Search results for "gtp-binding"

showing 10 items of 178 documents

Mutations in ARL2BP, Encoding ADP-Ribosylation-Factor-Like 2 Binding Protein, Cause Autosomal-Recessive Retinitis Pigmentosa

2013

Retinitis pigmentosa (RP) is a genetically heterogeneous retinal degeneration characterized by photoreceptor death, which results in visual failure. Here, we used a combination of homozygosity mapping and exome sequencing to identify mutations in ARL2BP, which encodes an effector protein of the small GTPases ARL2 and ARL3, as causative for autosomal-recessive RP (RP66). In a family affected by RP and situs inversus, a homozygous, splice-acceptor mutation, c.101−1G>C, which alters pre-mRNA splicing of ARLBP2 in blood RNA, was identified. In another family, a homozygous c.134T>G (p.Met45Arg) mutation was identified. In the mouse retina, ARL2BP localized to the basal body and cilium-associated…

AdultMaleRetinal degenerationCentrioleMolecular Sequence DataGenes RecessiveBiologymedicine.disease_causeMice03 medical and health sciences0302 clinical medicineBardet–Biedl syndromeGTP-Binding ProteinsReportRetinitis pigmentosaGeneticsmedicineAnimalsHumansBasal bodyGenetics(clinical)Photoreceptor CellsGenetics (clinical)030304 developmental biologyPrimary ciliary dyskinesiaGenetics0303 health sciencesMutationBase SequenceADP-Ribosylation FactorsCiliumHomozygoteMembrane Transport ProteinsEpithelial Cellsmedicine.diseasePedigreeCell biologyMutationFemalesense organsCarrier ProteinsRetinitis Pigmentosa030217 neurology & neurosurgeryProtein BindingTranscription FactorsThe American Journal of Human Genetics
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Urine cadmium levels and albuminuria in a general population from Spain: A gene-environment interaction analysis

2017

Background: The interaction of cadmium with genes involved in oxidative stress, cadmium metabolism and transport pathways on albuminuria can provide biological insight on the relationship between cadmium and albuminuria at low exposure levels. Objectives: We tested the hypothesis that specific genotypes in candidate genes may confer increased susceptibility to cadmium exposure. Methods: Cadmium exposure was estimated by inductively coupled plasma mass spectrometry (ICPMS) in urine from 1397 men and women aged 18–85years participating in the Hortega Study, a representative sample of a general population from Spain. Urine albumin was measured by automated nephelometric immunochemistry. Abnorm…

AdultMalerac1 GTP-Binding Protein0301 basic medicinemedicine.medical_specialtyAdolescentPopulationchemistry.chemical_elementUrine010501 environmental sciences01 natural sciencesYoung Adult03 medical and health scienceschemistry.chemical_compoundInternal medicineDiabetes mellitusPrevalencemedicineAlbuminuriaHumanseducationCation Transport Proteinslcsh:Environmental sciencesAged0105 earth and related environmental sciencesGeneral Environmental Sciencelcsh:GE1-350Aged 80 and overCreatinineCadmiumeducation.field_of_studybusiness.industryOdds ratioMiddle Agedmedicine.diseaseOxidative Stress030104 developmental biologyEndocrinologychemistrySpainCreatinineAlbuminuriaEnvironmental PollutantsFemaleGene-Environment Interactionmedicine.symptombusinessCadmiumKidney diseaseEnvironment International
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Transglutaminase Type II Plays a Protective Role in Hepatic Injury

2003

The up-regulation of "tissue" transglutaminase (TG2) gene has been shown to occur in various pathologies and can lead to severe liver injury; however, its role in the onset of liver damage has not yet been clarified. To address this issue, we have used two experimental settings: carbon tetrachloride (CCl(4))-induced liver injury in wild-type and TG2 knockout mice; and liver biopsies obtained from a large cohort of hepatitis C virus (HCV)-infected patients. Mice lacking TG2 failed to clear the hepatic necrotic tissue formed in response to prolonged CCl(4) exposure (5 weeks) and 60% of them died before the end of the treatment. By contrast, wild-type mice were able to recover after the toxic …

AdultPathologymedicine.medical_specialtyNecrosisGenotypeTissue transglutaminaseHepatitis C virusCCL4medicine.disease_causeGene Expression Regulation EnzymologicPathology and Forensic MedicineExtracellular matrixMiceNecrosisGTP-Binding ProteinsmedicineAnimalsHumansProtein Glutamine gamma Glutamyltransferase 2Mice KnockoutHepatitisLiver injuryTransglutaminasesbiologyCarbon Tetrachloride PoisoningHepatitis C ChronicMiddle Agedmedicine.diseaseMice Inbred C57BLLiverKnockout mousebiology.proteinmedicine.symptomRegular ArticlesThe American Journal of Pathology
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Agonist potency differentiates G protein activation and Ca2+ signalling by the orexin receptor type 1.

2005

The G protein coupling characteristics of a flag epitope-tagged orexin receptor type 1 (OX1R) was investigated in HEK293 cells. Immunoprecipitation of the OX1R and immunoblotting revealed interactions with Gq/G11 proteins as well as with Gs and Gi proteins. Stimulation with orexin-A did not affect the ability of the OX1R to coprecipitate Gq/G11 proteins, but it robustly elevated the intracellular concentration of Ca2+, [Ca2+]i. No changes in cAMP levels could be detected upon receptor stimulation. To get further insight into the functional correlation of G protein activation and Ca2+ signalling, we used baculovirus transduction to express chimeric G proteins, containing the Galphas protein …

AgonistReceptors Neuropeptidemedicine.drug_classG proteinBiologyKidneyBiochemistryCell LineReceptors G-Protein-CoupledGTP-binding protein regulatorsGTP-Binding ProteinsOrexin ReceptorsTransduction GeneticMuscarinic acetylcholine receptormedicineCyclic AMPHumansCalcium SignalingPharmacologyReceptor Muscarinic M3Neurotransmitter AgentsOrexinsDose-Response Relationship DrugNeuropeptidesIntracellular Signaling Peptides and ProteinsMuscarinic acetylcholine receptor M3Fusion proteinOrexin receptorCell biologyBiochemistryCalciumSignal transductionBaculoviridaeSignal TransductionBiochemical pharmacology
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Induction of Transglutaminase 2 by a Liver X Receptor/Retinoic Acid Receptor α Pathway Increases the Clearance of Apoptotic Cells by Human Macrophages

2009

Rationale: Liver X receptors (LXRs) are oxysterol-activated nuclear receptors that are involved in the control of cholesterol homeostasis and inflammatory response. Human monocytes and macrophages express high levels of these receptors and are appropriate cells to study the response to LXR agonists. Objective: The purpose of this study was to identify new LXR targets in human primary monocytes and macrophages and the consequences of their activation. Methods and Results: We show that LXR agonists significantly increase the mRNA and protein levels of the retinoic acid receptor (RAR)α in primary monocytes and macrophages. LXR agonists promote RARα gene transcription through binding to a spec…

Agonistmedicine.medical_specialtyReceptors Retinoic AcidPhysiologymedicine.drug_classResponse elementReceptors Cytoplasmic and NuclearApoptosisBiologyCell LinePhagocytosisGTP-Binding ProteinsInternal medicinemedicineHumansMacrophageProtein Glutamine gamma Glutamyltransferase 2ReceptorLiver X receptorLiver X ReceptorsTransglutaminasesMacrophagesRetinoic Acid Receptor alphaMacrophage ActivationAtherosclerosisOrphan Nuclear ReceptorsCell biologyDNA-Binding ProteinsRetinoic acid receptorEndocrinologyNuclear receptorRetinoic acid receptor alphaEnzyme InductionCardiology and Cardiovascular MedicineCirculation Research
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Simultaneous stimulation of GABA and beta adrenergic receptors stabilizes isotypes of activated adenylyl cyclase heterocomplex

2004

Abstract Background We investigated how the synthesis of cAMP, stimulated by isoproterenol acting through β-adrenoreceptors and Gs, is strongly amplified by simultaneous incubation with baclofen. Baclofen is an agonist of δ-aminobutyric acid type B receptors [GABAB], known to inhibit adenylyl cyclase via Gi. Because these agents have opposite effects on cAMP levels, the unexpected increase in cAMP synthesis when they are applied simultaneously has been intensively investigated. From previous reports, it appears that cyclase type II contributes most significantly to this phenomenon. Results We found that simultaneous application of isoproterenol and baclofen specifically influences the assoc…

Baclofenlcsh:CytologyGTP-Binding Protein beta SubunitsIsoproterenolAdrenergic beta-AgonistsRatsIsoenzymesRats Sprague-DawleyReceptors GABAGTP-Binding Protein gamma SubunitsMultiprotein ComplexesReceptors Adrenergic betaSynapsesCyclic AMPGTP-Binding Protein alpha Subunits GsAnimalslcsh:QH573-671GABA AgonistsResearch ArticleAdenylyl CyclasesSignal TransductionBMC Cell Biology
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Small GTP-binding proteins of the Rho- and Ras-subfamilies are not involved in the actin rearrangements induced by attaching and effacingEscherichia …

1998

Attaching and effacing Escherichia coli (AEEC) are extracellular pathogens that induce the formation of actin-rich structures at their sites of attachment to eukaryotic host cells. We analysed whether small GTP-binding proteins of the Rho- and Ras-subfamilies, which control the cellular actin system, are essential for these bacterial-induced microfilament reorganizations. For this purpose we specifically inactivated them using the Clostridium difficile toxins TcdB-10463 and TcdB-1470. Such treatment led to a dramatic breakdown of the normal actin cytoskeleton, but did not abrogate the bacterial-induced actin rearrangements. Our data therefore indicate that the microfilament reorganizations …

Bacterial ToxinsExotoxinsArp2/3 complexmacromolecular substancesShiga ToxinsMicrofilamentMicrobiologyGTP-Binding ProteinsEscherichia coliGeneticsAnimalsHumansActin-binding proteinCytoskeletonMolecular BiologyActinbiologyClostridioides difficileActin remodelingActin cytoskeletonActinsActin CytoskeletonMicroscopy ElectronBiochemistryMicroscopy Electron Scanningras Proteinsbiology.proteinCattleMDia1HeLa CellsFEMS Microbiology Letters
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Delineation of the catalytic domain of Clostridium difficile toxin B-10463 to an enzymatically active N-terminal 467 amino acid fragment.

2006

Abstract In an attempt to directly approach the postulated toxic domain of Clostridium difficile 's TcdB-10463, eight subclones of different size and locations in the N-terminal third of the toxin were generated. Expression of these toxin fragments was checked in Western blots and the enzymatic activity of the expressed proteins was analyzed by glucosylating Ras related small GTP-binding proteins. Two polypeptides of 875 aa (TcdBc1–3) and 557 aa (TcdBc1-H) glucosylated their targets Rho, Rac and Cdc42 with the same activity and specificity as the holotoxin. In comparison 516 aa (TcdBc1-N) and 467 aa (TcdBc1-A) protein fragments exhibited highly reduced activity, while Tcdc1 and TcdB2–3 (aa …

Bacterial ToxinsMolecular Sequence DataClostridium difficile toxin Bmedicine.disease_causeMicrobiologyStructure-Activity RelationshipGTP-binding protein regulatorsClostridiumBacterial ProteinsGeneticsmedicineMolecular Biologychemistry.chemical_classificationBinding SitesbiologyBase SequenceToxinbiology.organism_classificationMolecular biologyPeptide FragmentsRecombinant ProteinsAmino acidEnzymechemistryCdc42 GTP-Binding ProteinBiochemistryGlucosyltransferasesbiology.proteinGlucosyltransferaseFEMS microbiology letters
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Biphasic Erk1/2 activation sequentially involving Gs and Gi signaling is required in beta3-adrenergic receptor-induced primary smooth muscle cell pro…

2013

Abstract The beta3 adrenergic receptor (B3-AR) reportedly induces cell proliferation, but the signaling pathways that were proposed, involving either Gs or Gi coupling, remain controversial. To further investigate the role of G protein coupling in B3-AR induced proliferation, we stimulated primary human myometrial smooth muscle cells with SAR150640 (B3-AR agonist) in the absence or presence of variable G-protein inhibitors. Specific B3-AR stimulation led to an Erk1/2 induced proliferation. We observed that the proliferative effects of B3-AR require two Erk1/2 activation peaks (the first after 3 min, the second at 8 h). Erk1/2 activation at 3 min was mimicked by forskolin (adenylyl-cyclase a…

Beta-3 adrenergic receptorGs alpha subunitMAP Kinase Signaling SystemMyocytes Smooth MuscleProliferationG protein coupled receptorBiologyGTP-Binding Protein alpha Subunits Gi-GoPertussis toxinchemistry.chemical_compoundErk1/2Protein kinasesCyclinsReceptors Adrenergic betaGTP-Binding Protein alpha Subunits GsHumansMolecular BiologyPI3K/AKT/mTOR pathwayCells CulturedG protein-coupled receptorCell ProliferationForskolinColforsinBeta-3 adrenergic receptorCell BiologyCell biologychemistryGene Expression RegulationPertussis ToxinMyometriumFemaleSignal transductionProto-oncogene tyrosine-protein kinase SrcBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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Phosphorylation of CalDAG-GEFI by protein kinase A prevents Rap1b activation.

2013

Summary Background Signaling via protein kinase A (PKA) and protein kinase G (PKG) is critical for maintaining platelets in the resting state. Both kinases down-regulate the activity of the small GTPase Rap1b, a critical signaling switch for integrin activation and platelet aggregation. However, the mechanism of Rap1b regulation by PKA and PKG is largely unknown. Objective To identify the PKA phosphorylation sites in calcium and diacylglycerol-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), the main GEF for Rap1b in platelets, and the effect of CalDAG-GEFI phosphorylation in Rap1b activation. Methods The phosphorylation sites in CalDAG-GEFI were identified by radio-active phos…

Blood PlateletsPlatelet AggregationMolecular Sequence DataBiologyMass SpectrometryPhosphorylation cascadeCyclic AMPGuanine Nucleotide Exchange FactorsHumansImmunoprecipitationProtein phosphorylationAmino Acid SequenceCalcium SignalingPhosphorylationProtein kinase ACalcium signalingAlanineSequence Homology Amino AcidKinaseHematologyCyclic AMP-Dependent Protein KinasesEnzyme Activationrab1 GTP-Binding ProteinsHEK293 CellsBiochemistryMutationPhosphorylationGuanine nucleotide exchange factorGuanosine TriphosphatecGMP-dependent protein kinasePlasmidsSignal TransductionJournal of thrombosis and haemostasis : JTH
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