Base de dados : MEDLINE
Pesquisa : D12.776.157.530.450.162.887 [Categoria DeCS]
Referências encontradas : 21 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 3 ir para página          

  1 / 21 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27040629
[Au] Autor:Moriyama S; Hiasa M
[Ad] Endereço:Department of Membrane Biochemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences.
[Ti] Título:Expression of Vesicular Nucleotide Transporter in the Mouse Retina.
[So] Source:Biol Pharm Bull;39(4):564-9, 2016.
[Is] ISSN:1347-5215
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Vesicular nucleotide transporter (VNUT) is a membrane protein that is responsible for vesicular storage and subsequent vesicular release of nucleotides, such as ATP, and plays an essential role in purinergic chemical transmission. In the present study, we investigated whether VNUT is present in the rodent retina to define the site(s) of vesicular ATP release. In the mouse retina, reverse transcription polymerase chain reaction (RT-PCR) and immunological analyses using specific anti-VNUT antibodies indicated that VNUT is expressed as a polypeptide with an apparent molecular mass of 59 kDa. VNUT is widely distributed throughout the inner and outer retinal layers, particularly in the outer segment of photoreceptors, outer plexiform layer, inner plexiform layer, and ganglion cell layer. VNUT is colocalized with vesicular glutamate transporter 1 and synaptophysin in photoreceptor cells, while it is colocalized with vesicular γ-aminobutyric acid (GABA) transporter in amacrine cells and bipolar cells. VNUT is also present in astrocytes and Müller cells. The retina from VNUT knockout (VNUT(-/-)) mice showed the loss of VNUT immunoreactivity. The retinal membrane fraction took up radiolabeled ATP in diisothiocyanate stilbene disulfonic acid (DIDS)-, an inhibitor of VNUT, and bafilomycin A1-, a vacuolar adenosine triphosphatase (ATPase) inhibitor, in a sensitive manner, while membranes from VNUT(-/-) mice showed the loss of DIDS-sensitive ATP uptake. Taken together, these results indicate that functional VNUT is expressed in the rodent retina and suggest that ATP is released from photoreceptor cells, bipolar cells, amacrine cells, and astrocytes as well as Müller cells to initiate purinergic chemical transmission.
[Mh] Termos MeSH primário: Retina/metabolismo
Proteínas Vesiculares de Transporte de Neurotransmissores/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Animais
Masculino
Camundongos Endogâmicos C57BL
Camundongos Knockout
RNA Mensageiro/metabolismo
Proteínas Vesiculares de Transporte de Neurotransmissores/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (Vesicular Neurotransmitter Transport Proteins); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170107
[Lr] Data última revisão:
170107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160405
[St] Status:MEDLINE
[do] DOI:10.1248/bpb.b15-00872


  2 / 21 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26514205
[Au] Autor:Omote H; Miyaji T; Hiasa M; Juge N; Moriyama Y
[Ad] Endereço:Department of Membrane Biochemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama 700-8530, Japan; email: moriyama@pheasant.pharm.okayama-u.ac.jp , omote@pheasant.pharm.okayama-u.ac.jp.
[Ti] Título:Structure, Function, and Drug Interactions of Neurotransmitter Transporters in the Postgenomic Era.
[So] Source:Annu Rev Pharmacol Toxicol;56:385-402, 2016.
[Is] ISSN:1545-4304
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Vesicular neurotransmitter transporters are responsible for the accumulation of neurotransmitters in secretory vesicles and play essential roles in chemical transmission. The SLC17 family contributes to sequestration of anionic neurotransmitters such as glutamate, aspartate, and nucleotides. Identification and subsequent cellular and molecular biological studies of SLC17 transporters unveiled the principles underlying the actions of these transporters. Recent progress in reconstitution methods in combination with postgenomic approaches has advanced studies on neurotransmitter transporters. This review summarizes the molecular properties of SLC17-type transporters and recent findings regarding the novel SLC18 transporter.
[Mh] Termos MeSH primário: Transporte Biológico/fisiologia
Interações Medicamentosas/fisiologia
Proteínas Vesiculares de Transporte de Neurotransmissores/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Vesicular Neurotransmitter Transport Proteins)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:160107
[Lr] Data última revisão:
160107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151031
[St] Status:MEDLINE
[do] DOI:10.1146/annurev-pharmtox-010814-124816


  3 / 21 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:24745982
[Au] Autor:Anne C; Gasnier B
[Ad] Endereço:Université Paris Descartes, Sorbonne Paris Cité, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 8192, Centre Universitaire des Saints-Pères, Paris, France.
[Ti] Título:Vesicular neurotransmitter transporters: mechanistic aspects.
[So] Source:Curr Top Membr;73:149-74, 2014.
[Is] ISSN:1063-5823
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Secondary transporters driven by a V-type H⁺-ATPase accumulate nonpeptide neurotransmitters into synaptic vesicles. Distinct transporter families are involved depending on the neurotransmitter. Monoamines and acetylcholine on the one hand, and glutamate and ATP on the other hand, are accumulated by SLC18 and SLC17 transporters, respectively, which belong to the major facilitator superfamily (MFS). GABA and glycine accumulate through a common SLC32 transporter from the amino acid/polyamine/organocation (APC) superfamily. Although crystallographic structures are not yet available for any vesicular transporter, homology modeling studies of MFS-type vesicular transporters based on distantly related bacterial structures recently provided significant advances, such as the characterization of substrate-binding pockets or the identification of spatial clusters acting as hinge points during the alternating-access cycle. However, several basic issues, such as the ion stoichiometry of vesicular amino acid transporters, remain unsettled.
[Mh] Termos MeSH primário: Proteínas Vesiculares de Transporte de Neurotransmissores/metabolismo
[Mh] Termos MeSH secundário: Animais
Transporte Biológico
Cloretos/metabolismo
Seres Humanos
Ligantes
Proteínas Vesiculares de Transporte de Neurotransmissores/antagonistas & inibidores
Proteínas Vesiculares de Transporte de Neurotransmissores/química
Proteínas Vesiculares de Transporte de Neurotransmissores/classificação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Chlorides); 0 (Ligands); 0 (Vesicular Neurotransmitter Transport Proteins)
[Em] Mês de entrada:1411
[Cu] Atualização por classe:140421
[Lr] Data última revisão:
140421
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140422
[St] Status:MEDLINE


  4 / 21 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:24704795
[Au] Autor:Martin CA; Krantz DE
[Ad] Endereço:UCLA Interdepartmental Program in Molecular Toxicology, United States.
[Ti] Título:Drosophila melanogaster as a genetic model system to study neurotransmitter transporters.
[So] Source:Neurochem Int;73:71-88, 2014 Jul.
[Is] ISSN:1872-9754
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The model genetic organism Drosophila melanogaster, commonly known as the fruit fly, uses many of the same neurotransmitters as mammals and very similar mechanisms of neurotransmitter storage, release and recycling. This system offers a variety of powerful molecular-genetic methods for the study of transporters, many of which would be difficult in mammalian models. We review here progress made using Drosophila to understand the function and regulation of neurotransmitter transporters and discuss future directions for its use.
[Mh] Termos MeSH primário: Proteínas de Drosophila/genética
Drosophila melanogaster/metabolismo
Proteínas de Transporte de Neurotransmissores/genética
[Mh] Termos MeSH secundário: Animais
Membrana Celular/efeitos dos fármacos
Membrana Celular/metabolismo
Proteínas de Drosophila/metabolismo
Seres Humanos
Proteínas de Transporte de Neurotransmissores/efeitos dos fármacos
Proteínas de Transporte de Neurotransmissores/metabolismo
Proteínas Vesiculares de Transporte de Neurotransmissores/genética
Proteínas Vesiculares de Transporte de Neurotransmissores/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Neurotransmitter Transport Proteins); 0 (Vesicular Neurotransmitter Transport Proteins)
[Em] Mês de entrada:1502
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140408
[St] Status:MEDLINE


  5 / 21 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:24696406
[Au] Autor:Marecos C; Ng J; Kurian MA
[Ad] Endereço:Department of Neurology, Great Ormond Street Hospital for Children NHS Foundation Trust, London, UK.
[Ti] Título:What is new for monoamine neurotransmitter disorders?
[So] Source:J Inherit Metab Dis;37(4):619-26, 2014 Jul.
[Is] ISSN:1573-2665
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The monoamine neurotransmitter disorders are increasingly recognized as an expanding group of inherited neurometabolic syndromes caused by disturbances in the synthesis, transport and metabolism of the biogenic amines, including the catecholamines (dopamine, norepinephrine, and epinephrine) and serotonin. Disturbances in monoamine metabolism lead to neurological syndromes that frequently mimic other conditions, such as hypoxic ischemic encephalopathy, cerebral palsy, parkinsonism-dystonia syndromes, primary genetic dystonia and paroxysmal disorders. As a consequence, neurotransmitter disorders are frequently misdiagnosed. Early and accurate diagnosis of these neurotransmitter disorders is important, as many are highly amenable to, and some even cured by, therapeutic intervention. In this review, we highlight recent advances in the field, particularly the recent extensive characterization of known neurotransmitter disorders and identification of novel neurotransmitter disorders. We also provide an overview of current and future research in the field focused on developing novel treatment strategies.
[Mh] Termos MeSH primário: Monoaminas Biogênicas
Encefalopatias Metabólicas Congênitas/terapia
Neurotransmissores/deficiência
[Mh] Termos MeSH secundário: Erros Inatos do Metabolismo dos Aminoácidos/diagnóstico
Erros Inatos do Metabolismo dos Aminoácidos/terapia
Descarboxilases de Aminoácido-L-Aromático/deficiência
Monoaminas Biogênicas/metabolismo
Encefalopatias Metabólicas Congênitas/diagnóstico
Proteínas da Membrana Plasmática de Transporte de Dopamina/deficiência
Proteínas da Membrana Plasmática de Transporte de Dopamina/genética
Distonia/diagnóstico
Distonia/terapia
Distúrbios Distônicos/congênito
Distúrbios Distônicos/diagnóstico
Distúrbios Distônicos/terapia
Seres Humanos
Erros Inatos do Metabolismo/diagnóstico
Erros Inatos do Metabolismo/terapia
Neurotransmissores/metabolismo
Transtornos Psicomotores/diagnóstico
Transtornos Psicomotores/terapia
Síndrome
Proteínas Vesiculares de Transporte de Neurotransmissores/deficiência
Proteínas Vesiculares de Transporte de Neurotransmissores/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Biogenic Monoamines); 0 (Dopamine Plasma Membrane Transport Proteins); 0 (Neurotransmitter Agents); 0 (Vesicular Neurotransmitter Transport Proteins); EC 4.1.1.28 (Aromatic-L-Amino-Acid Decarboxylases)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140404
[St] Status:MEDLINE
[do] DOI:10.1007/s10545-014-9697-4


  6 / 21 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:22961619
[Au] Autor:Lendvai D; Morawski M; Négyessy L; Gáti G; Jäger C; Baksa G; Glasz T; Attems J; Tanila H; Arendt T; Harkany T; Alpár A
[Ad] Endereço:Department of Anatomy, Histology and Embryology, Semmelweis University, Budapest, Hungary.
[Ti] Título:Neurochemical mapping of the human hippocampus reveals perisynaptic matrix around functional synapses in Alzheimer's disease.
[So] Source:Acta Neuropathol;125(2):215-29, 2013 Feb.
[Is] ISSN:1432-0533
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Perineuronal matrix is an extracellular protein scaffold to shape neuronal responsiveness and survival. Whilst perineuronal nets engulf the somatodendritic axis of neurons, axonal coats are focal extracellular protein aggregates surrounding individual synapses. Here, we addressed the chemical identity and subcellular localization of both perineuronal and perisynaptic matrices in the human hippocampus, whose neuronal circuitry is progressively compromised in Alzheimer's disease. We hypothesized that (1) the cellular expression sites of chondroitin sulphate proteoglycan-containing extracellular matrix associate with specific neuronal identities, reflecting network dynamics, and (2) the regional distribution and molecular composition of axonal coats must withstand Alzheimer's disease-related modifications to protect functional synapses. We show by epitope-specific antibodies that the perineuronal protomap of the human hippocampus is distinct from other mammals since pyramidal cells but not calretinin(+) and calbindin(+) interneurons, neurochemically classified as novel neuronal subtypes, lack perineuronal nets. We find that cartilage link protein-1 and brevican-containing matrices form isolated perisynaptic coats, engulfing both inhibitory and excitatory terminals in the dentate gyrus and entorhinal cortex. Ultrastructural analysis revealed that presynaptic neurons contribute components of perisynaptic coats via axonal transport. We demonstrate, by combining biochemical profiling and neuroanatomy in Alzheimer's patients and transgenic (APdE9) mice, the preserved turnover and distribution of axonal coats around functional synapses along dendrite segments containing hyperphosphorylated tau and in amyloid-ß-laden hippocampal microdomains. We conclude that the presynapse-driven formation of axonal coats is a candidate mechanism to maintain synapse integrity under neurodegenerative conditions.
[Mh] Termos MeSH primário: Doença de Alzheimer/metabolismo
Hipocampo/química
Sinapses/metabolismo
[Mh] Termos MeSH secundário: Agrecanas/metabolismo
Doença de Alzheimer/patologia
Peptídeos beta-Amiloides/biossíntese
Peptídeos beta-Amiloides/genética
Animais
Axônios/metabolismo
Western Blotting
Mapeamento Encefálico
Brevicam/metabolismo
Proteínas de Ligação ao Cálcio/metabolismo
Estudos de Coortes
Dendritos/metabolismo
Matriz Extracelular/metabolismo
Proteínas da Matriz Extracelular/metabolismo
Feminino
Seres Humanos
Imuno-Histoquímica
Masculino
Camundongos
Camundongos Transgênicos
Microscopia Confocal
Microscopia Eletrônica
Microscopia de Fluorescência
Proteoglicanas/metabolismo
Sinapses/patologia
Proteínas Vesiculares de Transporte de Neurotransmissores/metabolismo
Proteínas tau/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Aggrecans); 0 (Amyloid beta-Peptides); 0 (Brevican); 0 (Calcium-Binding Proteins); 0 (Extracellular Matrix Proteins); 0 (Proteoglycans); 0 (Vesicular Neurotransmitter Transport Proteins); 0 (link protein); 0 (tau Proteins)
[Em] Mês de entrada:1306
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120911
[St] Status:MEDLINE
[do] DOI:10.1007/s00401-012-1042-0


  7 / 21 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:22811938
[Au] Autor:Amaral MD; Pozzo-Miller L
[Ad] Endereço:Department of Neurobiology, Civitan International Research Center, The University of Alabama at Birmingham, SHEL-1002, 1825 University Boulevard, Birmingham, AL 35294-2182, USA.
[Ti] Título:Intracellular Ca2+ stores and Ca2+ influx are both required for BDNF to rapidly increase quantal vesicular transmitter release.
[So] Source:Neural Plast;2012:203536, 2012.
[Is] ISSN:1687-5443
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Brain-derived neurotrophic factor (BDNF) is well known as a survival factor during brain development as well as a regulator of adult synaptic plasticity. One potential mechanism to initiate BDNF actions is through its modulation of quantal presynaptic transmitter release. In response to local BDNF application to CA1 pyramidal neurons, the frequency of miniature excitatory postsynaptic currents (mEPSC) increased significantly within 30 seconds; mEPSC amplitude and kinetics were unchanged. This effect was mediated via TrkB receptor activation and required both full intracellular Ca(2+) stores as well as extracellular Ca(2+). Consistent with a role of Ca(2+)-permeable plasma membrane channels of the TRPC family, the inhibitor SKF96365 prevented the BDNF-induced increase in mEPSC frequency. Furthermore, labeling presynaptic terminals with amphipathic styryl dyes and then monitoring their post-BDNF destaining in slice cultures by multiphoton excitation microscopy revealed that the increase in frequency of mEPSCs reflects vesicular fusion events. Indeed, BDNF application to CA3-CA1 synapses in TTX rapidly enhanced FM1-43 or FM2-10 destaining with a time course that paralleled the phase of increased mEPSC frequency. We conclude that BDNF increases mEPSC frequency by boosting vesicular fusion through a presynaptic, Ca(2+)-dependent mechanism involving TrkB receptors, Ca(2+) stores, and TRPC channels.
[Mh] Termos MeSH primário: Fator Neurotrófico Derivado do Encéfalo/farmacologia
Cálcio/metabolismo
Proteínas Vesiculares de Transporte de Neurotransmissores/metabolismo
[Mh] Termos MeSH secundário: Animais
Região CA1 Hipocampal/efeitos dos fármacos
Região CA1 Hipocampal/fisiologia
Bloqueadores dos Canais de Cálcio/farmacologia
Potenciais Pós-Sinápticos Excitadores/efeitos dos fármacos
Imidazóis/farmacologia
Cinética
Microscopia de Fluorescência
Técnicas de Cultura de Órgãos
Técnicas de Patch-Clamp
Terminações Pré-Sinápticas/efeitos dos fármacos
Células Piramidais/efeitos dos fármacos
Células Piramidais/fisiologia
Ratos
Ratos Sprague-Dawley
Receptor trkB/efeitos dos fármacos
Estimulação Química
Tetrodotoxina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Brain-Derived Neurotrophic Factor); 0 (Calcium Channel Blockers); 0 (Imidazoles); 0 (Vesicular Neurotransmitter Transport Proteins); 4368-28-9 (Tetrodotoxin); EC 2.7.10.1 (Receptor, trkB); I61V87164A (1-(2-(3-(4-methoxyphenyl)propoxy)-4-methoxyphenylethyl)-1H-imidazole); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1211
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120720
[St] Status:MEDLINE
[do] DOI:10.1155/2012/203536


  8 / 21 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:22296263
[Au] Autor:Owesson-White CA; Roitman MF; Sombers LA; Belle AM; Keithley RB; Peele JL; Carelli RM; Wightman RM
[Ad] Endereço:Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
[Ti] Título:Sources contributing to the average extracellular concentration of dopamine in the nucleus accumbens.
[So] Source:J Neurochem;121(2):252-62, 2012 Apr.
[Is] ISSN:1471-4159
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mesolimbic dopamine neurons fire in both tonic and phasic modes resulting in detectable extracellular levels of dopamine in the nucleus accumbens (NAc). In the past, different techniques have targeted dopamine levels in the NAc to establish a basal concentration. In this study, we used in vivo fast scan cyclic voltammetry (FSCV) in the NAc of awake, freely moving rats. The experiments were primarily designed to capture changes in dopamine caused by phasic firing - that is, the measurement of dopamine 'transients'. These FSCV measurements revealed for the first time that spontaneous dopamine transients constitute a major component of extracellular dopamine levels in the NAc. A series of experiments were designed to probe regulation of extracellular dopamine. Lidocaine was infused into the ventral tegmental area, the site of dopamine cell bodies, to arrest neuronal firing. While there was virtually no instantaneous change in dopamine concentration, longer sampling revealed a decrease in dopamine transients and a time-averaged decrease in the extracellular level. Dopamine transporter inhibition using intravenous GBR12909 injections increased extracellular dopamine levels changing both frequency and size of dopamine transients in the NAc. To further unmask the mechanics governing extracellular dopamine levels we used intravenous injection of the vesicular monoamine transporter (VMAT2) inhibitor, tetrabenazine, to deplete dopamine storage and increase cytoplasmic dopamine in the nerve terminals. Tetrabenazine almost abolished phasic dopamine release but increased extracellular dopamine to ∼500 nM, presumably by inducing reverse transport by dopamine transporter (DAT). Taken together, data presented here show that average extracellular dopamine in the NAc is low (20-30 nM) and largely arises from phasic dopamine transients.
[Mh] Termos MeSH primário: Dopamina/metabolismo
Espaço Extracelular/metabolismo
Núcleo Accumbens/metabolismo
[Mh] Termos MeSH secundário: Anestésicos Locais/administração & dosagem
Anestésicos Locais/farmacologia
Animais
Dopamina/fisiologia
Proteínas da Membrana Plasmática de Transporte de Dopamina/antagonistas & inibidores
Fenômenos Eletrofisiológicos
Lidocaína/administração & dosagem
Lidocaína/farmacologia
Masculino
Microdiálise
Técnicas de Patch-Clamp
Ratos
Ratos Sprague-Dawley
Tetrabenazina/farmacologia
Área Tegmentar Ventral
Proteínas Vesiculares de Transporte de Monoamina/antagonistas & inibidores
Proteínas Vesiculares de Transporte de Monoamina/metabolismo
Proteínas Vesiculares de Transporte de Neurotransmissores/antagonistas & inibidores
Proteínas Vesiculares de Transporte de Neurotransmissores/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Anesthetics, Local); 0 (Dopamine Plasma Membrane Transport Proteins); 0 (Slc18a2 protein, rat); 0 (Vesicular Monoamine Transport Proteins); 0 (Vesicular Neurotransmitter Transport Proteins); 98PI200987 (Lidocaine); VTD58H1Z2X (Dopamine); Z9O08YRN8O (Tetrabenazine)
[Em] Mês de entrada:1205
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120203
[St] Status:MEDLINE
[do] DOI:10.1111/j.1471-4159.2012.07677.x


  9 / 21 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:22054239
[Au] Autor:Hnasko TS; Edwards RH
[Ad] Endereço:Departments of Physiology & Neurology, University of California, San Francisco, California 94158-2517, USA. thomas.hnasko@ucsf.edu
[Ti] Título:Neurotransmitter corelease: mechanism and physiological role.
[So] Source:Annu Rev Physiol;74:225-43, 2012.
[Is] ISSN:1545-1585
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neurotransmitter identity is a defining feature of all neurons because it constrains the type of information they convey, but many neurons release multiple transmitters. Although the physiological role for corelease has remained poorly understood, the vesicular uptake of one transmitter can regulate filling with the other by influencing expression of the H(+) electrochemical driving force. In addition, the sorting of vesicular neurotransmitter transporters and other synaptic vesicle proteins into different vesicle pools suggests the potential for distinct modes of release. Corelease thus serves multiple roles in synaptic transmission.
[Mh] Termos MeSH primário: Neurotransmissores/fisiologia
Transmissão Sináptica/fisiologia
[Mh] Termos MeSH secundário: Acetilcolina/metabolismo
Animais
Ânions/metabolismo
Monoaminas Biogênicas/fisiologia
Cátions/metabolismo
Cloretos/metabolismo
Cloretos/fisiologia
Ácido Glutâmico/metabolismo
Ácido Glutâmico/fisiologia
Seres Humanos
Concentração de Íons de Hidrogênio
Neurotransmissores/metabolismo
Prótons
Vesículas Sinápticas/metabolismo
Vesículas Sinápticas/fisiologia
Proteínas Vesiculares de Transporte de Neurotransmissores/metabolismo
Ácido gama-Aminobutírico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Anions); 0 (Biogenic Monoamines); 0 (Cations); 0 (Chlorides); 0 (Neurotransmitter Agents); 0 (Protons); 0 (Vesicular Neurotransmitter Transport Proteins); 3KX376GY7L (Glutamic Acid); 56-12-2 (gamma-Aminobutyric Acid); N9YNS0M02X (Acetylcholine)
[Em] Mês de entrada:1206
[Cu] Atualização por classe:161025
[Lr] Data última revisão:
161025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:111108
[St] Status:MEDLINE
[do] DOI:10.1146/annurev-physiol-020911-153315


  10 / 21 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:22052906
[Au] Autor:Miyaji T; Sawada K; Omote H; Moriyama Y
[Ad] Endereço:Advanced Science Research Center, Okayama University, Okayama 700-8530, Japan.
[Ti] Título:Divalent cation transport by vesicular nucleotide transporter.
[So] Source:J Biol Chem;286(50):42881-7, 2011 Dec 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The vesicular nucleotide transporter (VNUT) is a secretory vesicle protein that is responsible for the vesicular storage and subsequent exocytosis of ATP (Sawada, K., Echigo, N., Juge, N., Miyaji, T., Otsuka, M., Omote, H., and Moriyama, Y. (2008) Proc. Natl. Acad. Sci. U.S.A. 105, 5683-5686). Because VNUT actively transports ATP in a membrane potential (Δψ)-dependent manner irrespective of divalent cations such as Mg(2+) and Ca(2+), VNUT recognizes free ATP as a transport substrate. However, whether or not VNUT transports chelating complexes with divalent cations remains unknown. Here, we show that proteoliposomes containing purified VNUT actively took up Mg(2+) when ATP was present, as detected by atomic absorption spectroscopy. The VNUT-containing proteoliposomes also took up radioactive Ca(2+) upon imposing Δψ (positive-inside) but not ΔpH. The Δψ-driven Ca(2+) uptake required ATP and a millimolar concentration of Cl(-), which was inhibited by Evans blue, a specific inhibitor of SLC17-type transporters. VNUT in which Arg-119 was specifically mutated to alanine, the counterpart of the essential amino acid residue of the SLC17 family, lost the ability to take up both ATP and Ca(2+). Ca(2+) uptake was also inhibited in the presence of various divalent cations such as Mg(2+). Kinetic analysis indicated that Ca(2+) or Mg(2+) did not affect the apparent affinity for ATP. RNAi of the VNUT gene in PC12 cells decreased the vesicular Mg(2+) concentration to 67.7%. These results indicate that VNUT transports both nucleotides and divalent cations probably as chelating complexes and suggest that VNUT functions as a divalent cation importer in secretory vesicles under physiological conditions.
[Mh] Termos MeSH primário: Cátions Bivalentes/metabolismo
Nucleotídeos/metabolismo
Proteínas Vesiculares de Transporte de Neurotransmissores/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Animais
Transporte Biológico
Cálcio/metabolismo
Proteínas de Transporte de Glutamato da Membrana Plasmática/genética
Proteínas de Transporte de Glutamato da Membrana Plasmática/metabolismo
Seres Humanos
Cinética
Magnésio/metabolismo
Camundongos
Células PC12
Ratos
Proteínas Cotransportadoras de Sódio-Fosfato Tipo III/metabolismo
Proteínas Vesiculares de Transporte de Neurotransmissores/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cations, Divalent); 0 (Glutamate Plasma Membrane Transport Proteins); 0 (Nucleotides); 0 (Sodium-Phosphate Cotransporter Proteins, Type III); 0 (Vesicular Neurotransmitter Transport Proteins); 8L70Q75FXE (Adenosine Triphosphate); I38ZP9992A (Magnesium); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1203
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:111105
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M111.277269



página 1 de 3 ir para página          
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde