Search results for "Molecular sequence"

showing 10 items of 1972 documents

Multiple identification of a particular type of hereditary C1q deficiency in the Turkish population: review of the cases and additional genetic and f…

1997

Complete selective deficiencies of the complement component C1q are rare genetic disorders that are associated with recurrent infections and a high prevalence of lupus erythematosus-like symptoms. All C1q deficiencies studied at the genetic level revealed single-base mutations leading to termination codons, frameshifts or amino acid exchanges and these were thought to be responsible for the defects as no other aberrations were found. One particular mutation, leading to a stop codon in the C1qA gene, was first identified in members of a Gypsy family from the Slovak Republic. The same mutation has been found in all cases of C1q deficiency from Turkey that have been investigated. Here we prese…

MaleHeterozygoteSlovakiaTurkish populationRomaTurkeyGenetic counselingMolecular Sequence DataPopulationBiologyPolymerase Chain ReactionGenetic analysisGeneticsHumansPoint MutationAmino Acid SequenceeducationGeneGenetics (clinical)Geneticseducation.field_of_studyBase SequenceComplement C1qImmunologic Deficiency SyndromesHuman geneticsStop codonPedigreeChild PreschoolMutation (genetic algorithm)Codon TerminatorFemalePolymorphism Restriction Fragment LengthHuman Genetics
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Compound heterozygosity in the SPG4 gene causes hereditary spastic paraplegia

2008

The SPG4 gene is frequently mutated in autosomal dominant form of hereditary spastic paraplegia (HSP). We report that the compound heterozygous sequence variants S44L, a known polymorphism, and c.1687G>A, a novel mutation in SPG4 cause a severe form of HSP in a patient. The family members carrying solely c.1687G>A mutation are asymptomatic for HSP. The reverse transcriptase-polymerase chain reaction (RT-PCR) analysis revealed that the c.1687G>A mutation is a splice site mutation and causes skipping of the exon 15 of spastin. Furthermore, quantification of RT-PCR products by sequencing and quantification of allele-specific expression by pyrosequencing assay revealed that c.1687G>A is a leaky…

MaleHeterozygoteSpastinHereditary spastic paraplegiaDNA Mutational AnalysisMolecular Sequence DataMutantIntracellular SpaceBiologyCompound heterozygositySpastinPolymorphism Single NucleotideWhite PeopleLoss of heterozygosity03 medical and health sciencesExon0302 clinical medicineGermanyGeneticsmedicineHumansRNA MessengerAllelesGenetics (clinical)030304 developmental biologyAdenosine TriphosphatasesRegulation of gene expressionGenetics0303 health sciencesSplice site mutationBase SequenceSpastic Paraplegia HereditaryComputational BiologyExonsmedicine.diseasePedigreeProtein TransportAmino Acid SubstitutionGene Expression RegulationMutationFemaleRNA Splice Sites030217 neurology & neurosurgeryHeLa CellsClinical Genetics
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Expression of the rat connexin 39 (rCx39) gene in myoblasts and myotubes in developing and regenerating skeletal muscles: an in situ hybridization st…

2005

We report a detailed analysis of the expression pattern of the recently identified rat connexin gene, named rat connexin 39 (rCx39), both during embryonic development and in adult life. Qualitative and quantitative reverse transcription/polymerase chain reaction analysis showed intense expression of rCx39 restricted to differentiating skeletal muscles, with a peak of expression detected at 18 days of embryonic life, followed by a rapid decline to undetectable levels within the first week of postnatal life. A combination of the in situ hybridization technique for the detection of rCx39 mRNA and immunohistochemistry for myogenin, a myoblast-specific marker, allowed us to establish that the mR…

MaleHistologyTime FactorsGap junctionMyoblasts SkeletalMolecular Sequence DataMuscle Fibers SkeletalConnexinIn situ hybridizationBiologyConnexinsPathology and Forensic MedicineSatellite cellsmedicineMyocyteAnimalsCell LineageTissue DistributionAmino Acid SequenceRNA MessengerRats WistarMuscle SkeletalMyogeninIn Situ HybridizationPhylogenyMessenger RNABase SequenceSequence Homology Amino AcidMyogenesisReverse Transcriptase Polymerase Chain ReactionRegeneration (biology)Skeletal muscleGene Expression Regulation DevelopmentalCell BiologyMolecular biologyImmunohistochemistryProtein Structure TertiaryRatsmedicine.anatomical_structureMyogenesiMyogeninMyogenic cell lineageCell and tissue research
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Yersinia pestis DNA from Skeletal Remains from the 6th Century AD Reveals Insights into Justinianic Plague

2013

Yersinia pestis, the etiologic agent of the disease plague, has been implicated in three historical pandemics. These include the third pandemic of the 19th and 20th centuries, during which plague was spread around the world, and the second pandemic of the 14th–17th centuries, which included the infamous epidemic known as the Black Death. Previous studies have confirmed that Y. pestis caused these two more recent pandemics. However, a highly spirited debate still continues as to whether Y. pestis caused the so-called Justinianic Plague of the 6th–8th centuries AD. By analyzing ancient DNA in two independent ancient DNA laboratories, we confirmed unambiguously the presence of Y. pestis DNA in…

MaleHistoryYersinia pestis590Social and Behavioral SciencesPandemicBiology (General)16th CenturyPhylogenyHistory 15th CenturybiologyBacterialHistory 19th Century20th CenturyBiological AnthropologyHistory 16th Century17th CenturyFemaleBase Sequence; Bone and Bones; DNA Bacterial; Female; Genotype; History 15th Century; History 16th Century; History 17th Century; History 19th Century; History 20th Century; History Medieval; Humans; Male; Molecular Sequence Data; Pandemics; Yersinia pestis; Phylogeny; PlagueMedievalResearch ArticleDNA BacterialGenotypeQH301-705.5ImmunologyMolecular Sequence DataPlague (disease)MicrobiologyBone and BonesNOHistory 17th CenturyVirologyGeneticsHumansBase sequenceMolecular BiologyPandemicsBiologyPlague bacillus19th CenturyPlagueBase SequenceDNARC581-607History 20th Centurybiology.organism_classificationVirologyHistory Medieval15th CenturyAncient DNAYersinia pestisAnthropologyYersinia pestis DNAParasitologyImmunologic diseases. Allergy
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Expression of liver peroxisomal proteins as compared to other organelle marker enzymes in rats treated with hypolipidemic agents.

1990

Abstract Peroxisome proliferation induced by 2 hypolipidemic agents (clofibrate and ciprofibrate) was studied in rats by complementary approaches, ie cell fractionation, electron microscopy, marker enzyme activities, immunoblotting and nucleic acid hybridization techniques. Administration of clofibrates for 2 and 52 weeks in doses of 500 ppm and 50 ppm respectively, or ciprofibrate for 2,28 and 52 weeks in doses of 250, 25 and 25 ppm respectively, did not alter the behavior of the peroxisomes after induction as shown by ultracentrifugation profiles. The peroxisome mass was increased as shown by the purification procedure. Specific enzymes (catalase and mostly cyanide insensitive palmitoyl C…

MaleImmunoblottingMolecular Sequence DataPeroxisome ProliferationMitochondrionCell FractionationMicrobodiesClofibric AcidOrganellemedicineAnimalsClofibrateRNA MessengerHypolipidemic AgentsOrganellesClofibratebiologyBase SequenceEndoplasmic reticulumFibric AcidsRats Inbred StrainsCell BiologyGeneral MedicinePeroxisomeMolecular biologyRats Inbred F344RatsBiochemistryLiverCatalasebiology.proteinCiprofibrateDNA Probesmedicine.drugBiology of the cell
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Echinostoma caproni: identification of enolase in excretory/secretory products, molecular cloning, and functional expression.

2007

In order to investigate molecules that could be involved in host-trematode relationships, we have analysed the excretory/secretory products (ESP) of Echinostoma caproni following a proteomic approach. Actin, Gluthathione S-transferase (GST) and enolase have been identified in the ESP. Enolase, observed to be one of the most abundant proteins, was further characterized. The molecular cloning and in vitro expression in Escherichia coli of E. caproni enolase allowed us to determine that the protein contains 431 amino acids and a theoretical MW of 46272 Da. E. caproni enolase shows high homology to other trematode enolases. The recombinant protein binds specifically to human plasminogen in vitr…

MaleImmunologyEnolaseBlotting WesternMolecular Sequence DataMolecular cloningBiologymedicine.disease_causeGene Expression Regulation Enzymologiclaw.inventionlawCricetinaeEchinostomamedicineAnimalsHumansElectrophoresis Gel Two-DimensionalAmino Acid SequenceCloning MolecularRats WistarEscherichia coliActinchemistry.chemical_classificationMesocricetusSequence Homology Amino AcidReverse Transcriptase Polymerase Chain ReactionPlasminogenGeneral MedicineMolecular biologyIn vitroRecombinant ProteinsAmino acidRatsInfectious DiseaseschemistryBiochemistryExcretory systemPhosphopyruvate HydrataseSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationRecombinant DNAParasitologyElectrophoresis Polyacrylamide GelSequence AlignmentExperimental parasitology
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Differential Infectivity of Two Pseudomonas Species and the Immune Response in the Milkweed Bug, Oncopeltus fasciatus (Insecta: Hemiptera)

2002

Pseudomonas aeruginosa and Pseudomonas putida show a profound differential infectivity after inoculation in Oncopeltus fasciatus. Whereas P. putida has no significant impact on nymphs, P. aeruginosa kills all experimental animals within 48 h. Both Pseudomonas species, however, induce the same four hemolymph peptides in O. fasciatus. Also injection of saline solution and injury induced these peptides. In general peptide induction was stronger in nymphs than in adult males. A significantly higher number of nymphs survived a challenge with P. aeruginosa when an immunization with P. putida preceded. The antibacterial properties of the hemolymph were demonstrated in inhibition experiments with P…

MaleInfectivitychemistry.chemical_classificationEdman degradationPseudomonas putidaMolecular Sequence DataPseudomonasPeptideBiologyPyrrhocorisbiology.organism_classificationPseudomonas putidaMicrobiologyHemipterachemistryPseudomonas aeruginosaHemolymphAnimalsAmino Acid SequenceEcology Evolution Behavior and SystematicsAntibacterial agentJournal of Invertebrate Pathology
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Elevated blood Hsp60, its structural similarities and cross-reactivity with thyroid molecules, and its presence on the plasma membrane of oncocytes p…

2014

The role Hsp60 might play in various inflammatory and autoimmune diseases is under investigation, but little information exists pertaining to Hashimoto’s thyroiditis (HT). With the aim to fill this gap, in the present work, we directed our attention to Hsp60 participation in HT pathogenesis. We found Hsp60 levels increased in the blood of HT patients compared to controls. The chaperonin was immunolocalized in thyroid tissue specimens from patients with HT, both in thyrocytes and oncocytes (Hurthle cells) with higher levels compared to controls (goiter). In oncocytes, we found Hsp60 not only in the cytoplasm but also on the plasma membrane, as shown by double immunofluorescence performed on …

MaleIntegrinsmedicine.medical_treatmentThyroid Glandmedicine.disease_causeBiochemistryThyroiditisAutoimmunityHashimoto DiseaseThyroglobulin (TG)Hashimoto's thyroiditis (HT)Oxyphil CellsbiologyThyroid peroxidase (TPO)GoiterThyroidHsp60Immunohistochemistrymedicine.anatomical_structureFemaleAntibodyAdultmedicine.medical_specialtyendocrine systemanimal structuresMolecular Sequence Datachemical and pharmacologic phenomenaEnzyme-Linked Immunosorbent AssayHashimoto DiseaseCross Reactionscomplex mixturesIodide PeroxidaseThyroglobulinMitochondrial ProteinsYoung AdultThyroid peroxidaseInternal medicinemedicineHumansAmino Acid SequenceAutoantibodiesOriginal PaperfungiCell MembraneAutoantibodyComputational BiologyCell BiologyChaperonin 60medicine.diseaseHsp60 . Hashimoto's thyroiditis (HT) . Thyroglobulin (TG) . Thyroid peroxidase (TPO) . Autoantibodies . Oncocytes . Hurthle cells . Thyrocytes . Chaperonin . AutoimmunityEndocrinologyStructural Homology Proteinbiology.proteinLeukocytes MononuclearThyroglobulinCell stresschaperones
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Friedreich's Ataxia: Autosomal Recessive Disease Caused by an Intronic GAA Triplet Repeat Expansion

1996

International audience; Friedreich's ataxia (FRDA) is an autosomal recessive, degenerative disease that involves the central and peripheral nervous systems and the heart. A gene, X25, was identified in the critical region for the FRDA locus on chromosome 9q13. This gene encodes a 210-amino acid protein, frataxin, that has homologs in distant species such as Caenorhabditis elegans and yeast. A few FRDA patients were found to have point mutations in X25, but the majority were homozygous for an unstable GAA trinucleotide expansion in the first X25 intron.

MaleIron-sulfur cluster assemblyPolymerase Chain Reaction0302 clinical medicineTrinucleotide RepeatsIron-Binding ProteinsGenetics0303 health sciencesMultidisciplinaryAutosomal recessive cerebellar ataxiaPedigree3. Good healthFemalemedicine.symptomChromosomes Human Pair 9HumanPair 9Heterozygotecongenital hereditary and neonatal diseases and abnormalitiesAtaxiaMolecular Sequence DataGenes RecessiveLocus (genetics)BiologyChromosomes03 medical and health sciencesGene mappingAlleles; Amino Acid Sequence; Base Sequence; Chromosomes Human Pair 9; DNA Primers; Female; Friedreich Ataxia; Genes Recessive; Heterozygote; Humans; Male; Molecular Sequence Data; Pedigree; Point Mutation; Polymerase Chain Reaction; Proteins; Sequence Alignment; Introns; Iron-Binding Proteins; Trinucleotide RepeatsmedicineRecessiveHumansPoint MutationAmino Acid SequenceAlleleAllelesDNA Primers030304 developmental biologyBase SequencePoint mutationProteins[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologymedicine.diseaseMolecular biologyIntronsGenes[SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human geneticsFriedreich AtaxiaFrataxinbiology.proteinSequence Alignment030217 neurology & neurosurgeryScience
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Molecular and morphological evidence for three species of Diplostomum (Digenea: Diplostomidae), parasites of fishes and fish-eating birds in Spain

2014

Background Recent molecular studies have revealed high species diversity of Diplostomum in central and northern Europe. However, our knowledge of the distribution of Diplostomum spp. in the southern distributional range in Europe of the snail intermediate hosts (Lymnaea stagnalis and Radix spp.) is rather limited. This study aims to fill this gap in our knowledge using molecular and morphological evidence. Methods Nineteen fish species and six fish-eating bird species were sampled opportunistically in three regions (Catalonia, Extremadura and Aragon) in Spain. All isolates of Diplostomum spp. were characterised morphologically and molecularly. Partial sequences of the barcode region of the …

MaleLens metacercariaeEntomologyRange (biology)Molecular Sequence DataZoologyDiplostomum pseudospathaceumDigeneaBirdsFish DiseasesSensuAnimalsITS1-5.8S-ITS2CladePhylogenyFreshwater fishbiologyBird DiseasesEcologyResearchFishesSpecies diversityDiplostomum spathaceumCestode Infectionsbiology.organism_classificationGullsInfectious DiseasesPlatyhelminthsSpainFreshwater fishFemaleParasitologySpecies richnessCox1Parasites & Vectors
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