Search results for "G alpha subunit"

showing 7 items of 7 documents

Frontiers in Physiology

2021

Besides its roles in locomotion and thermogenesis, skeletal muscle plays a significant role in global glucose metabolism and insulin sensitivity through complex nutrient sensing networks. Our previous work showed that the muscle-specific ablation of O-GlcNAc transferase (OGT) led to a lean phenotype through enhanced interleukin-15 (IL-15) expression. We also showed OGT epigenetically modified and repressed the Il15 promoter. However, whether there is a causal relationship between OGT ablation-induced IL-15 secretion and the lean phenotype remains unknown. To address this question, we generated muscle specific OGT and interleukin-15 receptor alpha subunit (IL-15rα) double knockout mice (mDKO…

0301 basic medicinePhysiologymyokinesinterleukin-15Nutrient sensingCarbohydrate metabolism03 medical and health sciences0302 clinical medicinetissue cross-talkPhysiology (medical)Myokinemedicineinsulin sensitivityQP1-981ReceptorG alpha subunitChemistrySkeletal muscleBrief Research ReportCell biology030104 developmental biologymedicine.anatomical_structureKnockout mouseO-GlcNAc signalingSignal transduction030217 neurology & neurosurgeryFrontiers in Physiology
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The role of hypoxia-induced factors in tumor progression.

2004

Abstract Learning Objectives After completing this course, the reader will be able to: Describe hypoxia-induced mechanisms for cell survival. Discuss hypoxia-induced gene expression. Relate hypoxia and glucose metabolism. Access and take the CME test online and receive 1 hour of AMA PRA category 1 credit atCME.TheOncologist.com Hypoxia is a common characteristic of locally advanced solid tumors that has been associated with diminished therapeutic response and, more recently, with malignant progression, that is, an increasing probability of recurrence, locoregional spread, and distant metastasis. Emerging evidence indicates that the effect of hypoxia on malignant progression is mediated by a…

Cancer ResearchAngiogenesisCell SurvivalRegulatorBiologyNeoplasmsmedicineHumansNuclear proteinSelection GeneticTranscription factorG alpha subunitRegulation of gene expressionHelix-Loop-Helix MotifsNuclear ProteinsHypoxia (medical)Hypoxia-Inducible Factor 1 alpha SubunitCell HypoxiaDNA-Binding ProteinsGene Expression Regulation NeoplasticCell Transformation NeoplasticGlucoseOncologyTumor progressionImmunologyCancer researchDisease ProgressionHypoxia-Inducible Factor 1medicine.symptomTranscription FactorsThe oncologist
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On the origin of Metazoan adhesion receptors: cloning of integrin alpha subunit from the sponge Geodia cydonium

1997

Integrins are prominent receptors known from vertebrates and the higher phyla of invertebrates. Until now, no evidence has been provided for the existence of integrins in the lowest Metazoa, the sponges (Porifera). We have isolated and characterized a cDNA clone encoding the alpha subunit of integrin from the marine sponge Geodia cydonium (GCINTEG). The open reading frame encodes a polypeptide of 1,086 residues (118 kDa). The intracellular domain features the sequence Tyr-Phe-x-Gly-Phe-Phe-x-Arg, which is different in one residue from the characteristic consensus pattern for integrin alpha subunits. We conclude that sponges, the oldest multicellular animal phylum, already utilize the struct…

IntegrinsDNA ComplementaryMolecular Sequence DataIntegrinExtracellular matrixGeneticsAnimalsCloning MolecularReceptorMolecular BiologyEcology Evolution Behavior and SystematicsG alpha subunitCloningMembrane GlycoproteinsBase SequenceSequence Homology Amino AcidbiologyMembrane Proteinsbiology.organism_classificationPoriferaCell biologySuberites domunculaOpen reading frameSpongePlatelet Glycoprotein GPIb-IX Complexbiology.proteinMolecular Biology and Evolution
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Expression of nicotinic acetylcholine receptors in the rat superior cervical ganglion on mRNA and protein level.

1994

The expression of nicotinic acetylcholine receptors (nAChR) in the rat superior cervical ganglion was investigated by Western blotting, immunohistochemistry and non-radioactive in situ hybridization applying probes for the alpha 4-1 and beta 2 subunit mRNA. Immunoblot analysis of homogenized ganglia using the anti-nAChRs antibody WF6 revealed a labeled protein band of apparent molecular weight of 40 kDa which is typical for the alpha subunit of nAChRs. Applying double-labeling immunofluorescence with antibodies against tyrosine hydroxylase, nAChR-like molecules were identified in most postganglionic neurons and in a subpopulation of small intensely fluorescent (SIF) cells. alpha 4-1 and bet…

Malemedicine.medical_specialtySuperior cervical ganglionBlotting WesternFluorescent Antibody TechniqueGene ExpressionNerve Tissue ProteinsSuperior Cervical GanglionBiologyReceptors NicotinicRats Sprague-DawleyCellular and Molecular NeuroscienceGanglion type nicotinic receptorInternal medicineMuscarinic acetylcholine receptormedicineAnimalsRNA MessengerMolecular BiologyIn Situ HybridizationG alpha subunitAcetylcholine receptorNeuronsMolecular biologyRatsEndocrinologyNicotinic agonistnervous systemSmall intensely fluorescent cellFemalesense organsAcetylcholinemedicine.drugBrain research. Molecular brain research
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Synthesis of GABAA receptor agonists and evaluation of their alpha-subunit selectivity and orientation in the GABA binding site.

2008

Drugs used to treat various disorders target GABA A receptors. To develop alpha subunit selective compounds, we synthesized 5-(4-piperidyl)-3-isoxazolol (4-PIOL) derivatives. The 3-isoxazolol moiety was substituted by 1,3,5-oxadiazol-2-one, 1,3,5-oxadiazol-2-thione, and substituted 1,2,4-triazol-3-ol heterocycles with modifications to the basic piperidine substituent as well as substituents without basic nitrogen. Compounds were screened by [(3)H]muscimol binding and in patch-clamp experiments with heterologously expressed GABA A alpha ibeta 3gamma 2 receptors (i = 1-6). The effects of 5-aminomethyl-3 H-[1,3,4]oxadiazol-2-one 5d were comparable to GABA for all alpha subunit isoforms. 5-pipe…

Models MolecularPatch-Clamp TechniquesStereochemistryAlpha (ethology)gamma-Aminobutyric acidArticleGABAA-rho receptorCell Linechemistry.chemical_compoundStructure-Activity RelationshipXenopus laevisPiperidinesDrug DiscoverymedicineAnimalsHumansGABA-A Receptor AgonistsBinding siteReceptorgamma-Aminobutyric AcidG alpha subunitBinding SitesMolecular StructureChemistryGABAA receptorMuscimolBrainIsoxazolesReceptors GABA-ARatsElectrophysiologyProtein SubunitsBiochemistryMuscimolMutationOocytesMolecular MedicineFemalemedicine.drugJournal of medicinal chemistry
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miR-20b modulates VEGF expression by targeting HIF-1 alpha and STAT3 in MCF-7 breast cancer cells.

2010

MicroRNAs (miRNAs) are small non-coding RNAs that regulate the expression of different genes, including genes involved in cancer progression. A functional link between hypoxia, a key feature of the tumor microenvironment, and miRNA expression has been documented. We investigated whether and how miR-20b can regulate the expression of vascular endothelial growth factor (VEGF) in MCF-7 breast cancer cells under normoxic and hypoxia-mimicking conditions (CoCl(2) exposure). Using immunoblotting, ELISA, and quantitative real-time PCR, we demonstrated that miR-20b decreased VEGF protein levels at 4 and 24 h following CoCl(2) treatment, and VEGF mRNA at 4 h of treatment. In addition, miR-20b reduce…

STAT3 Transcription FactorVascular Endothelial Growth Factor ATime FactorsPhysiologySettore MED/06 - Oncologia MedicaClinical BiochemistryDown-RegulationBreast NeoplasmsBiologyTransfectionchemistry.chemical_compoundmir20b VEGFCell Line TumormicroRNAHumansSTAT3Promoter Regions GeneticG alpha subunitRegulation of gene expressionTumor microenvironmentBinding SitesCell BiologyTransfectionCobaltHypoxia-Inducible Factor 1 alpha SubunitMolecular biologyCell HypoxiaVascular endothelial growth factorGene Expression Regulation NeoplasticMicroRNAsHIF1Achemistrybiology.proteinFemaleRNA InterferenceSignal TransductionJournal of cellular physiology
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Selective Binding of Collagen Subtypes by Integrin α1I, α2I, and α10I Domains

2001

Four integrins, namely alpha(1)beta(1), alpha(2)beta(1), alpha(10)beta(1), and alpha(11)beta(1), form a special subclass of cell adhesion receptors. They are all collagen receptors, and they recognize their ligands with an inserted domain (I domain) in their alpha subunit. We have produced the human integrin alpha(10)I domain as a recombinant protein to reveal its ligand binding specificity. In general, alpha(10)I did recognize collagen types I-VI and laminin-1 in a Mg(2+)-dependent manner, whereas its binding to tenascin was only slightly better than to albumin. When alpha(10)I was tested together with the alpha(1)I and alpha(2)I domains, all three I domains seemed to have their own collag…

Type IV collagenIntegrin alpha2Integrin alpha ChainsAlpha (ethology)Cell BiologyBiologyMolecular BiologyBiochemistryMolecular biologyType I collagenBinding domainCollagen receptorG alpha subunitJournal of Biological Chemistry
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