Search results for "Protein Subunits"

showing 10 items of 77 documents

ß-COP mutants show specific high sensitivity to chloride ions.

2021

Coat Protein I (COPI) consists of a complex (coatomer) formed by seven subunits (α-, β-, β’-, γ-, δ-, ε-, and ζ-COP) that is recruited to Golgi membranes to form vesicles that shuttle from the Golgi apparatus to the ER and between Golgi stacks. Recently, it has been described that loss of function mutants of the two Arabidopsis β-COP genes, β1-COP and β2-COP, showed increased sensitivity to salt stress (NaCl). Using a mixture of either Na(+) or Cl(−) salts, we have now found that β-COP mutants are specifically and highly sensitive to chloride ions.

0106 biological sciences0301 basic medicineShort CommunicationMutantArabidopsisSalt (chemistry)Plant ScienceBiology01 natural sciencesChlorideCoatomer Protein03 medical and health sciencessymbols.namesakeChloridesArabidopsismedicinechemistry.chemical_classificationIonsVesicleCOPIGolgi apparatusbiology.organism_classificationhumanitiesProtein Subunits030104 developmental biologyPhenotypechemistryCoatomerMutationsymbolsBiophysics010606 plant biology & botanymedicine.drugProtein BindingPlant signalingbehavior
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Novel KIAA1033/WASHC4 mutations in three patients with syndromic intellectual disability and a review of the literature.

2019

In 2011, KIAA1033/WASHC4 was associated with autosomal recessive intellectual disability (ARID) in a large consanguineous family comprising seven affected individuals with moderate ID and short stature. Since then, no other cases of KIAA1033 variants have been reported. Here we describe three additional patients (from two unrelated families) with syndromic ID due to compound heterozygous KIAA1033 variants ascertained by exome sequencing (ES). Two sisters, aged 4 and 5.5 years, had a stop-gain and a missense variants, each inherited from one parent (p.(Gln442*) and p.(Asp1048Gly)). Both had learning disabilities, macrocephaly, dysmorphic features, skeletal anomalies, and subependymal heterot…

0301 basic medicineAdultMaleMicrocephaly030105 genetics & heredityCompound heterozygosityShort stature03 medical and health sciencesKIAA0196Intellectual DisabilityIntellectual disabilityGeneticsMedicineMissense mutationHumansGenetics (clinical)Exome sequencingGeneticsbusiness.industryMacrocephalyInfant NewbornIntracellular Signaling Peptides and Proteinsmedicine.diseasePedigreeProtein Subunits030104 developmental biologyPhenotypeChild PreschoolMutationFemalemedicine.symptombusinessAmerican journal of medical genetics. Part AREFERENCES
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Endothelial cell damage is the central part of COVID-19 and a mouse model induced by injection of the S1 subunit of the spike protein☆

2021

Neurologic complications of symptomatic COVID-19 are common. Brain tissues from 13 autopsies of people who died of COVID-19 were examined. Cultured endothelial and neuronal cells were incubated with and wild type mice were injected IV with different spike subunits. In situ analyses were used to detect SARS-CoV-2 proteins and the host response. In 13/13 brains from fatal COVID-19, pseudovirions (spike, envelope, and membrane proteins without viral RNA) were present in the endothelia of microvessels ranging from 0 to 14 positive cells/200× field (mean 4.3). The pseudovirions strongly co-localized with caspase-3, ACE2, IL6, TNFα, and C5b-9. The surrounding neurons demonstrated increased NMDAR2…

0301 basic medicineAdultMalePathologymedicine.medical_specialtyProtein subunitH&E stainCaspase 3Spike proteinThirstPathology and Forensic Medicine03 medical and health sciencesMice0302 clinical medicineS1 subunitmedicineAnimalsHumansAgedAged 80 and overChemistrySARS-CoV-2COVID-19Endothelial CellsGeneral MedicineOriginal ContributionMiddle AgedMolecular biologyEndothelial stem cellDisease Models AnimalProtein Subunits030104 developmental biologyMembrane protein030220 oncology & carcinogenesisMicrovesselsSpike Glycoprotein CoronavirusImmunohistochemistryRNA ViralTumor necrosis factor alphaFemaleAutopsymedicine.symptomAnnals of Diagnostic Pathology
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Diversity, evolution, and function of myriapod hemocyanins.

2018

Background Hemocyanin transports O2 in the hemolymph of many arthropod species. Such respiratory proteins have long been considered unnecessary in Myriapoda. As a result, the presence of hemocyanin in Myriapoda has long been overlooked. We analyzed transcriptome and genome sequences from all major myriapod taxa – Chilopoda, Diplopoda, Symphyla, and Pauropoda – with the aim of identifying hemocyanin-like proteins. Results We investigated the genomes and transcriptomes of 56 myriapod species and identified 46 novel full-length hemocyanin subunit sequences in 20 species of Chilopoda, Diplopoda, and Symphyla, but not Pauropoda. We found in Cleidogona sp. (Diplopoda, Chordeumatida) a hemocyanin-…

0301 basic medicineArthropodaEvolutionmedicine.medical_treatmentMyriapodaZoologychemical and pharmacologic phenomenacomplex mixturesHemocyaninPauropodaEvolution Molecular03 medical and health sciencesHemolymphmedicineQH359-425AnimalsAmino Acid SequenceRNA MessengerArthropodsEcology Evolution Behavior and SystematicsPhylogenyBinding SitesbiologyBase SequenceMonophenol MonooxygenaseMyriapodaGenetic VariationHemocyaninhemic and immune systemsbiology.organism_classificationRespiratory proteinOxygenProtein Subunits030104 developmental biologyHemocyaninsPhenoloxidaseSubunit diversityArthropodSymphylaCentipedeCopperResearch ArticleBMC evolutionary biology
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Singular Location and Signaling Profile of Adenosine A2A-Cannabinoid CB1 Receptor Heteromers in the Dorsal Striatum

2018

The dorsal striatum is a key node for many neurobiological processes such as motor activity, cognitive functions, and affective processes. The proper functioning of striatal neurons relies critically on metabotropic receptors. Specifically, the main adenosine and endocannabinoid receptors present in the striatum, ie, adenosine A(2A) receptor (A(2A)R) and cannabinoid CB1 receptor (CB1R), are of pivotal importance in the control of neuronal excitability. Facilitatory and inhibitory functional interactions between striatal A(2A)R and CB1R have been reported, and evidence supports that this cross-talk may rely, at least in part, on the formation of A(2A)R-CB1R heteromeric complexes. However, th…

0301 basic medicineCannabinoid receptorAdenosineReceptor Adenosine A2Amedicine.medical_treatmentAdenosinaAdenosine A2A receptormediated inhibitionStriatumBiologyhuntingtons-disease micecannabinoid CB1Mice03 medical and health sciencesglutamatergic neurotransmission0302 clinical medicineReceptor Cannabinoid CB1NeurobiologyNeural PathwaysBasal gangliamedicineAnimalsHumansendocannabinoid systemGenetically modified animalProtein Structure QuaternaryA(2A) receptorsPharmacologyEndocannabinoid systemCorpus Striatumprotein-coupled receptorsProtein SubunitsPsychiatry and Mental healthtransgenic mouse modelHuntington Disease030104 developmental biologyMetabotropic receptornervous systembasal gangliaCannabinoidallosteric interactionsNeuroscience030217 neurology & neurosurgeryNeurobiologiaSignal Transduction
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Comparison of hemolytic activity of the intermediate subunit of Entamoeba histolytica and Entamoeba dispar lectins.

2017

Galactose and N-acetyl-D-galactosamine-inhibitable lectin of Entamoeba histolytica has roles in pathogenicity and induction of protective immunity in rodent models of amoebiasis. Recently, the intermediate subunit of the lectin, Igl1, of E. histolytica has been shown to have hemolytic activity. However, the corresponding lectin is also expressed in a non-virulent species, Entamoeba dispar, and another subunit, Igl2, is expressed in the protozoa. Therefore, in this study, we compared the activities of Igl1 and Igl2 subunits from E. histolytica and E. dispar using various regions of recombinant Igl proteins expressed in Escherichia coli. The recombinant E. dispar Igl proteins had comparable h…

0301 basic medicineErythrocytesTime Factorslcsh:MedicineProtein Sequencingmedicine.disease_causePathology and Laboratory MedicineBiochemistrylaw.inventionEntamoebafluids and secretionslawLectinsMedicine and Health SciencesRecombinant Protein Purificationlcsh:ScienceProtozoansMultidisciplinarybiologyPseudomonas AeruginosaRecombinant ProteinsBacterial PathogensMedical MicrobiologyRecombinant DNAPathogensResearch ArticleProtein PurificationProtein subunitDisparResearch and Analysis MethodsReal-Time Polymerase Chain ReactionMicrobiologyHemolysisMicrobiologyEntamoeba Histolytica03 medical and health sciencesEntamoeba histolyticaPseudomonasParasite Groupsparasitic diseasesmedicineAnimalsTrophozoitesHemoglobinGene SilencingHorsesMolecular Biology TechniquesSequencing TechniquesEscherichia coliMolecular BiologyMicrobial PathogensBacterialcsh:REntamoebaOrganismsLectinBiology and Life SciencesProteinsbiology.organism_classificationParasitic Protozoansdigestive system diseasesProtein Subunits030104 developmental biologybiology.proteinProtozoaParasitologylcsh:QApicomplexaPurification TechniquesPLoS ONE
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Differential role of interleukin-1β in neuroinflammation-induced impairment of spatial and nonspatial memory in hyperammonemic rats.

2019

Activated microglia and increased brain IL-1β play a main role in cognitive impairment in much pathology. We studied the role of IL-1β in neuroinflammation-induced impairment of the following different types of learning and memory: novel object recognition (NOR), novel object location (NOL), spatial learning, reference memory (RM), and working memory (WM). All these processes are impaired in hyperammonemic rats. We assessed which of these types of learning and memory are restored by blocking the IL-1 receptor in vivo in hyperammonemic rats and the possible mechanisms involved. Blocking the IL-1 receptor reversed microglial activation in the hippocampus, perirhinal cortex, and prefrontal cor…

0301 basic medicineMaleInterleukin-1betaPostrhinal cortexHippocampusBiochemistryHippocampusReceptors N-Methyl-D-Aspartate03 medical and health sciences0302 clinical medicineReceptors GABAAmmoniaMemoryPerirhinal cortexGeneticsmedicineMemory impairmentAnimalsHyperammonemiaReceptors AMPARats WistarPrefrontal cortexMolecular BiologyNeuroinflammationCerebral CortexInflammationMicrogliabusiness.industryWorking memoryAnimal FeedRatsInterleukin 1 Receptor Antagonist ProteinProtein Subunits030104 developmental biologymedicine.anatomical_structureGene Expression RegulationReceptors GlutamateMicrogliabusinessNeuroscience030217 neurology & neurosurgeryBiotechnologyFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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Dopaminergic-GABAergic interplay and alcohol binge drinking

2019

© 2019 Elsevier Ltd The dopamine D 3 receptor (D 3 R), in the nucleus accumbens (NAc), plays an important role in alcohol reward mechanisms. The major neuronal type within the NAc is the GABAergic medium spiny neuron (MSN), whose activity is regulated by dopaminergic inputs. We previously reported that genetic deletion or pharmacological blockade of D 3 R increases GABA A α6 subunit in the ventral striatum. Here we tested the hypothesis that D 3 R-dependent changes in GABA A α6 subunit in the NAc affect voluntary alcohol intake, by influencing the inhibitory transmission of MSNs. We performed in vivo and ex vivo experiments in D 3 R knockout (D 3 R −/− ) mice and wild type littermates (D 3 …

0301 basic medicineMalemedicine.medical_specialtyDopaminergic-GABAergicSettore BIO/09 - FISIOLOGIAAlpha6 subunit; Dopamine D3 receptor; Ethanol; Furosemide (PubChem CID: 3440); GABA(A)receptor; Nucleus accumbens; Ro 15-4513; Ro 15-4513 (PubChem CID: 5081); SB 277011A (PubChem CID: 75358288)Alpha6 subunitNucleus accumbensMedium spiny neuronInhibitory postsynaptic potentialNucleus AccumbensBinge Drinking03 medical and health sciencesMiceDopamine D3 receptor0302 clinical medicineDopamine receptor D3Internal medicinemedicineAnimalsFurosemide (PubChem CID: 3440)Nucleus accumbenPharmacology & PharmacyRNA MessengerRo 15-4513GABAergic NeuronsSB 277011A (PubChem CID: 75358288).PharmacologyMice KnockoutEthanolGABAA receptorChemistryDopaminergicAntagonistReceptors Dopamine D3Receptors GABA-ARo 15-4513 (PubChem CID: 5081)GABA(A)receptor3. Good healthProtein Subunits030104 developmental biologyEndocrinologynervous systemGene Expression Regulation030220 oncology & carcinogenesisGABAergicNucleus accumbensSB 277011A (PubChem CID: 75358288)
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Triclosan-Evoked Neurotoxicity Involves NMDAR Subunits with the Specific Role of GluN2A in Caspase-3-Dependent Apoptosis

2018

Triclosan (TCS) is an antimicrobial agent that is used extensively in personal care and in sanitising products. A number of studies have shown the presence of TCS in different human tissues such as blood, adipose tissue, the liver, brain as well as in breast milk and urine. N-Methyl-D-aspartate receptors (NMDARs) are glutamate-gated ion channels that are widely expressed in the central nervous system and which play key roles in excitatory synaptic transmission. There is, however, no data on the involvement of NMDAR subunits in the apoptotic and neurotoxic effects of TCS. Our experiments are the first to show that TCS used at environmentally relevant concentrations evoked NMDA-dependent effe…

0301 basic medicineProgrammed cell deathGluN1Protein subunitNeurotoxinsNeuroscience (miscellaneous)Glutamic AcidCaspase 3ApoptosisReceptors N-Methyl-D-AspartateArticle03 medical and health sciencesCellular and Molecular NeuroscienceMice0302 clinical medicinemedicineAnimalsGene SilencingRNA MessengerReceptorNeuronsL-Lactate DehydrogenaseChemistryCaspase 3fungiNeurotoxicityROSTransfectionmedicine.diseaseTriclosanCell biologyGluN2BGluN2AProtein Subunits030104 developmental biologyNeurologyNMDAApoptosisNMDA receptorFemale030217 neurology & neurosurgeryMolecular Neurobiology
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Membrane insertion and topology of the translocon-associated protein (TRAP) gamma subunit

2017

Translocon-associated protein (TRAP) complex is intimately associated with the ER translocon for the insertion or translocation of newly synthesised proteins in eukaryotic cells. The TRAP complex is comprised of three single-spanning and one multiple-spanning subunits. We have investigated the membrane insertion and topology of the multiple-spanning TRAP-γ subunit by glycosylation mapping and green fluorescent protein fusions both in vitro and in cell cultures. Results demonstrate that TRAP-γ has four transmembrane (TM) segments, an Nt/Ct cytosolic orientation and that the less hydrophobic TM segment inserts efficiently into the membrane only in the cellular context of full-length protein.

0301 basic medicineVesicle-associated membrane protein 8Receptors PeptideProtein subunitBiophysicsReceptors Cytoplasmic and NuclearBiologyEndoplasmic ReticulumTopologyBiochemistryGreen fluorescent protein03 medical and health sciencesN-linked glycosylationMembranes (Biologia)Membrane GlycoproteinsEndoplasmic reticulumCalcium-Binding ProteinsProteïnes de membranaMembrane ProteinsCell BiologyTransloconTransmembrane proteinProtein Subunits030104 developmental biologyHydrophobic and Hydrophilic InteractionsGamma subunit
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