Search results for "Leucine-Rich Repeat Serine-Threonine Protein Kinase-2"

showing 5 items of 5 documents

Autophagy in the pathogenesis of ankylosing spondylitis

2016

The pathogenesis of ankylosing spondylitis (AS) is not well understood, and treatment options have met with limited success. Autophagy is a highly conserved mechanism of controlled digestion of damaged organelles within a cell. It helps in the maintenance of cellular homeostasis. The process of autophagy requires the formation of an isolation membrane. They form double-membraned vesicles called “autophagosomes” that engulf a portion of the cytoplasm. Beyond the role in maintenance of cellular homeostasis, autophagy has been demonstrated as one of the most remarkable tools employed by the host cellular defense against bacteria invasion. Autophagy also affects the immune system and thus is im…

0301 basic medicineCellAutophagy-Related ProteinsATG16L1Cellular homeostasisInflammationBiologyLeucine-Rich Repeat Serine-Threonine Protein Kinase-2Pathogenesis03 medical and health sciencesImmune systemRheumatologyATG16L1; Autophagy; Inflammation; LRRK2; Pathogenesis; Spondyloarthritis; RheumatologyPathogenesiAutophagymedicineHomeostasisHumansSpondylitis AnkylosingATG16L1InflammationAutophagyLRRK2General MedicineCell biology030104 developmental biologymedicine.anatomical_structureCytoplasmSpondyloarthritimedicine.symptomClinical Rheumatology
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Human R1441C LRRK2 regulates the synaptic vesicle proteome and phosphoproteome in a Drosophila model of Parkinson's disease

2016

International audience; Mutations in leucine-rich repeat kinase 2 (LRRK2) cause late-onset, autosomal dominant familial Parkinsons disease (PD) and variation at the LRRK2 locus contributes to the risk for idiopathic PD. LRRK2 can function as a protein kinase and mutations lead to increased kinase activity. To elucidate the pathophysiological mechanism of the R1441C mutation in the GTPase domain of LRRK2, we expressed human wild-type or R1441C LRRK2 in dopaminergic neurons of Drosophila and observe reduced locomotor activity, impaired survival and an age-dependent degeneration of dopaminergic neurons thereby creating a new PD-like model. To explore the function of LRRK2 variants in vivo, we …

0301 basic medicineProteomerab3 GTP-Binding Proteinsalpha-synucleindomainSyntaxin 1Interactomedopaminergic-neuronsAnimals Genetically Modifiedchemistry.chemical_compound0302 clinical medicinemicrotubule stabilityDrosophila ProteinsProtein Interaction MapsGenetics (clinical)LRRK2 GeneKinasephosphorylationBrainParkinson DiseaseArticlesGeneral Medicineautosomal-dominant parkinsonismLRRK2Drosophila melanogasterSynaptotagmin IProteomePhosphorylationSynaptic VesiclesNerve Tissue ProteinsBiologyLeucine-Rich Repeat Serine-Threonine Protein Kinase-203 medical and health sciencesGeneticsAnimalsHumansKinase activitygeneMolecular BiologyAlpha-synucleingtp-bindingDopaminergic Neuronsrepeat kinase 2Molecular biologyPhosphoric Monoester Hydrolasesnervous system diseasesDisease Models Animal030104 developmental biologyGene Expression Regulationchemistrymutation030217 neurology & neurosurgery[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
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Myocardial 123metaiodobenzylguanidine uptake in genetic Parkinson's disease.

2008

Myocardial (123)Metaiodobenzylguanidine (MIBG) enables the assessment of postganglionic sympathetic cardiac innervation. MIBG uptake is decreased in nearly all patients with Parkinson's disease (PD). Our objective was to evaluate MIBG uptake in patients with genetic PD. We investigated MIBG uptake in 14 patients with PD associated with mutations in different genes (Parkin, DJ-1, PINK], and leucine-rich repeat kinase 2 -LRRK2), in 15 patients with idiopathic PD, and 10 control subjects. The myocardial MIGB uptake was preserved in 3 of the 4 Parkin-associated Parkinsonisms, in I of the 2 patients with DJ-1 mutations, in 1 of the 2 brothers with PINK] mutations, in 3 of the 6 unrelated patient…

AdultMalemedicine.medical_specialtyParkinson's diseaseGenotypeUbiquitin-Protein LigasesDNA Mutational AnalysisProtein Deglycase DJ-1PINK1Gene mutationProtein Serine-Threonine Kinasesmedicine.disease_causeLeucine-Rich Repeat Serine-Threonine Protein Kinase-2Severity of Illness IndexParkinCentral nervous system diseaseDiagnosis DifferentialDegenerative diseaseParkinsonian DisordersInternal medicineSurveys and QuestionnairesmedicineHumansPoint MutationPromoter Regions GeneticGenetic PD Myocardial scintigraphyOncogene ProteinsTomography Emission-Computed Single-PhotonMutationMovement Disordersbusiness.industryMyocardiumIntracellular Signaling Peptides and ProteinsParkinson DiseaseGalvanic Skin ResponseMiddle Agedmedicine.diseaseLRRK2nervous system diseases3-IodobenzylguanidineEndocrinologyNeurologySettore MED/26 - NeurologiaFemaleNeurology (clinical)RadiopharmaceuticalsbusinessProtein KinasesMovement disorders : official journal of the Movement Disorder Society
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LRRK2 is expressed in areas affected by Parkinson's disease in the adult mouse brain.

2006

The leucine-rich repeat kinase 2 (LRRK2) gene was recently found to have multiple mutations that are causative for autosomal dominant inherited Parkinson's disease (PD). Previously, we used Northern blot analysis to show that this gene was expressed in the cerebellum, cerebral cortex, medulla, spinal cord, occipital pole, frontal lobe, temporal lobe and caudate putamen. However, a more comprehensive map of LRRK2 mRNA localization in the central nervous system is still lacking. In this study we have mapped the distribution of the mRNA encoding for LRRK2 using nonradioactive in situ hybridization. We detected a moderate expression of this PD-related gene throughout the adult B2B6 mouse brain.…

Cingulate cortexMaleCerebellumGene ExpressionSubstantia nigraHippocampal formationBiologyProtein Serine-Threonine KinasesLeucine-Rich Repeat Serine-Threonine Protein Kinase-2Temporal lobeMicePiriform cortexmedicineAnimalsRNA MessengerIn Situ HybridizationBrain MappingGeneral NeuroscienceBrainParkinson Diseasenervous system diseasesDisease Models Animalmedicine.anatomical_structurenervous systemFrontal lobeCerebral cortexNeuroscienceThe European journal of neuroscience
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The Parkinson Disease Gene LRRK2: Evolutionary and Structural Insights

2006

Mutations in the human leucine-rich repeat kinase 2 (LRRK2) gene are associated with both familial and sporadic Parkinson disease (PD). LRRK2 belongs to a gene family known as Roco. Roco genes encode for large proteins with several protein domains. Particularly, all Roco proteins have a characteristic GTPase domain, named Roc, plus a domain of unknown function called COR. In addition, LRRK2 and several other Roco proteins also contain a protein kinase domain. In this study, I use a combination of phylogenetic and structural analyses of the COR, Roc, and kinase domains present in Roco proteins to describe the origin and evolutionary history of LRRK2. Phylogenetic analyses using these domains…

Models MolecularProtein ConformationMolecular Sequence DataProtein domainGTPaseProtein Serine-Threonine KinasesBiologyLeucine-Rich Repeat Serine-Threonine Protein Kinase-2MAP3K7SH3 domainGTP PhosphohydrolasesEvolution MolecularGeneticsAnimalsHumansDictyosteliumAmino Acid Sequencec-RafMolecular BiologyPhylogenyEcology Evolution Behavior and SystematicsGeneticsSequence Homology Amino AcidParkinson DiseaseLRRK2Protein Structure Tertiarynervous system diseasesDisease Models AnimalProtein kinase domainRabProtein KinasesMolecular Biology and Evolution
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