Search results for "LIM Domain Proteins"

showing 10 items of 10 documents

Transcriptome-Wide Analysis Identifies Novel Associations With Blood Pressure.

2017

Hypertension represents a major cardiovascular risk factor. The pathophysiology of increased blood pressure (BP) is not yet completely understood. Transcriptome profiling offers possibilities to uncover genetics effects on BP. Based on 2 populations including 2549 individuals, a meta-analyses of monocytic transcriptome-wide profiles were performed to identify transcripts associated with BP. Replication was performed in 2 independent studies of whole-blood transcriptome data including 1990 individuals. For identified candidate genes, a direct link between long-term changes in BP and gene expression over time and by treatment with BP-lowering therapy was assessed. The predictive value of pro…

0301 basic medicineMaleCandidate geneGene ExpressionGenome-wide association studyBlood Pressure030204 cardiovascular system & hematologyCardiorespiratory Medicine and HaematologyCardiovascularLMNATranscriptome0302 clinical medicineRisk FactorsCEBPAGene expression2.1 Biological and endogenous factorsAetiologyGeneticsMyelin and Lymphocyte-Associated Proteolipid ProteinsBlood Pressure ; Gene Expression ; Genome-wide Association Study ; Hypertension ; Transcriptomeblood pressureGenomicsSingle NucleotideLIM Domain Proteinsblood pressure; gene expression; genome-wide association study; hypertension; transcriptomeStrokeHeart DiseaseHypertensionPublic Health and Health ServicesBiomarker (medicine)FemaleEssential HypertensionPoly(ADP-ribose) PolymerasesBiotechnologyAdulthypertensionClinical SciencesNucleoside Transport ProteinsBiologyPolymorphism Single NucleotideArticle03 medical and health sciencesClinical ResearchInternal MedicineGeneticsHumansPolymorphismgenome-wide association studyGene Expression ProfilingHuman GenomeBlood Pressure DeterminationGene expression profiling030104 developmental biologyGood Health and Well BeingCardiovascular System & Hematologygene expressionCCAAT-Enhancer-Binding ProteinsCarrier ProteinstranscriptomeTranscription Factors
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Clinical, histological and genetic characterization of reducing body myopathy caused by mutations in FHL1

2008

We recently identified the X-chromosomal four and a half LIM domain gene FHL1 as the causative gene for reducing body myopathy, a disorder characterized by progressive weakness and intracytoplasmic aggregates in muscle that exert reducing activity on menadione nitro-blue-tetrazolium (NBT). The mutations detected in FHL1 affected highly conserved zinc coordinating residues within the second LIM domain and lead to the formation of aggregates when transfected into cells. Our aim was to define the clinical and morphological phenotype of this myopathy and to assess the mutational spectrum of FHL1 mutations in reducing body myopathy in a larger cohort of patients. Patients were ascertained via th…

AdultMaleWeaknessPathologymedicine.medical_specialtyMutation MissenseMuscle ProteinsBiologymedicine.disease_causeMuscular DiseasesBiopsymedicineHumansGenetic Predisposition to DiseaseMyopathyChildMicroscopy ImmunoelectronMuscle SkeletalMutationMuscle biopsymedicine.diagnostic_testIntracellular Signaling Peptides and ProteinsInfantGenetic Diseases X-LinkedOriginal ArticlesLIM Domain Proteinsmedicine.diseaseCongenital myopathyFHL1PedigreeChild PreschoolFemaleNeurology (clinical)medicine.symptomProgressive disease
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Cyclic AMP-mediated upregulation of the expression of neuronal NO synthase in human A673 neuroepithelioma cells results in a decrease in the level of…

2004

The expression level of neuronal nitric oxide synthase (nNOS) can vary depending on the (patho)physiological conditions. Here we document a marked induction of nNOS mRNA, protein, and total NO production in response to dibutyryl cyclic AMP (db-cAMP) in human A673 neuroepithelial cells. However, the upregulation of nNOS was associated with a decreased level of production of bioactive NO and by an increase in the level of generation of reactive oxygen species (ROS). ROS production could be prevented by the NOS inhibitor L-NAME, suggesting nNOS itself is involved in ROS generation. Sepiapterin supplementation of db-cAMP-treated A673 cells could restore full bioactive NO production, most likely…

CAMP-Responsive Element ModulatorNitric Oxide Synthase Type IBiologyCREBNitric OxideBiochemistryAdenylyl cyclaseCyclic AMP Response Element Modulatorchemistry.chemical_compoundMiceNeuroblastomaCoactivatorComplement C3b Inactivator ProteinsCyclic AMPAnimalsHumansNeuroectodermal Tumors Primitive PeripheralCREB-binding proteinEnzyme InhibitorsProtein kinase AeducationCyclic AMP Response Element-Binding ProteinGTP CyclohydrolaseCAMP response element bindingHomeodomain ProteinsNeuronseducation.field_of_studyForskolinPhosphoric Diester HydrolasesIntracellular Signaling Peptides and ProteinsBlood ProteinsLIM Domain ProteinsMolecular biologyCyclic AMP-Dependent Protein KinasesPterinsUp-RegulationDNA-Binding ProteinsRepressor ProteinsAntisense Elements (Genetics)NG-Nitroarginine Methyl EsterchemistryBucladesineGene Expression RegulationComplement Factor Hbiology.proteinNitric Oxide SynthaseReactive Oxygen SpeciesSignal TransductionBiochemistry
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Characterization of the interaction between Actinin-Associated LIM Protein (ALP) and the rod domain of α-actinin

2009

Abstract Background The PDZ-LIM proteins are a family of signalling adaptors that interact with the actin cross-linking protein, α-actinin, via their PDZ domains or via internal regions between the PDZ and LIM domains. Three of the PDZ-LIM proteins have a conserved 26-residue ZM motif in the internal region, but the structure of the internal region is unknown. Results In this study, using circular dichroism and nuclear magnetic resonance (NMR), we showed that the ALP internal region (residues 107–273) was largely unfolded in solution, but was able to interact with the α-actinin rod domain in vitro, and to co-localize with α-actinin on stress fibres in vivo. NMR analysis revealed that the ti…

Circular dichroismPDZ domaineducationAmino Acid MotifsMolecular Sequence DataPlasma protein bindingActininmacromolecular substancesBiology03 medical and health sciences0302 clinical medicineCell Line TumorHumansActininAmino Acid Sequencelcsh:QH573-671Peptide sequenceActin030304 developmental biologyLIM domainFluorescent Dyes0303 health scienceslcsh:CytologyMicrofilament ProteinsCell BiologyLIM Domain ProteinsSurface Plasmon Resonancemusculoskeletal systemRecombinant ProteinsCell biologyProtein Structure TertiaryLHX3Peptides030217 neurology & neurosurgeryResearch ArticleProtein BindingBMC Cell Biology
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Comparative architectural aspects of regions of conserved synteny on human chromosome 11p15.3 and mouse chromosome 7 (including genes WEE1 and LMO1)

2001

Human chromosome 11p15.3 is associated with chromosome aberrations in the Beckwith Wiedemann Syndrome and implicated in the pathogenesis of different tumor types including lung cancer and leukemias. To date, only single tumor-relevant genes with linkage to this region (e.g. LMO1) have been found suggesting that this region may harbor additional potential disease associated genes. Although this genomic area has been studied for years, the exact order of genes/chromosome markers between D11S572 and the WEE1 gene locus remained unclear. Using the FISH technique and PAC clones of the flanking markers we determined the order of the genomic markers. Based on these clones we established a PAC cont…

Genetic Markerscongenital hereditary and neonatal diseases and abnormalitiesBeckwith–Wiedemann syndromeCell Cycle ProteinsBiologyChromosomesEvolution MolecularContig MappingMiceChromosome regionsGene OrderMetalloproteinsGeneticsmedicineAnimalsHumansCloning MolecularMolecular BiologyGeneConserved SequenceIn Situ Hybridization FluorescenceGenetics (clinical)Repetitive Sequences Nucleic AcidSyntenyOncogene ProteinsGeneticsChromosome 7 (human)Base CompositionChromosomes Human Pair 11Nuclear ProteinsChromosomeSequence Analysis DNALIM Domain ProteinsProtein-Tyrosine Kinasesmedicine.diseaseAT Rich SequenceGC Rich SequenceDNA-Binding ProteinsChromosome 3CpG IslandsChromosome 21Transcription FactorsCytogenetic and Genome Research
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Liver-specific Ldb1 deletion results in enhanced liver cancer development.

2009

Background & Aims LIM-domain-binding (Ldb) proteins have been demonstrated to be essential not only to key embryonic developmental processes but also to carcinogenesis. We have previously demonstrated Ldb1 to be of high biological and developmental relevance, as a targeted deletion of the Ldb1 gene in mice results in an embryonic lethal and pleiotropic phenotype. Methods We have now established a liver-specific Ldb1 knock out to investigate the role of Ldb1 in carcinogenesis, in particular in hepatocellular carcinoma (HCC) development, in vivo . Results These mice demonstrated a significantly enhanced growth of liver cancer by means of tumor size and number, advocating for an essential role…

Liver Stem CellApoptosisMice TransgenicBiologymedicine.disease_causeArticleMiceCyclin D1Liver Neoplasms ExperimentalmedicineAnimalsRNA MessengerRNA NeoplasmOligonucleotide Array Sequence AnalysisMice KnockoutHepatologyOncogeneBase SequenceMicroarray analysis techniquesCancerLIM Domain Proteinsmedicine.diseaseDNA-Binding ProteinsMice Inbred C57BLLiverImmunologyKnockout mouseCancer researchLiver cancerCarcinogenesisJournal of hepatology
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Downregulation and Nuclear Relocation of MLP During the Progression of Right Ventricular Hypertrophy Induced by Chronic Pressure Overload

2000

Abstract The cardiac LIM domain protein MLP plays a crucial role in the architecture and mechanical function of cardiac myocytes. Mice lacking the MLP gene develop cardiac hypertrophy, dilated cardiopathy and heart failure. We investigated whether downregulation of MLP is induced by pressure overload and contributes to the physiopathology of cardiac hypertrophy and failure. We studied this mechanism in rat right ventricles submitted to pulmonary arterial hypertension, because it is known that this ventricle is very vulnerable to the deleterious effects of pressure overload. During the progression of cardiac hypertrophy to failure over a 31 days period there was a dramatic decrease by 50% of…

MaleCytoplasmmedicine.medical_specialtyTime FactorsTranscription GeneticHeart VentriclesDown-RegulationMuscle ProteinsCardiomegalyCytosolMyofibrilsDownregulation and upregulationRight ventricular hypertrophyInternal medicinePressureAnimalsVentricular FunctionMedicineMyocyteRNA MessengerRats WistarLungMolecular BiologyCell NucleusHomeodomain ProteinsPressure overloadReverse Transcriptase Polymerase Chain Reactionbusiness.industryMyocardiumLIM Domain Proteinsmedicine.diseaseImmunohistochemistryPulmonary hypertensionRatsMicroscopy Electronmedicine.anatomical_structureVentricleHeart failureCardiologyCardiology and Cardiovascular MedicinebusinessMyofibrilJournal of Molecular and Cellular Cardiology
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Gene expression profiles of metabolic aggressiveness and tumor recurrence in benign meningioma.

2013

Around 20% of meningiomas histologically benign may be clinically aggressive and recur. This strongly affects management of meningioma patients. There is a need to evaluate the potential aggressiveness of an individual meningioma. Additional criteria for better classification of meningiomas will improve clinical decisions as well as patient follow up strategy after surgery. The aim of this study was to determine the relationship between gene expression profiles and new metabolic subgroups of benign meningioma with potential clinical relevance. Forty benign and fourteen atypical meningioma tissue samples were included in the study. We obtained metabolic profiles by NMR and recurrence after s…

MalePathologyNon-Clinical MedicineAngiogenesisGene Expressionlcsh:MedicineTranscriptomeGene expressionMolecular Cell BiologyPathologyMeningeal NeoplasmsCluster Analysislcsh:ScienceNeurological TumorsNeuropathologyAged 80 and overMultidisciplinaryLIM Domain ProteinsMiddle AgedUp-RegulationGene Expression Regulation NeoplasticReal-time polymerase chain reactionOncologyMedicineFemaleMeningiomaResearch ArticleAdultmedicine.medical_specialtyBiologyReal-Time Polymerase Chain ReactionMeningiomaDiagnostic MedicinemedicineGeneticsCancer Detection and DiagnosisBiomarkers Tumorotorhinolaryngologic diseasesHumansMeningeal NeoplasmClinical significanceBiologyneoplasmsAdaptor Proteins Signal TransducingAgedHealth Care Policylcsh:RHealth Risk AnalysisCancers and NeoplasmsMolecular Sequence Annotationmedicine.diseasenervous system diseasesAnatomical PathologyBenign Meningiomalcsh:QNeoplasm Recurrence LocalTranscriptomePLoS ONE
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Proteomic identification of FHL1 as the protein mutated in human reducing body myopathy

2007

Reducing body myopathy (RBM) is a rare disorder causing progressive muscular weakness characterized by aggresome-like inclusions in the myofibrils. Identification of genes responsible for RBM by traditional genetic approaches has been impossible due to the frequently sporadic occurrence in affected patients and small family sizes. As an alternative approach to gene identification, we used laser microdissection of intracytoplasmic inclusions identified in patient muscle biopsies, followed by nanoflow liquid chromatography-tandem mass spectrometry and proteomic analysis. The most prominent component of the inclusions was the Xq26.3-encoded four and a half LIM domain 1 (FHL1) protein, expresse…

Models MolecularProteomicsMolecular Sequence DataMuscle ProteinsBiologyTransfectionProteomicsInclusion bodiesMuscular DiseasesmedicineAmino Acid SequenceLaser capture microdissectionInclusion BodiesIntracellular Signaling Peptides and ProteinsCardiac muscleSkeletal muscleGenetic Diseases X-LinkedGeneral MedicineLIM Domain Proteinsmedicine.diseaseCongenital myopathyMolecular biologyFHL1medicine.anatomical_structureMutationMyofibrilResearch Article
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Zasp/Cypher internal ZM-motif containing fragments are sufficient to co-localize with α-actinin—Analysis of patient mutations

2005

Z-band alternatively spliced PDZ-containing protein (ZASP/Cypher) has an important role in maintaining Z-disc stability in striated and cardiac muscle. ZASP/Cypher interacts through its PDZ domain with the major Z-disc actin cross-linker, alpha-actinin. ZASP/Cypher also has a conserved sequence called the ZM-motif, and it is found in two alternatively spliced exons 4 and 6. We have shown earlier that the ZM-motif containing internal regions of two related proteins ALP and CLP36 interact with alpha-actinin rod region, and that the ZM-motif is important in targeting ALP to the alpha-actinin containing structures in cell. Here, we show that the ZASP/Cypher internal fragments containing either …

SarcomeresAmino Acid MotifsPDZ domainCHO Cellsmacromolecular substancesBiologyConserved sequenceStress fiber assemblyMyoblastsMiceExonCricetinaeStress FibersmedicineAnimalsHumansMyocyteActininMuscle SkeletalActinAdaptor Proteins Signal TransducingOrganellesGeneticsMyocardiumPoint mutationCardiac muscleExonsIntracellular MembranesCell BiologyLIM Domain Proteinsmusculoskeletal systemPeptide FragmentsCell biologymedicine.anatomical_structureMutationCardiomyopathiesProtein BindingExperimental Cell Research
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