Search results for "Neuropeptide"

showing 10 items of 194 documents

Salivary and serum levels of substance p, neurokinin A and calcitonin gene related peptide in burning mouth syndrome

2009

Background: Burning mouth syndrome (BMS) is an enigmatic condition with the etiopathogenesis remaining largely obscure. However, a neuropathic basis for BMS continues to be an area of active clinical and research interest. Aim: It is becoming increasingly evident that certain oral disorders may be modulated by imbalances in certain neuropeptides such as substance P (SP), neurokinin A (NKA) and calcitonin gene-related peptide (CGRP) therefore we measured SP, NKA and CGRP in the saliva and sera of BMS patients as well as controls. Subjects and Methods: Salivary and serum SP, NKA and CGRP were determined in the 26 female patients with burning mouth syndrome (age range 51-78, mean 65.69 yrs), a…

Malemedicine.medical_specialtySalivaCalcitonin Gene-Related PeptideNeurokinin ANeuropeptideSubstance PBurning Mouth SyndromeCalcitonin gene-related peptideSubstance Pchemistry.chemical_compoundInternal medicinemedicineHumansSalivaGeneral DentistryAgedbusiness.industryDopaminergicBurning mouth syndromeMiddle Agedrespiratory system:CIENCIAS MÉDICAS [UNESCO]stomatognathic diseasesEndocrinologyOtorhinolaryngologychemistryCalcitoninUNESCO::CIENCIAS MÉDICASSubstance P ; neurokinin A ; calcitonin gene-related peptide ; burning mouth syndromeSurgeryFemaleNeurokinin Amedicine.symptombusiness
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Alpha 2-receptor-mediated inhibition of intraluminal release of gastric somatostatin in anaesthetized rats.

1992

Alino, S. F., Garcia, D. & Uvnas-Moberg, K. 1992. Alpha2-receptor-mediated inhibition of intraluminal release of gastric somatostatin in anaesthetized rats. Acta Physiol Scand144, 233–238. Received 22 February 1991, accepted 11 October 1991. ISSN 00014772. Department of Pharmacology and Pharmaceutics, University of Valencia, Valencia, Spain, Department of Cell Biology and Morphology Science, University of Pais Vasco, Leioa, Spain and Department of Pharmacology, Karolinska Institute, Stockholm, Sweden. The aim of the present study was to investigate how the sympathetic nervous system affects the vagally induced intragastric release of somatostatin and gastrin. Experiments were performed on a…

Malemedicine.medical_specialtySympathetic Nervous SystemPhysiologyNeuropeptideClonidinePhentolamineInternal medicineGastrinsmedicineAnimalsAnesthesiaPhentolamineGastrinbusiness.industryStomachdigestive oral and skin physiologyRats Inbred StrainsVagus NerveHydrogen-Ion ConcentrationReceptors Adrenergic alphaElectric StimulationVagus nerveRatsEndocrinologymedicine.anatomical_structureSomatostatinGastrointestinal hormoneGastric MucosabusinessSomatostatinPerfusionhormones hormone substitutes and hormone antagonistsmedicine.drugActa physiologica Scandinavica
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Frequency-dependent effects of activation and inhibition of protein kinase C on neurohypophysial release of oxytocin and vasopressin

1989

Isolated rat neurohypophyses were superfused in vitro and the release of vasopressin and oxytocin into the medium was determined by specific radioimmunoassays. Hormone secretion was increased by electrical stimulation of the pituitary stalk at different frequencies. The effects of several phorbol esters, known to activate (phorbol 12,13-dibutyrate, PDB) or not to affect (4a-phorbol 12,13-dideconate and phorbol 12-monoacetate) protein kinase C, and of the direct protein kinase C inhibitor 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H7) were tested. Electrical stimulation with 450 pulses caused the release of about 45 μU vasopressin and 55 μU oxytocin, when a frequency of 3 Hz was applied…

Malemedicine.medical_specialtyVasopressinVasopressinsNeuropeptideStimulationIn Vitro TechniquesBiologyOxytocinchemistry.chemical_compoundPituitary Gland PosteriorInternal medicinemedicineAnimalsPhorbol 1213-DibutyrateProtein Kinase CProtein kinase CEndogenous opioidPharmacologyNaloxoneOxytocin secretionRats Inbred StrainsGeneral MedicineElectric StimulationRatsEndocrinologyOxytocinchemistryPhorbolhormones hormone substitutes and hormone antagonistsmedicine.drugNaunyn-Schmiedeberg's Archives of Pharmacology
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Episodic Social Stress-Escalated Cocaine Self-Administration: Role of Phasic and Tonic Corticotropin Releasing Factor in the Anterior and Posterior V…

2016

Intermittent social defeat stress escalates later cocaine self-administration. Reward and stress both activate ventral tegmental area (VTA) dopamine neurons, increasing downstream extracellular dopamine concentration in the medial prefrontal cortex and nucleus accumbens. The stress neuropeptide corticotropin releasing factor (CRF) and its receptors (CRF-R1, CRF-R2) are located in the VTA and influence dopaminergic activity. These experiments explore how CRF release and the activation of its receptors within the VTA both during and after stress influence later cocaine self-administration in rats.In vivomicrodialysis of CRF in the VTA demonstrated that CRF is phasically released in the poster…

Malemedicine.medical_specialtyendocrine systemCorticotropin-Releasing HormoneMicrodialysisDrug-Seeking BehaviorNeuropeptideSelf AdministrationNucleus accumbensSocial EnvironmentReceptors Corticotropin-Releasing HormoneSocial defeat03 medical and health sciencesCorticotropin-releasing hormoneCocaine-Related Disorders0302 clinical medicineDopamineInternal medicinemental disordersmedicineAnimalsRats Long-EvansSocial stressGeneral Neurosciencemusculoskeletal neural and ocular physiologyDopaminergicVentral Tegmental AreaArticles030227 psychiatryRatsSubstance Withdrawal SyndromeVentral tegmental areamedicine.anatomical_structureEndocrinologynervous systemPsychologyNeuroscience030217 neurology & neurosurgeryhormones hormone substitutes and hormone antagonistsStress Psychologicalmedicine.drug
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Rac1 GTPase, a multifunctional player in the regulation of genotoxic stress response

2013

The Ras-related C3 botulinum toxin substrate 1 (Rac1) belongs to the Ras-homologous (Rho) family of small GTPases, which transduce signals from the outside to the inside of a cell. Rac1 becomes activated upon ligand binding of a variety of receptors, including receptor tyrosine kinases and heterotrimeric G-protein-coupled receptors. After GTP loading by guanine exchange factors (GEFs), GTP-bound Rac1 engages numerous effector proteins, thereby eventually regulating cell motility and adhesion, cell cycle progression through G1, mitosis and meiosis, as well as cell death and metastasis.1 Besides, Rac1 adjusts cellular responses to genotoxic agents, such as UV light and alkylating agents, by r…

Malerac1 GTP-Binding Proteintopoisomerase IIAgingRHOADNA repairDNA damagep38 mitogen-activated protein kinasesApoptosisRAC1Editorials: Cell Cycle FeaturesDNA damage responseReceptor tyrosine kinasechemical carcinogenesisHistonesMiceTransforming Growth Factor betaRho GTPasesAnimalsMolecular BiologyTranscription factoranthracyclinesMice KnockoutbiologyKinaseNeuropeptidesConnective Tissue Growth FactorHMG-CoA reductase inhibitors (statins)Cell BiologyFibrosisgenotoxic stressActinsrac GTP-Binding ProteinsCell biologyOxidative Stressnormal tissue damageGene Expression RegulationLiverBiochemistryDoxorubicinGamma Raysbiology.proteinFemaleDNA DamageMutagensSignal TransductionDevelopmental BiologyCell Cycle
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The 1258 GA polymorphism in the neuropeptide Y gene is associated with greater alcohol consumption in a Mediterranean population.

2011

Abstract Neuropeptide Y (NPY) is a neurotransmitter widely distributed in the central nervous system. Several studies have demonstrated that increases of NPY are associated with reduced alcohol intake and anxiety manifestations. The Leu7Pro polymorphism in the NPY has been associated with alcohol consumption, but evidence is scarce. In the Spanish Mediterranean population, this variant is not polymorphic. Thus, our aim is to identify novel functional variants in the NPY and to investigate the impact of these markers and others previously described on alcohol consumption in this population. A total of 911 subjects (321 men and 590 women) from the Spanish Mediterranean population were recruit…

Mediterranean climateAdultMalemedicine.medical_specialtyHealth (social science)Alcohol DrinkingGenotypePopulationNeuropeptide Y GeneBiologyToxicologyBiochemistryPolymorphism Single NucleotideBehavioral NeuroscienceGene FrequencyPopulation GroupsPolymorphism (computer science)Internal medicinemedicineSNPHumansNeuropeptide YeducationAllele frequencyGeneticseducation.field_of_studyMediterranean RegionGeneral MedicineMiddle AgedNeuropeptide Y receptorEndocrinologyNeurologySpainFemaleAlcohol consumptionSequence AnalysisAlcohol (Fayetteville, N.Y.)
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Pharmacogenomics of cantharidin in tumor cells.

2014

Cantharis vesicatoria (blister beetle) is used in Chinese medicine and has been categorized as highly toxic in the Chinese pharmacopeia. In Europe, Cantharis patches have been used since ages to treat various skin-related diseases. We investigated the cytotoxicity of the Cantharis ingredient, cantharidin, in 41 tumor cell lines (Oncotest panel) and compared the results with those of 60 cell lines of the National Cancer Institute, USA. We found profound activity at low micromolar concentrations (log ₁₀IC₅₀ values between -6.980 and 5.009 M). Cantharidin bound to protein phosphatase 2A (PP2A) with higher affinity (-8.12 kcal/mol) than to PP1 (-6.25 kcal/mol) in molecular docking analyses. Usi…

Models MolecularProtein ConformationBlister beetleBiologyCantharisBiochemistryFas ligandGene Expression Regulation Enzymologicchemistry.chemical_compoundCell Line TumorGene expressionAnimalsHumansRNA MessengerCytotoxicityOligonucleotide Array Sequence AnalysisPharmacologyCantharidinBinding SitesMolecular Structurebiology.organism_classificationMolecular biologyReceptors Neuropeptide YchemistryCell cultureApoptosisPharmacogeneticsImmunologyCantharidinBiochemical pharmacology
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The Tempered Polymerization of Human Neuroserpin

2012

Neuroserpin, a member of the serpin protein superfamily, is an inhibitor of proteolytic activity that is involved in pathologies such as ischemia, Alzheimer's disease, and Familial Encephalopathy with Neuroserpin Inclusion Bodies (FENIB). The latter belongs to a class of conformational diseases, known as serpinopathies, which are related to the aberrant polymerization of serpin mutants. Neuroserpin is known to polymerize, even in its wild type form, under thermal stress. Here, we study the mechanism of neuroserpin polymerization over a wide range of temperatures by different techniques. Our experiments show how the onset of polymerization is dependent on the formation of an intermediate mon…

Models MolecularProtein FoldingAmyloidScienceNeuroserpinBiophysicsSerpinBiochemistryAggregationchemistry.chemical_compoundNeuroserpinmedicineHumansPolumerization; Aggregation; Neuroserpin; FENIB; Light scatteringFamilial encephalopathy with neuroserpin inclusion bodiesBiologySerpinschemistry.chemical_classificationMultidisciplinaryPolumerizationPhysicsNeuropeptidesQTemperatureRLight scatteringProteinsPolymermedicine.diseaseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)EnzymesKineticsMonomerchemistryPolymerizationBiochemistryFENIBBiophysicsMedicineProtein foldingProtein MultimerizationResearch ArticlePLoS ONE
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On the molecular structure of human neuroserpin polymers

2012

The polymerization of serpins is at the root of a large class of diseases; the molecular structure of serpin polymers has been recently debated. In this work, we study the polymerization kinetics of human neuroserpin by Fourier Transform Infra Red spectroscopy and by time-lapse Size Exclusion Chromatography. First, we show that two distinct neuroserpin polymers, formed at 45 and 85°C, display the same isosbestic points in the Amide I' band, and therefore share common secondary structure features. We also find a concentration independent polymerization rate at 45°C suggesting that the polymerization rate-limiting step is the formation of an activated monomeric species. The polymer structures…

Models MolecularSize-exclusion chromatographySerpinBiochemistryProtein Structure Secondaryserpinopathieprotein aggregationchemistry.chemical_compoundStructural BiologyNeuroserpinCatalytic DomainSpectroscopy Fourier Transform InfraredPolymer chemistryHumansMolecular BiologyProtein secondary structureSerpinschemistry.chemical_classificationIsosbestic pointChemistryNeuropeptidesserpinPolymerSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)KineticsCrystallographyMonomerprotein aggregation; serpins; serpinopathies; serpin polymerization; FTIRPolymerizationFTIRChromatography GelProtein Multimerizationserpin polymerization
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Neuropeptide Y receptors (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

2019

Neuropeptide Y (NPY) receptors (nomenclature as agreed by the NC-IUPHAR Subcommittee on Neuropeptide Y Receptors [156]) are activated by the endogenous peptides neuropeptide Y, neuropeptide Y-(3-36), peptide YY, PYY-(3-36) and pancreatic polypeptide (PP). The receptor originally identified as the Y3 receptor has been identified as the CXCR4 chemokine recepter (originally named LESTR, [137]). The y6 receptor is a functional gene product in mouse, absent in rat, but contains a frame-shift mutation in primates producing a truncated non-functional gene [83]. Many of the agonists exhibit differing degrees of selectivity dependent on the species examined. For example, the potency of PP is greater…

MutationChemokinebiologyChemistryNeuropeptidePharmacologymedicine.disease_causeNeuropeptide Y receptorPeptide YYmedicinebiology.proteinPancreatic polypeptideReceptorPeptide sequenceIUPHAR/BPS Guide to Pharmacology CITE
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