Search results for "Subunit"

showing 10 items of 513 documents

Complete Hemocyanin Subunit Sequences of the Hunting SpiderCupiennius salei

2002

Hemocyanins are large copper-containing respiratory proteins found in many arthropod species. Scorpions and orthognath spiders possess a highly conserved 4 x 6-mer hemocyanin that consists of at least seven distinct subunit types (termed a to g). However, many "modern" entelegyne spiders such as Cupiennius salei differ from the standard arachnid scheme and have 2 x 6-mer hemocyanins. Here we report the complete primary structure of the 2 x 6-mer hemocyanin of C. salei as deduced from cDNA sequencing, gel electrophoresis, and matrix-assisted laser desorption spectroscopy. Six distinct subunit types (1 through 6) and three additional allelic sequences were identified. Each 1 x 6-mer half-mole…

ArachnidSpiderbiologyProtein subunitmedicine.medical_treatmentProtein primary structuremyrHemocyaninCell BiologyAnatomybiology.organism_classificationcomplex mixturesBiochemistryCupiennius saleiEvolutionary biologymedicineArthropodMolecular BiologyJournal of Biological Chemistry
researchProduct

Molecular and Functional Characterisation of Hemocyanin of the Giant African Millipede Archispirostreptus gigas

2013

SummaryIn contrast to other terrestrial arthropods where gaseous O2 that fuels aerobic metabolism diffuses to the tissues in tracheal tubes, and most other metazoans where O2 is transported to tissues by circulating respiratory proteins, the myriapods (millipedes and centipedes) strikingly have tracheal systems as well as circulating hemocyanin (Hc). In order to elucidate the evolutionary origin and biological significance of millipede Hc we report the molecular structure (subunit composition and amino acid sequence) of multimeric (36-mer) Hc from the forest-floor dwelling giant African millipede Archispirostreptus gigas and its allosteric oxygen binding properties under various physico-che…

Archispirostreptus gigasGlycosylationPhysiologymedicine.medical_treatmentProtein subunitAllosteric regulationMolecular Sequence DataCoenzymesBohr effectCooperativityAquatic ScienceBiologyModels Biologicalchemistry.chemical_compoundAllosteric RegulationmedicineAnimalsBody SizeMolecular BiologyPeptide sequenceArthropodsEcology Evolution Behavior and SystematicsPhylogenyHemocyaninBayes TheoremHydrogen-Ion Concentrationbiology.organism_classificationOxygenchemistryBiochemistryInsect ScienceAfricaHemocyaninsAnimal Science and ZoologyCalciumElectrophoresis Polyacrylamide GelProtein Binding
researchProduct

INFγ stimulates arginine transport through system y+L in human monocytes

2004

Freshly isolated human monocytes transport L-arginine mostly through a sodium independent, NEM insensitive pathway inhibited by L-leucine in the presence, but not in the absence of sodium. Interferon-gamma (IFNgamma) stimulates this pathway, identifiable with system y+L, and markedly enhances the expression of SLC7A7, the gene that encodes for system y+L subunit y+LAT1, but not of SLC7A6, that codes for the alternative subunit y+LAT2. System y+ plays a minor role in arginine uptake by monocytes and the expression of system y+-related genes, SLC7A1 and SLC7A2, is not changed by IFNgamma. These results demonstrate that system y+L is sensitive to IFNgamma.

ArginineSodiumProtein subunitBiophysicschemistry.chemical_elementBiologyLPI - Lysinuric protein intoleranceArginineMonocyteBiochemistryMonocytesInterferon-gammaInterferon γLeucineStructural BiologyArginine transportSystem y+L.GeneticsmedicineHumansMolecular BiologyGeneLysinuric protein intoleranceCells CulturedArginine transportReverse Transcriptase Polymerase Chain ReactionFusion Regulatory Protein 1 Light ChainsMonocyteSodiumAmino Acid Transport System y+LBiological TransportCell BiologyMolecular biologyRecombinant ProteinsKineticsmedicine.anatomical_structurechemistryEthylmaleimideAmino Acid Transport Systems BasicInterferon-γFEBS Letters
researchProduct

The Low-Affinity ATP Binding Site of the Escherichia coli SecA Dimer Is Localized at the Subunit Interface

1997

The homodimeric SecA protein is the ATP-dependent force generator in the Escherichia coli precursor protein translocation cascade. SecA contains two essential nucleotide binding sites (NBSs), i.e., NBS1 and NBS2 that hind ATP with high and low affinity, respectively. The photoactivatable bifunctional cross-linking agent 3'-arylazido-8-azidoadenosine 5'-triphosphate (diN(3)ATP) was used to investigate the spatial arrangement of the nucleotide binding sites of SecA, DiN(3)ATP is an authentic ATP analogue as it supports SecA-dependent precursor protein translocation and translocation ATPase, UV-induced photo-cross-linking of the diN(3)ATP-bound SecA results in the formation of stable dimeric s…

AzidesUltraviolet RaysProtein subunitATPaseDimerMutantPhotoaffinity LabelsBiologymedicine.disease_causeESSENTIAL COMPONENTenvironment and public healthBiochemistryBACILLUS-SUBTILISchemistry.chemical_compoundAdenosine TriphosphateBacterial ProteinsPROTON MOTIVE FORCEEscherichia colimedicinePRECURSOR PROTEIN TRANSLOCATIONNucleotideBinding siteEscherichia coliAdenosine Triphosphataseschemistry.chemical_classificationBinding SitesSecA ProteinsNucleotidesChemiosmosisEscherichia coli ProteinsMembrane Transport ProteinsPHOTOAFFINITY CROSS-LINKINGCross-Linking ReagentschemistryBiochemistryMEMBRANE-VESICLES REQUIRESPLASMA-MEMBRANE3'-ARYLAZIDO-BETA-ALANYL-8-AZIDO ATPCYTOPLASMIC MEMBRANEbiology.proteinPREPROTEIN TRANSLOCASEbacteriaDimerizationSEC Translocation ChannelsBiochemistry
researchProduct

11,12-EET Stimulates the Association of BK Channel α and β1 Subunits in Mitochondria to Induce Pulmonary Vasoconstriction

2012

In the systemic circulation, 11,12-epoxyeicosatrienoic acid (11,12-EET) elicits nitric oxide (NO)- and prostacyclin-independent vascular relaxation, partially through the activation of large conductance Ca(2+)-activated potassium (BK) channels. However, in the lung 11,12-EET contributes to hypoxia-induced pulmonary vasoconstriction. Since pulmonary artery smooth muscle cells also express BK channels, we assessed the consequences of BKβ(1) subunit deletion on pulmonary responsiveness to 11,12-EET as well as to acute hypoxia. In buffer-perfused mouse lungs, hypoxia increased pulmonary artery pressure and this was significantly enhanced in the presence of NO synthase (NOS) and cyclooxygenase (…

BK channelAnatomy and PhysiologyLarge-Conductance Calcium-Activated Potassium Channel beta SubunitsRespiratory Systemlcsh:MedicineCardiovascularCardiovascular SystemBiochemistryIon ChannelsMembrane PotentialsMice81114-Eicosatrienoic AcidHypoxic pulmonary vasoconstrictionHypoxiaLarge-Conductance Calcium-Activated Potassium Channel alpha Subunitslcsh:ScienceLungEnergy-Producing OrganellesEpoxide HydrolasesMembrane Potential MitochondrialMembrane potentialMultidisciplinarybiologyChemistryDepolarizationHyperpolarization (biology)IberiotoxinMitochondriaBiochemistryCirculatory Physiologycardiovascular systemMedicinelipids (amino acids peptides and proteins)medicine.symptomResearch ArticleCell Physiologymedicine.medical_specialtyPulmonary ArteryBioenergeticsCardiovascular PharmacologyInternal medicinemedicineAnimalsHumansArterial Pressureddc:610Protein InteractionsBiologylcsh:RProteinsCalcium-activated potassium channelMice Inbred C57BLHEK293 CellsEndocrinologyVasoconstrictionbiology.proteinlcsh:QGene DeletionVasoconstrictionPLoS ONE
researchProduct

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
researchProduct

Glomerular basement membrane: evidence for collagenous domain of the alpha 3 and alpha 4 chains of collagen IV.

1990

Abstract A collagenous component(s) of Mr = 60K was extracted from glomerular basement membrane with urea and was purified. Upon digestion, it yielded a collagenase-resistant fragment(s) of Mr = 23.5K. Both component and fragment showed immunochemical identity with the noncollagenous domains of the new α3 & α4 chains of collagen IV. The component is characterized by a collagenous domain of about 280 residues and a noncollagenous domain of about 250 residues. These findings further establish these new chains as distinct entities of collagen IV.

Basement membraneGel electrophoresischemistry.chemical_classificationChemistryRenal glomerulusMacromolecular SubstancesProtein ConformationProtein subunitGlomerular basement membraneKidney GlomerulusBiophysicsBiological membraneCell BiologyBiochemistryBasement Membranemedicine.anatomical_structureBiochemistryDomain (ring theory)medicineAnimalsCattleCollagenAmino AcidsGlycoproteinMolecular BiologyBiochemical and biophysical research communications
researchProduct

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
researchProduct

D-Galactose binding lectins from the tunicate Ascidiamalaca: Subunit characterization and hemocyte surface distribution

1988

Abstract D-galactose specific lectins purified from Ascidia malaca serum contain a major protein component with an apparent molecular weight of about 58,000 daltons, which moves more rapidly under non-reducing conditions. Intramolecular disulfide linkages can explain this behaviour, suggesting a compact protein structure. Membrane lectins have been demonstrated on the surface of about 34% hemocytes by immunofluorescent methods using a rabbit antiserum against the isolated serum lectins. Small, medium and large hemocytes can be positive, as also shown by binding on Sepharose spherules or by rosette formation with sheep and rabbit erythrocytes. Binding is inhibited by the same sugars specific…

Binding SitesBlood CellsHemocytesRosette FormationGalectinsProtein subunitCell MembraneImmunologyLectinBiologyBinding CompetitiveSepharosechemistry.chemical_compoundHemagglutininsProtein structurechemistryBiochemistryGalactoseGalactose bindingbiology.proteinAnimalsProtein quaternary structureUrochordataAntibodyDevelopmental BiologyDevelopmental & Comparative Immunology
researchProduct

Nested allosteric interactions in extracellular hemoglobin of the leech Macrobdella decora

2003

Hemoglobin from the leech Macrobdella decora belongs to the class of giant extracellular hexagonal bilayer globin structures found in annelid and vestimentiferan worms. These complexes consist of 144 heme-bearing subunits, exhibit a characteristic quaternary structure (2 × (6 × (3 × 4))), and contain tetramers as basic substructures that express cooperative oxygen binding and thus provide a structural basis for a hierarchy in allosteric interactions. A thorough analysis of the isolated tetramer indicates that it functions as a trimer of cooperatively interacting subunits and a non-cooperative monomer rather than as four interacting subunits. A thermodynamic analysis of the whole molecule fa…

Binding Sitesgenetic structuresStereochemistryMacromolecular SubstancesProtein ConformationBilayerAllosteric regulationTrimerCell BiologyBiologyBiochemistryGroELOxygenHemoglobinsProtein SubunitsTetramerLeechesAnimalsProtein quaternary structureGlobinProtein Structure QuaternaryMolecular BiologyOxygen binding
researchProduct