate that dynein translocates rhodopsin-bearing vesicles along microtubules. This interaction occurs directly between the C-terminal cytoplasmic tail of rhodopsin and Tctex-1, a dynein light chain. C-terminal rhodopsin mutations responsible for retinitis pigmentosa inhibit this interaction. Our results point to an alternative docking mechanism for cytoplasmic dynein, provide novel insights into the role of motor proteins in the pola…

CytoplasmRhodopsingenetic structuresMicrotubule-associated proteinRecombinant Fusion ProteinsDyneinMolecular Sequence DataReceptors Cell Surfacemacromolecular substancesBiologyT-Complex Genome RegionMicrotubulesGeneral Biochemistry Genetics and Molecular BiologyMotor protein03 medical and health sciencesMice0302 clinical medicineMicrotubuleAnimalsAmino Acid Sequence030304 developmental biologyt-Complex Genome Region0303 health sciencesBinding SitesBiochemistry Genetics and Molecular Biology(all)DyneinsNuclear ProteinsBiological Transport3. Good healthCell biologyCytoplasmRhodopsinMutagenesisDynactinbiology.proteinMicrotubule ProteinsCattlesense organsMicrotubule-Associated Proteins030217 neurology & neurosurgeryPhotoreceptor Cells VertebrateCell
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Selective targeting of avidin/mannose 6-phosphate receptor chimeras to early or late endosomes

2000

Summary In this study we have used the Semliki forest virus expression system to transiently express chimeric proteins that contain transmembrane and cytoplasmic domains of the cation-independent mannose 6-phosphate receptor (CI-MPR) fused to chicken avidin. Immunofluorescence and electron microscopy studies showed that the chimeric protein with the entire cytoplasmic domain of CI-MPR was transported to late endosomes, where it accumulated. We made use of the biotin-binding capacity of lumenal avidin, and found that, in agreement with this distribution, the chimeric protein could be labelled with biotinylated HRP endocytosed for a long, but not a brief, period of time. However, truncation o…

CytoplasmTime FactorsHistologyEndosomeRecombinant Fusion ProteinsAmino Acid MotifsGreen Fluorescent ProteinsEndosomesEndocytosisReceptor IGF Type 2Pathology and Forensic Medicine03 medical and health sciencesCationsCricetinaeAnimalsBiotinylation030304 developmental biologyProtein Synthesis Inhibitors0303 health sciencesBrefeldin AMannose 6-phosphate receptorbiologyCell Membrane030302 biochemistry & molecular biologyPovidoneBiological TransportCell BiologyGeneral MedicineAvidinSilicon DioxideSemliki forest virusFusion proteinMolecular biologyEndocytosisTransmembrane proteinProtein Structure TertiaryLuminescent ProteinsMicroscopy ElectronTransmembrane domainCross-Linking ReagentsMicroscopy FluorescenceBiotinylationbiology.proteinCattleChickensDimerizationAvidinEuropean Journal of Cell Biology
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Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity …

1999

ERK1 and ERK2 associate with the tyrosine phosphatase PTP-SL through a kinase interaction motif (KIM) located in the juxtamembrane region of PTP-SL. A glutathione S-transferase (GST)-PTP-SL fusion protein containing the KIM associated with ERK1 and ERK2 as well as with p38/HOG, but not with the related JNK1 kinase or with protein kinase A or C. Accordingly, ERK2 showed in vitro substrate specificity to phosphorylate GST-PTP-SL in comparison with GST-c-Jun. Furthermore, tyrosine dephosphorylation of ERK2 by the PTP-SLDeltaKIM mutant was impaired. The in vitro association of ERK1/2 with GST-PTP-SL was highly stable; however, low concentrations of nucleotides partially dissociated the ERK1/2.P…

Cytoplasmanimal structuresProtein Kinase C-alphaRecombinant Fusion ProteinsCèl·lulesNerve Tissue ProteinsProtein tyrosine phosphataseMitogen-activated protein kinase kinaseTransfectionenvironment and public healthBiochemistrySH3 domainReceptor tyrosine kinaseMAP2K7Substrate SpecificitySerineAnimalsc-RafAmino Acid SequenceMolecular BiologyProtein Kinase CSequence DeletionMitogen-Activated Protein Kinase 1Binding SitesMitogen-Activated Protein Kinase 3biologyCyclin-dependent kinase 2Intracellular Signaling Peptides and ProteinsJNK Mitogen-Activated Protein KinasesCell BiologyCyclic AMP-Dependent Protein KinasesIsoenzymesenzymes and coenzymes (carbohydrates)KineticsBiochemistryAmino Acid SubstitutionCOS CellsCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedCyclin-dependent kinase 9CattleMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesProteïnes
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A neutralizing antibody against human DNA polymerase epsilon inhibits cellular but not SV40 DNA replication.

1999

The contribution of human DNA polymerase epsilon to nuclear DNA replication was studied. Antibody K18 that specifically inhibits DNA polymerase activity of human DNA polymerase epsilon in vitro significantly inhibits DNA synthesis both when microinjected into nuclei of exponentially growing human fibroblasts and in isolated HeLa cell nuclei. The capability of this neutralizing antibody to inhibit DNA synthesis in cells is comparable to that of monoclonal antibody SJK-132-20 against DNA polymerase alpha. Contrary to the antibody against DNA polymerase alpha, antibody K18 against DNA polymerase epsilon did not inhibit SV40 DNA replication in vitro. These results indicate that DNA polymerase e…

DNA ReplicationDNA polymeraseDNA polymerase IIDNA polymerase epsilonSimian virus 40Virus ReplicationDNA polymerase deltaAntibodiesCell LineNeutralization TestsCatalytic DomainGeneticsAnimalsHumansPolymeraseDNA clampbiologyDNA replicationDNA Polymerase IIFibroblastsMolecular biologyProliferating cell nuclear antigenBromodeoxyuridineDNA Viralbiology.proteinCattleRabbitsHeLa CellsResearch ArticleNucleic acids research
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Inhibition of DNA synthesis in chick embryo retinas, in vitro, by a factor from fetal bovine serum

1989

Fetal bovine serum inhibited deoxyribonucleic acid (DNA) synthesis in chick embryo retina explants. The inhibitory activity was precipitated from fetal bovine serum by 45% saturated ammonium sulfate and isolated by means of Sephadex G-100 and Bio-Gel P-60 columns as a peak with an apparent molecular weight of 7000 Da. DNA-inhibiting activity was heat- and acid-stable and was destroyed by dithiothreitol and alkaline treatment. The purified factor inhibited similarly both DNA synthesis and thymidine kinase activity; 50% inhibitory effect was found with 160 ng, 17 h after the addition into the incubation medium.

DNA ReplicationThymidine kinase activityDNA synthesisEmbryoBlood ProteinsBiologyMolecular biologyGrowth InhibitorsRetinaIn vitroDithiothreitolMolecular Weightchemistry.chemical_compoundOrgan Culture TechniquesDevelopmental NeurosciencechemistryBiochemistrySephadexAnimalsCattlechick embryoFetal bovine serumDNADevelopmental BiologyDevelopmental Brain Research
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Differences between cysteine and homocysteine in the induction of deoxyribose degradation and DNA damage.

2001

The effect of two naturally occurring thiols, such as cysteine and homocysteine, has been examined for their ability to induce deoxyribose degradation and DNA damage. Copper(II) ions have been added to incubation mixtures and oxygen consumption measurements have been performed in order to correlate the observed damaging effects with the rate of metal catalyzed thiol oxidation. Ascorbic acid plus copper has been used as a positive control of deoxyribose and DNA oxidation due to reactive oxygen species. Cysteine or homocysteine in the presence of copper ions induce the degradation of deoxyribose and the yield of 8-hydroxy-2'-deoxyguanosine (8-OHdG), although important differences are observed…

DNA damageAscorbic AcidThymus GlandBiochemistrySuperoxide dismutasechemistry.chemical_compoundOxygen ConsumptionPhysiology (medical)DeoxyguanosineAnimalsCysteineHomocysteineElectrophoresis Agar GelbiologyDeoxyriboseSuperoxide DismutaseThiourea8-Hydroxy-2'-deoxyguanosineDeoxyguanosineDNA oxidationAscorbic acidCatalasechemistryDeoxyriboseBiochemistry8-Hydroxy-2'-DeoxyguanosineSpectrophotometrybiology.proteinCattleReactive Oxygen SpeciesOxidation-ReductionCopperCysteineDNA DamageFree radical biologymedicine
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