Search results for "Neuropeptides"

showing 10 items of 81 documents

Interplay between PACAP and NO in mouse ileum

2003

Abstract We investigated the possibility that pituitary adenylate cyclase activating peptide (PACAP) has a role in the control of contractility in the mouse ileum. PACAP-(1-27) produced tetrodotoxin (TTX)-insensitive, concentration-dependent reduction of the amplitude of the spontaneous contractions of longitudinal muscle up to their complete disappearance. This effect was inhibited by PACAP-(6-38), PACAP receptor antagonist, and by apamin, blocker of small-conductance Ca2+-activated K+-channels. Nω-nitro- l -arginine methyl ester (L-NAME), nitric oxide (NO) synthase inhibitor, reduced the PACAP-inhibitory response, and the joint application of apamin plus L-NAME produced additive effects. …

Maleendocrine systemmedicine.medical_specialtyMuscle RelaxationMouse ileumStimulationIn Vitro TechniquesApaminSettore BIO/09 - FisiologiaContractilityMiceCellular and Molecular Neurosciencechemistry.chemical_compoundSmooth muscleIleumInternal medicinemedicineAnimalsMyocyteNitric Oxide DonorsPharmacologyDose-Response Relationship DrugNeuropeptidesNitric oxideSmooth muscle contractionMice Inbred C57BLPituitary adenylate cyclase-activating peptideEndocrinologyApaminchemistryTetrodotoxinPituitary Adenylate Cyclase-Activating PolypeptideSodium nitroprussidePACAP (pituitary adenylate cyclase activating peptide)hormones hormone substitutes and hormone antagonistsmedicine.drugNeuropharmacology
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Comparative investigations on the actions of ACTH1-24, somatostatin, neurotensin, substance P and vasopressin on locus coeruleus neuronal activity in…

1987

A considerable number of neuropeptides have been localized immunohistochemically in the area of the locus coeruleus of the rat. The objective of this study was to assess the actions of some of these transmitter candidates on spontaneously active locus coeruleus neurons in vitro. The effects of bath-applied peptides on the discharge rate of individual locus coeruleus neurons were investigated. A midpontine slice preparation of the gerbil brain was used. Excitatory dose-dependent effects were found with four peptides with the following rank order of potency: Substance P, (Arg8)-vasopressin, neurotensin, ACTH1–24. Somatostatin hyperpolarized all neurons tested. Given the pronounced effects see…

Maleendocrine systemmedicine.medical_specialtyVasopressinVasopressinsNeuropeptideSubstance PIn Vitro TechniquesSubstance Pchemistry.chemical_compoundSlice preparationInternal medicinemedicinePremovement neuronal activityAnimalsNeurotensinPharmacologyNeuronsChemistryNeuropeptidesGeneral MedicineArginine VasopressinEndocrinologySomatostatinnervous systemLocus coeruleusCosyntropinLocus CoeruleusGerbillinaeSomatostatinhormones hormone substitutes and hormone antagonistsNeurotensinNaunyn-Schmiedeberg's archives of pharmacology
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Immunohistochemical analysis of chromogranin A and multiple peptides in the mammalian Merkel cell: further evidence for its paraneuronal function?

1989

By the use of light microscopic immunohistochemistry, epidermal Merkel cells have been examined for the coexistence of some neuropeptides and chromogranin A (CGA). Peptide and CGA-immunophenotypes were similar in adult Merkel cells but variable in fetal skin, where CGA preceded the expression of peptides which were partly expressed only in a subpopulation of Merkel cells from hair follicles. Thus, only Substance P (SP) and calcitonin gene-related peptide (CGRP) were expressed in a subpopulation of Merkel cells from hair follicles. There were similar Merkel cell densities visualized on consecutive paraffin sections by the use of antisera against peptides, CGA and cytokeratin offering useful …

Maleendocrine systemmedicine.medical_specialtyanimal structuresHistologySwineRadioimmunoassayNeuropeptideSubstance PNerve Tissue ProteinsCalcitonin gene-related peptideBiologyCytokeratinchemistry.chemical_compoundInternal medicineEndocrine GlandsmedicineChromograninsAnimalsNeurons Afferentskin and connective tissue diseasesintegumentary systemNeuropeptidesvirus diseasesChromogranin AMolecular biologyImmunohistochemistryMicroscopy Electronmedicine.anatomical_structureEndocrinologychemistryEpidermal CellsCalcitoninbiology.proteinImmunohistochemistryChromogranin AFemaleEpidermisMerkel cellArchives of histology and cytology
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Antagonistic effects of hypertrehalosemic neuropeptide on the activities of 6-phosphofructo-1-kinase and fructose-1,6-bisphosphatase in cockroach fat…

2001

Hypertrehalosemic neuropeptides from the corpora cardiaca such as the decapeptide Bld HrTH bring about a profound switch in the metabolic activity of cockroach fat body during which production of the blood sugar trehalose is stimulated while the catabolism of carbohydrate (glycolysis) is inhibited. The mechanisms of the metabolic switch are not fully understood. Incubation of isolated fat body from the cockroach Blaptica dubia with 10(-8) M Bld HrTH, for 10-60 min, stimulated glycogen breakdown and increased the content of the substrates of both the glycolytic enzyme 6-phosphofructo-1-kinase (PFK, EC 2.7.1.11) and the gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase, EC 3.1.3.11) in…

Malemedicine.medical_specialtyBlaptica dubiaPhosphofructokinase-1Fat BodyFructose 16-bisphosphataseCockroachesIn Vitro TechniquesBiologyBiochemistryGene Expression Regulation Enzymologicchemistry.chemical_compoundInternal medicineFructosediphosphatesmedicineAnimalsGlycolysisPhosphofructokinase 1Molecular BiologyCatabolismNeuropeptidesTrehaloseFructosebiology.organism_classificationAdenosine MonophosphateFructose-BisphosphataseKineticsEndocrinologyFructose 26-bisphosphatechemistryBiochemistryInsect HormonesInsect Sciencebiology.proteinGlycogenPhosphofructokinaseInsect Biochemistry and Molecular Biology
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Altered expression of neuropeptides in the primary somatosensory cortex of the Down syndrome model Ts65Dn.

2011

Down syndrome is the most common genetic disorder associated with mental retardation. Subjects and mice models for Down syndrome (such as Ts65Dn) show defects in the formation of neuronal networks in both the hippocampus and the cerebral cortex. The principal neurons display alterations in the morphology, density and distribution of dendritic spines in the cortex as well as in the hippocampus. Several evidences point to the possibility that the atrophy observed in principal neurons could be mediated by changes in their inhibitory inputs and, in fact, an imbalance between excitation and inhibition has been observed in Ts65Dn mice in these regions, which are crucial for learning and informati…

Malemedicine.medical_specialtyDendritic spineHippocampusBiologySomatosensory systemCalbindinHippocampusCellular and Molecular NeuroscienceMiceEndocrinologyInterneuronsCortex (anatomy)Internal medicinemedicineAnimalsNeuronsEndocrine and Autonomic SystemsCalcium-Binding ProteinsNeuropeptidesGeneral MedicineSomatosensory CortexDisease Models Animalmedicine.anatomical_structureEndocrinologySomatostatinnervous systemNeurologyCerebral cortexCalretininDown SyndromeSomatostatinNeuroscienceNeuropeptides
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On the peptidergic hypothesis for non-adrenergic non-cholinergic innervation in the rat duodenum

1992

1. The nature of the non-adrenergic, non-cholinergic (NANC) transmitter was studied in vitro in the rat duodenum, by use of an isometric-isovolumic preparation. 2. Electrical field stimulation (EFS) induced a tetrodotoxin (TTX)-sensitive fall both in luminal pressure and in isometric tension. 3. Neurotensin (NT) induced TTX-insensitive inhibitory responses similar to those induced by EFS. Vasoactive intestinal peptide (VIP) caused a delayed, slow, concentration-dependent, TTX-insensitive inhibitory effect, detected only by a change in luminal pressure. 4. alpha-chymotrypsin prevented the NT- and VIP-induced inhibitory effects and antagonized the response to EFS. 5. Apamin antagonized the EF…

Malemedicine.medical_specialtyDuodenumMuscle RelaxationVasoactive intestinal peptideIn Vitro TechniquesBiologyAutonomic Nervous SystemApaminInhibitory postsynaptic potentialchemistry.chemical_compoundDesensitization (telecommunications)Isometric ContractionInternal medicinemedicineAnimalsChymotrypsinReceptorNeurotensinPharmacologymusculoskeletal neural and ocular physiologyGeneral NeuroscienceNeuropeptidesMuscle SmoothRats Inbred StrainsElectric StimulationRatsmedicine.anatomical_structureEndocrinologyApaminchemistryTetrodotoxinDuodenumhormones hormone substitutes and hormone antagonistsVasoactive Intestinal PeptideNeurotensinJournal of Autonomic Pharmacology
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The neuroimmune connection in human tonsils.

1991

The present light microscopic immunohistochemical study evaluates the distribution of peptidergic nerve fibers in human tonsil and describes their spatial relationship with specific cells of the immune system. Further, using a panneural marker protein gene product (PGP) 9.5, a qualitative evaluation of the density of specific peptidergic innervation of the human tonsil was performed. Nerve fibers staining for tachykinins, calcitonin gene-related peptide, neuropeptide Y, or vasoactive intestinal polypeptide/peptide histidine isoleucine showed characteristic distribution patterns, but constituted only a minor subfraction of the PGP 9.5-stained fiber population. Both peptide- and PGP 9.5-immun…

Malemedicine.medical_specialtyPathologyNeuroimmunomodulationImmunologyVasoactive intestinal peptidePopulationPalatine TonsilNerve fiberBiologyPalatine tonsilBehavioral NeuroscienceNerve FibersInternal medicinemedicineHumansLymphocyteseducationChildeducation.field_of_studyEndocrine and Autonomic SystemsMacrophagesNeuropeptidesGerminal centerNeuropeptide Y receptorImmunohistochemistryEndocrinologymedicine.anatomical_structurePeripheral nervous systemTonsilFemaleUbiquitin ThiolesteraseBiomarkersGranulocytesBrain, behavior, and immunity
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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 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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