Search results for "Molecular sequence"

showing 10 items of 1972 documents

High Variability of Fabry Disease Manifestations in an Extended Italian Family

2015

Fabry disease (FD) is an inherited metabolic disorder caused by partial or full inactivation of the lysosomal hydrolaseα-galactosidase A (α-GAL). The impairment ofα-GAL results in the accumulation of undegraded glycosphingolipids in lysosomes and subsequent cell and microvascular dysfunctions. This study reports the clinical, biochemical, and molecular characterization of 15 members of the same family. Eight members showed the exonic mutation M51I in the GLA gene, a disease-causing mutation associated with the atypical phenotype. The clinical history of this family highlights a wide phenotypic variability, in terms of involved organs and severity. The phenotypic variability of two male pati…

MaleDNA Mutational AnalysisFamilial Mediterranean feverlcsh:Medicinemedicine.disease_causePathogenesis0302 clinical medicineSettore BIO/13 - Biologia ApplicataFabry disease; GLA gene; LysoGb3glaFabry diseaseexonic mutation M51IGenetics0303 health sciencesMutationMetabolic disorderGeneral MedicineMiddle AgedPedigree3. Good healthItalyFemalemedicine.symptomResearch ArticleAdultArticle SubjectMolecular Sequence DataBiologyAsymptomaticGeneral Biochemistry Genetics and Molecular BiologyYoung Adult03 medical and health sciencesmedicineHumansFamilyGLA gene030304 developmental biologyfabry diseaseAlpha-galactosidaseBase SequenceGeneral Immunology and MicrobiologyMultiple sclerosislcsh:RLysoGb3medicine.diseaseFabry diseasealpha-GalactosidaseImmunologybiology.protein030217 neurology & neurosurgeryBioMed Research International
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The deletion of six amino acids at the C-terminus of the alpha 1 (II) chain causes overmodification of type II and type XI collagen: further evidence…

1996

We have identified an 18 bp deletion in exon 49 of the type II procollagen gene (COL2A1) in a patient with Kniest dysplasia. The deletion is located at the very C-terminus of the helical domain and removes two of three Gly-Pro-Pro triplets at positions 1007-1012, which are thought to be involved in helix formation and stability. Morphological investigation of an iliac crest biopsy showed large inclusions in the endoplasmic reticulum of chondrocytes, reflecting impaired secretion of type II collagen. Electrophoretic analysis of collagens extracted from cartilage or synthesised by cultured chondrocytes showed that type II and also type XI procollagen molecules containing mutant alpha 1 (II) c…

MaleDNA Mutational AnalysisMolecular Sequence DataMutantType II collagenBiologyOsteochondrodysplasiasChondrocyteIliumExonKniest dysplasiaGeneticsmedicineHumansAmino Acid SequencePeptide sequenceCells CulturedGenetics (clinical)Sequence DeletionInclusion BodiesGeneticsBase SequenceC-terminusExonsmedicine.diseaseMolecular biologyProcollagen peptidaseCartilagemedicine.anatomical_structureGenesChild PreschoolCollagenEndoplasmic Reticulum RoughProcollagenResearch ArticleJournal of Medical Genetics
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Bone marrow cell transcripts from Fanconi anaemia patients revealin vivoalterations in mitochondrial, redox and DNA repair pathways

2013

Fanconi anaemia (FA) is a genetic cancer predisposition disorder associated with cytogenetic instability, bone marrow failure and a pleiotropic cellular phenotype, including low thresholds of responses to oxidative stress, cross-linking agents and selected cytokines. This study was aimed at defining the scope of abnormalities in gene expression using the publicly available FA Transcriptome Consortium (FTC) database (Gene Expression Omnibus, 2009 and publicly available as GSE16334). We evaluated the data set that included transcriptomal analyses on RNA obtained from low-density bone marrow cells (BMC) from 20 patients with FA and 11 healthy volunteers, by seeking to identify changes in expre…

MaleDNA Repairiron-chelating proteinsTranscriptome0302 clinical medicineFanconi anemiaGene expressioncytokineoxidative stressChildbioenergetic pathwayRegulation of gene expression0303 health sciencesHematologyGeneral Medicineheat-shock proteinMitochondria3. Good health030220 oncology & carcinogenesisFemaleFanconi anaemiaOxidation-ReductionSignal TransductionAdultiron-chelating proteinDNA repairDNA repairBone Marrow CellsBiologyProinflammatory cytokine03 medical and health sciencesmedicineHumanstranscriptsGene030304 developmental biologyoxidative streGene Expression Profilingheat-shock proteinsMolecular Sequence Annotationmedicine.diseaseMolecular biologycytokinesDNA repair Fanconi anaemia bioenergetic pathways cytokines heat-shock proteins iron-chelating proteins oxidative stress transcriptsGene expression profilingOxidative StressFanconi AnemiaCase-Control Studiesbioenergetic pathwaysTranscriptomeEuropean Journal of Haematology
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A novel serine/threonine kinase gene, STK33 , on human chromosome 11p15.3

2001

Human chromosomal region 11p15 is known to be associated with several diseases including predispositions to develop various tumor types. In search of candidate genes, a novel human kinase gene is described, STK33, which codes for a serine/threonine protein kinase. The gene was discovered by comparative genome analysis of human chromosome 11p15.3 and its orthologous region on distal mouse chromosome 7. Human STK33 gene contains 12 exons as has been determined by the comparison to the full-length transcript amplified from human uterus RNA. Transcripts are found in a variety of tissues in at least two alternatively spliced forms as revealed by reverse transcriptase-polymerase chain reaction, c…

MaleDNA ComplementaryMolecular Sequence DataGene ExpressionProtein Serine-Threonine KinasesMAP3K7MAP2K7MiceTANK-binding kinase 1GeneticsAnimalsHumansTissue DistributionAmino Acid SequenceRNA Messengerc-RafPhylogenyGeneticsSerine/threonine-specific protein kinaseBase SequenceSequence Homology Amino AcidbiologyChromosomes Human Pair 11Cyclin-dependent kinase 2DNAExonsSequence Analysis DNAGeneral MedicineMolecular biologyIntronsGenesChromosomal regionbiology.proteinFemalePRKCB1Sequence AlignmentGene
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The Drosophila Cystoblast Differentiation Factor, benign gonial cell neoplasm, Is Related to DExH-box Proteins and Interacts Genetically With bag-of-…

2000

Abstract Selection of asymmetric cell fates can involve both intrinsic and extrinsic factors. Previously we have identified the bag-of-marbles (bam) gene as an intrinsic factor for cystoblast fate in Drosophila germline cells and shown that it requires active product from the benign gonial cell neoplasm (bgcn) gene. Here we present the cloning and characterization of bgcn. The predicted Bgcn protein is related to the DExH-box family of RNA-dependent helicases but lacks critical residues for ATPase and helicase functions. Expression of the bgcn gene is extremely limited in ovaries but, significantly, bgcn mRNA is expressed in a very limited number of germline cells, including the stem cells.…

MaleDNA ComplementaryMolecular Sequence DataGermlineGeneticsProtein biosynthesisAnimalsDrosophila ProteinsAmino Acid SequenceRNA MessengerCloning MolecularPromoter Regions GeneticGeneAllelesGene LibraryCloningGeneticsModels GeneticSequence Homology Amino AcidbiologyDNA HelicasesHelicasePhenotypeEnhancer Elements GeneticGerm CellsPhenotypeProtein Biosynthesisbiology.proteinInsect ProteinsDrosophilaFemaleStem cellRNA HelicasesDrosophila ProteinResearch ArticleGenetics
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Molecular characterization of Lma-p54, a new epicuticular surface protein in the cockroach Leucophaea maderae (Dictyoptera, oxyhaloinae)

2002

0965-1748 (Print) Journal Article Research Support, Non-U.S. Gov't; The epicuticular surface protein Lma-p54 is imbedded in the "cuticular waxes" which cover the abdominal surface of the adult Leucophaea maderae. Natural Lma-p54 was purified and the complete cDNA sequence was determined by RT-PCR using primers based on Edman degradation fragments. Northern blot and in situ hybridization analyses showed that Lma-p54 was expressed in the adult abdominal epidermis and in the chemical sense organs of both sexes. Sequence alignment indicates that Lma-p54 is closely related to aspartic proteases (EC 3.4.23). However, there are critical amino acid substitutions at the level of the active site and,…

MaleDNA ComplementaryMolecular Sequence DataSequence HomologyCockroachesSequence alignmentRecombinant Proteins/chemistryComplementary/geneticsBiochemistryPolymerase Chain ReactionCockroaches/*genetics/growth & developmentComplementary DNAAspartic Endopeptidases/*geneticsAspartic Acid EndopeptidasesAnimalsGlycoproteins/*geneticsNorthern blotAmino Acid SequenceMolecular BiologyPeptide sequenceIn Situ HybridizationGlycoproteinschemistry.chemical_classificationSequence Homology Amino AcidbiologyEdman degradationBase SequenceDictyopteraDNAbiology.organism_classificationMolecular biologyRecombinant ProteinsAmino acidInsect Proteins/*geneticsAmino AcidBiochemistrychemistryInsect ScienceLarvaInsect ProteinsFemaleGlycoproteinSequence Alignment
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Molecular characterisation and evolution of the hemocyanin from the European spiny lobster, Palinurus elephas.

2003

The hemocyanin of the European spiny lobster Palinurus elephas (synonym: Palinurus vulgaris) is a hexamer composed by four closely related but distinct subunits. We have obtained the full cDNA sequences of all four subunits, which cover 2275-2298 bp and encode for native polypeptides of 656 and 657 amino acids. The P. elephas hemocyanin subunits belong to the alpha-type of crustacean hemocyanins, whereas beta- and gamma-subunits are absent in this species. An unusual high ratio of non-synonymous versus synonymous nucleotide substitutions was observed, suggesting positive selection among subunits. Assuming a constant evolution rate, the P. elephas hemocyanin subunits emerged from a single he…

MaleDNA ComplementaryPanulirusPhysiologymedicine.medical_treatmentPalinurus elephasMolecular Sequence Datachemical and pharmacologic phenomenaBiochemistryEvolution MolecularPaleontologyEndocrinologyElephasPhylogeneticsmedicineAnimalsProtein IsoformsAmino Acid SequencePalinuridaeEcology Evolution Behavior and SystematicsPhylogenybiologySequence Homology Amino AcidHemocyaninBayes Theorembiology.organism_classificationCrustaceanPalinurusEvolutionary biologyHemocyaninsAnimal Science and ZoologySpiny lobsterJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology
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Isolation and characterization of cold-shock domain protein genes, Oryzias latipes Y-box protein 2 ( OlaYP2 ) and Fugu rubripes Y-box protein 1 ( Fru…

2002

The Y-box protein (YP) family shares a nucleic acid binding domain, called cold-shock domain, that has been evolutionarily highly conserved from bacteria to human. The different YPs identified so far in vertebrates are thought to function as transcriptional activators, transcriptional repressors and/or translational repressors. Medakafish and pufferfish are very suitable vertebrate models for the study of developmental genetics and comparative genomics, respectively. Here we report the isolation of two teleost YP genes, medakafish Oryzias latipes (Ola)YP2 and Fugu rubripes (Fru)YP1, which are expressed in multiple tissues. Phylogenetic analysis demonstrated that OlaYP2 and FruYP1 belong to …

MaleDNA ComplementarySequence analysisOryziasMolecular Sequence DataProtein domainOryziasGene ExpressionBiologyGeneticsAnimalsAmino Acid SequenceIn Situ Hybridization FluorescencePhylogenyComparative genomicsGeneticsBase SequenceSequence Homology Amino AcidFugufungiChromosome MappingSequence Analysis DNAGeneral MedicineY box binding protein 1Cold-shock domainbiology.organism_classificationTakifuguFemaleSequence AlignmentTranscription FactorsBinding domainGene
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Differential regulation by a peroxisome proliferator of the different multifunctional proteins in guinea pig: cDNA cloning of the guinea pig D-specif…

1998

After our previous report on the cloning of two cDNA species in guinea pig, both encoding the same hepatic 79 kDa multifunctional protein 1 (MFP-1) [Caira, Cherkaoui-Malki, Hoefler and Latruffe (1996) FEBS Lett. 378, 57-60], here we report the cloning of a cDNA encoding a second multifunctional peroxisomal protein (MFP-2) in guinea-pig liver. This 2356 nt cDNA encodes a protein of 735 residues (79.7 kDa) whose sequence shows 83% identity with rat MFP-2 [Dieuaide-Noubhani, Novikov, Baumgart, Vanhooren, Fransen, Goethals, Vandekerckhove, Van Veldhoven and Mannaerts (1996) Eur. J. Biochem. 240, 660-666]. In parallel, we studied the effect of ciprofibrate, a hypolipaemic agent also known as per…

MaleDNA ComplementaryTranscription GeneticGuinea PigsMolecular Sequence DataBiologyMicrobodiesBiochemistryEstradiol DehydrogenasesRats Sprague-DawleyGuinea pigClofibric AcidComplementary DNAGene expressionmedicineAnimalsAmino Acid SequenceRNA MessengerNorthern blotCloning MolecularEnoyl-CoA HydrataseMolecular BiologyHypolipidemic AgentsMessenger RNABase SequenceThiolaseFibric AcidsCell BiologyPeroxisomeMolecular biologyRatsGene Expression RegulationLiverBiochemistryCiprofibrateOxidoreductasesResearch Articlemedicine.drugBiochemical Journal
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The new gene DmX from Drosophila melanogaster encodes a novel WD-repeat protein

1998

DmX is a novel gene from Drosophila melanogaster located on the X chromosome in region 5D5/6-E1. The molecular analysis of the genomic and cDNA sequences of DmX shows that the gene spans appr. 16kb and displays a mosaic structure with 15 exons. The 12kb long DmX transcript is present in Drosophila embryos, larvae and adults of both sexes. The open reading frame of DmX encodes a novel WD-repeat protein, containing at least 30 WD-repeat units. WD-repeat proteins contain a conserved motif of approximately 40 amino acids (aa), usually ending with the dipeptide Trp-Asp (WD). Homologues of the DmX gene exist in other dipteran species, in Caenorhabditis elegans and human, revealing that DmX is an …

MaleDNA ComplementaryX ChromosomeTranscription GeneticMolecular Sequence DataGenes InsectOpen Reading FramesExonComplementary DNAGeneticsAnimalsDrosophila ProteinsAmino Acid SequenceRNA MessengerCloning MolecularPeptide sequenceGeneConserved SequenceX chromosomeCaenorhabditis elegansRepetitive Sequences Nucleic AcidGeneticsAspartic AcidbiologyTryptophanChromosome MappingGene Expression Regulation DevelopmentalSequence Analysis DNAGeneral Medicinebiology.organism_classificationOpen reading frameDrosophila melanogasterInsect ProteinsFemaleDrosophila melanogasterSequence AlignmentGene
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