Search results for "blotting"

showing 10 items of 899 documents

Mutations in a new gene, encoding a zinc-finger protein, cause tricho-rhino-phalangeal syndrome type I

1999

Tricho-rhino-phalangeal syndrome type I (TRPS I, MIM 190350) is a malformation syndrome characterized by craniofacial and skeletal abnormalities and is inherited in an autosomal dominant manner. TRPS I patients have sparse scalp hair, a bulbous tip of the nose, a long flat philtrum, a thin upper vermilion border and protruding ears. Skeletal abnormalities include cone-shaped epiphyses at the phalanges, hip malformations and short stature. We assigned TRPS1 to human chromosome 8q24. It maps proximal of EXT1, which is affected in a subgroup of patients with multiple cartilaginous exostoses and deleted in all patients with TRPS type II (TRPS II, or Langer-Giedion syndrome, MIM 150230; ref.2-5)…

MaleDNA Complementaryanimal structuresLanger-Giedion SyndromeMolecular Sequence DataBiologyLanger–Giedion syndromeOpen Reading FramesTRPS1 geneotorhinolaryngologic diseasesGeneticsmedicineTricho–rhino–phalangeal syndromeHumansGeneZinc fingerGeneticsSyndrome typeChromosome MappingZinc Fingersmedicine.diseaseBlotting NorthernPedigreeTrichorhinophalangeal syndromeMutationTrichorhinophalangeal Syndrome Type IFemaleChromosomes Human Pair 8Nature genetics
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Allopurinol has Immunomodulating Activity following Topical and Systemic Application in Experimental Autoimmune Uveitis

2001

PurposeAllopurinol has beneficial effects in the systemic treatment of lens-induced uveitis and experimental autoimmune uveitis (EAU). This is believed to be due to a reduction of oxidative tissue damage through its dose-dependent free radical scavenging ability, and to an immunomodulating effect. The purpose of this study was to demonstrate the immunological effects on the IgG-antibody repertoire in EAU after topical and systemic allopurinol and steroids.MethodsWe assigned 43 male Lewis rats to 6 different groups: healthy rats (BASE, n=3), EAU without therapy (CTRL, n=9); systemic treatment with allopurinol (ALSYS, n=9, 50 mg/kg body wt.i.v., given every three days for two weeks), topical …

MaleDrugmedicine.medical_specialtyAdministration TopicalAllopurinolmedicine.medical_treatmentmedia_common.quotation_subjectBlotting WesternAllopurinol hypersensitivity syndromeAllopurinol030204 cardiovascular system & hematologyPharmacologyAutoantigens030226 pharmacology & pharmacyAutoimmune DiseasesUveitis03 medical and health sciences0302 clinical medicineAdjuvants ImmunologicInternal medicinemedicineAnimalsGlucocorticoidsAutoantibodiesmedia_commonAutoimmune diseaseChemotherapybusiness.industryAutoantibodyFree Radical ScavengersGeneral Medicinemedicine.diseaseRatsDisease Models AnimalOphthalmologyEndocrinologyMethylprednisoloneRats Inbred LewImmunoglobulin GInjections IntravenousElectrophoresis Polyacrylamide GelbusinessUveitismedicine.drugEuropean Journal of Ophthalmology
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A novel pyruvate kinase (PK-S) from boar spermatozoa is localized at the fibrous sheath and the acrosome

2007

Boar spermatozoa contain a novel pyruvate kinase (PK-S) that is tightly bound at the acrosome of the sperm head and at the fibrous sheath in the principal piece of the flagellum, while the midpiece contains a soluble pyruvate kinase (PK). PK-S could not be solubilized by detergents, but by trypsin with no loss of activity. Purified PK-S as well as PK-S still bound to cell structures and soluble sperm PK have all kinetics similar to those of rabbit muscle PK-M1. The PK-S subunit had a relative molecular mass of 64 ± 1 × 103(n= 3), i.e. slightly higher than that of PK-M1, and carried an N-terminal extension (NH2-TSEAM-COOH) that is lacking in native PK-M1. Evidence is provided that PK-S is en…

MaleEmbryologyErythrocytesSwineProtein subunitBlotting WesternMolecular Sequence DataPyruvate KinaseBiologyEndocrinologySpecies SpecificitymedicineAnimalsAmino Acid SequenceAcrosomeSequence Homology Amino AcidMolecular massAntibodies MonoclonalObstetrics and GynecologyCell BiologyImmunogold labellingTrypsinSpermatozoaSpermReproductive MedicineBiochemistryPolyclonal antibodiesSperm Tailbiology.proteinElectrophoresis Polyacrylamide GelRabbitsSperm MidpieceAcrosomePyruvate kinasemedicine.drugReproduction
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Regulatory properties of 6-phosphofructokinase and control of glycolysis in boar spermatozoa.

2007

Glycolysis is crucial for sperm functions (motility and fertilization), but how this pathway is regulated in spermatozoa is not clear. This prompted to study the location and the regulatory properties of 6-phosphofructokinase (PFK, EC 2.7.1.11), the most important element for control of glycolytic flux. Unlike some other glycolytic enzymes, PFK showed no tight binding to sperm structures. It could readily be extracted from ejaculated boar spermatozoa by sonication and was then chromatographically purified. At physiological pH, the enzyme was allosterically inhibited by near-physiological concentrations of its co-substrate ATP, which induced co-operativity, i.e. reduced the affinity for the …

MaleEmbryologySwinePhosphofructokinase-1Allosteric regulationImmunoblottingMotilityBiologychemistry.chemical_compoundEndocrinologyAdenosine TriphosphateAllosteric RegulationFructosediphosphatesAnimalsGlycolysisCitrateschemistry.chemical_classificationObstetrics and GynecologyFructoseCell BiologyHydrogen-Ion ConcentrationSpermImmunohistochemistrySpermatozoaAdenosine MonophosphateEnzymeReproductive MedicinechemistryBiochemistryFlagellaElectrophoresis Polyacrylamide GelFlux (metabolism)AcrosomeGlycolysisPhosphofructokinaseReproduction (Cambridge, England)
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Defective nuclear localization of Hsp70 is associated with dyserythropoiesis and GATA-1 cleavage in myelodysplastic syndromes.

2012

Abstract Normal human erythroid cell maturation requests the transcription factor GATA-1 and a transient activation of caspase-3, with GATA-1 being protected from caspase-3–mediated cleavage by interaction with the chaperone heat shock protein 70 (Hsp70) in the nucleus. Erythroid cell dysplasia observed in early myelodysplastic syndromes (MDS) involves impairment of differentiation and excess of apoptosis with a burst of caspase activation. Analysis of gene expression in MDS erythroblasts obtained by ex vivo cultures demonstrates the down-regulation of a set of GATA-1 transcriptional target genes, including GYPA that encodes glycophorin A (GPA), and the up-regulation of members of the HSP70…

MaleErythroblasts[SDV]Life Sciences [q-bio]Biochemistry0302 clinical medicineTranscription (biology)hemic and lymphatic diseasesGene expressionErythropoiesisGATA1 Transcription FactorCells CulturedCaspaseComputingMilieux_MISCELLANEOUSOligonucleotide Array Sequence AnalysisAged 80 and over0303 health sciencesbiologyCaspase 3Reverse Transcriptase Polymerase Chain ReactionCell DifferentiationU937 CellsHematologyMiddle Agedmedicine.anatomical_structure030220 oncology & carcinogenesisFemaleAdultGreen Fluorescent ProteinsImmunoblottingImmunology03 medical and health sciencesErythroid CellsmedicineHumansHSP70 Heat-Shock ProteinsTranscription factorAged030304 developmental biologyCell NucleusGene Expression ProfilingCell BiologyMolecular biologyCell nucleusMicroscopy FluorescenceApoptosisMyelodysplastic SyndromesChaperone (protein)Mutationbiology.proteinNuclear localization sequence
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In-frame deletion in the seventh immunoglobulin-like repeat of filamin C in a family with myofibrillar myopathy.

2009

Myofibrillar myopathies (MFMs) are an expanding and increasingly recognized group of neuromuscular disorders caused by mutations in DES, CRYAB, MYOT, and ZASP. The latest gene to be associated with MFM was FLNC; a p.W2710X mutation in the 24th immunoglobulin-like repeat of filamin C was shown to be the cause of a distinct type of MFM in several German families. We studied an International cohort of 46 patients from 39 families with clinically and myopathologically confirmed MFM, in which DES, CRYAB, MYOT, and ZASP mutations have been excluded. In patients from an unrelated family a 12-nucleotide deletion (c.2997_3008del) in FLNC resulting in a predicted in-frame four-residue deletion (p.Val…

MaleFilaminsDNA Mutational AnalysisImmunoblottingMolecular Sequence DataImmunoglobulinsmacromolecular substancesBiologymedicine.disease_causeFilaminArticle03 medical and health sciences0302 clinical medicineContractile ProteinsMuscular DiseasesMyofibrilsGeneticsmedicineHumansFLNCAmino Acid SequenceMyopathyRepeated sequenceMuscle SkeletalGenePeptide sequenceGenetics (clinical)030304 developmental biologyRepetitive Sequences Nucleic AcidSequence DeletionGeneticsFamily Health0303 health sciencesMutationSequence Homology Amino AcidMicrofilament Proteinsmedicine.diseaseMolecular biologyImmunohistochemistry3. Good healthMicroscopy ElectronMutationFemalemedicine.symptom030217 neurology & neurosurgeryLimb-girdle muscular dystrophyEuropean journal of human genetics : EJHG
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Effect of aging and hypertension on β-myosin heavy chain in heart of spontaneously hypertensive rats

2001

During aging rat myocardium undergoes structural changes characterized by a shift in the synthesis of myosin heavy chain (MHC) from V1 isoform, composed of two alpha-MHC, to V3 isoform, composed of two beta-MHC. In rat, besides ageing, cardiac hypertrophy as adaptive response to a superimposed pressure load (such as hypertension) is characterized by predominance of V3 myosin isoform. The aim of our study was to evaluate the expression of beta-MHC in right (RV) and left (LV) ventricles of spontaneously hypertensive rats (SHRs), a well defined animal model of hypertension, in relation to aging. We used very young (8-week old) and young (15-week old) SHRs and age-matched normotensive Harlan Sp…

MaleGene isoformSenescenceAgingmedicine.medical_specialtyHeart VentriclesBlotting WesternAnimal modelRats Inbred SHRInternal medicineMyosinGeneticsmedicineAnimalsProtein Isoformscardiovascular diseasesMyosin Heavy ChainsOncogenebusiness.industryGeneral MedicineMolecular medicineRatsEndocrinologyApoptosisAgeingHypertensionbusinessInternational Journal of Molecular Medicine
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Nuclear localization of the protein encoded by the Wilms’ tumor gene WT1 in embryonic and adult tissues

1993

ABSTRACT The human Wilms’ tumor gene WT1 encodes a putative transcription factor implicated in tumorigenesis and in specifying normal urogenital development. We have studied the distribution of WT1 protein and mRNA using immunohistochemistry and in situ hybridization. Monoclonal antibodies were raised against a peptide specific to the first alternative splice site of WT1. Two antibodies specifically reacted on Western blot to this WT1 isoform. Immunofluorescence localized WT1 protein to podocytes during mesonephric and metanephric development. In situ hybridization revealed a similar pattern of expression except that WT1 mRNA was also present in metanephric blastema and renal vesicles. Mess…

MaleGene isoformcongenital hereditary and neonatal diseases and abnormalitiesmedicine.medical_specialtyBlotting WesternFluorescent Antibody TechniqueGene ExpressionUrogenital SystemIn situ hybridizationBiologyKidneyurologic and male genital diseasesPolymerase Chain ReactionInternal medicineGene expressionmedicineHumansRNA MessengerWT1 ProteinsMolecular BiologyTranscription factorIn Situ HybridizationCell NucleusMessenger RNAGranulosa CellsSertoli Cellsurogenital systemfungiZinc FingersWilms' tumormedicine.diseasefemale genital diseases and pregnancy complicationsWilms Tumor ProteinCell biologyDNA-Binding ProteinsCell nucleusmedicine.anatomical_structureEndocrinologyMesonephrosFemaleTranscription FactorsDevelopmental BiologyDevelopment
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Expression of thyroid hormone receptor isoforms in the hypertrophic heart of spontaneously hypertensive rats

2001

Thyroid hormones (THs) enhance MHC alpha gene- and repress MHC beta gene-transcription in the heart, by interacting with specific nuclear receptors (TRs), that bind to regulatory sequences localized upstream of basal promoter of myosin heavy chain (MHC) genes. The overall effects of THs include an increase in V1- and a decrease in V3-myosin isozyme concentration in the heart. Myosin V1 contains two MHC alpha chains and has a higher ATPase activity than V3 isoform, which contains two beta chains. Previous studies on papillary muscles of spontaneously hypertensive rats (SHRs) showed that heart hypertrophy is accompanied by a shift from alpha to beta MHC accumulation. The present study was aim…

MaleGene isoformmedicine.medical_specialtyHeart VentriclesBlotting WesternAlpha (ethology)CardiomegalyBiologyIsozymeRats Sprague-DawleyRats Inbred SHRInternal medicineMyosinGeneticsmedicineAnimalsProtein IsoformsReceptorReceptors Thyroid HormoneThyroid hormone receptorMyosin Heavy ChainsGeneral MedicineRatsBlotEndocrinologyNuclear receptorHypertensionModels AnimalInternational Journal of Molecular Medicine
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PAH gene mutations in the Sicilian population: association with minihaplotypes and expression analysis.

2001

Abstract The molecular basis of PAH deficiency in the Sicilian population is characterized by a marked heterogeneity, with 44 mutations at a single locus identified by a "gene-scanning" approach and accounting for a detection rate of 91%. The remaining 9% of PAH alleles does not bear mutations in any of the 13 exons and 24 exon/intron junctions. Three mutations IVS10nt-11 G > A, R261Q, and A300S accounted for 30.5%, whereas the remaining mutations were found at relative frequencies of less than 5% and 20 mutations were observed once only. Five mutations have been detected only in Sicilians so far. By studying the association of mutations with intragenic STR-VNTR haplotypes ("minihaplotypes"…

MaleGenotypeEndocrinology Diabetes and MetabolismRecombinant Fusion ProteinsPopulationDNA Mutational AnalysisBiologyGene mutationBiochemistryIdentity by descentGene Expression Regulation EnzymologicEndocrinologyHyperphenylalaninemiaPhenylketonuriasGenotypeGeneticsmedicineAnimalsHumansRNA MessengerAlleleeducationChildMolecular BiologySicilyAllelesGeneticseducation.field_of_studyPolymorphism GeneticHaplotypePhenylalanine HydroxylaseDNAmedicine.diseaseBlotting NorthernPhenotypePhenotypeHaplotypesCOS CellsMutationFemaleMolecular genetics and metabolism
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