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Pesquisa : D12.776.157.530.450.625.139 [Categoria DeCS]
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  1 / 1027 MEDLINE  
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[PMID]:28535436
[Au] Autor:Yan W; Li L; Li G; Zhao S
[Ad] Endereço:Institute of Agricultural Quality Standards & Testing Technology, Hubei Academy of Agricultural Sciences, Wuhan 430064, China.
[Ti] Título:Microcystin-LR induces changes in the GABA neurotransmitter system of zebrafish.
[So] Source:Aquat Toxicol;188:170-176, 2017 Jul.
[Is] ISSN:1879-1514
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:It has been reported that exposure to microcystins altered adult zebrafish swimming performance parameters, but the possible mechanisms of action remain unknown. Neuronal activity depends on the balance between the number of excitatory and inhibitory processes which are associated with neurotransmitters. In the present study, zebrafish embryos (5 d post-fertilization) were exposed to 0, 0.3, 3 and 30µg/L (microcystin-LR) MCLR for 90day until reaching sexual maturity. To investigate the effects of MCLR on the neurotransmitter system, mRNA levels involved in amino acid g-aminobutyric acid (GABA) and glutamate metabolic pathways were tested using quantitative real-time PCR. Significant increase of GABAA receptor, alpha 1 (gabra1), glutamate decarboxylase (gad1b), glutaminase (glsa) and reduction of mRNA expression of GABA transporter (gat1) at transcriptional level were observed in the brain. Meanwhile, western blotting showed that the protein levels of gabra1, gad1b were induced by MCLR, whereas the expression of gat1 was decreased. In addition, MCLR induced severe damage to cerebrum ultrastructure, showing edematous and collapsed myelinated nerve fibers, distention of endoplasmic reticulum and swelling mitochondria. Our results suggested that MCLR showed neurotoxicity in zebrafish which might attribute to the disorder of GABA neurotransmitter pathway.
[Mh] Termos MeSH primário: Embrião não Mamífero/efeitos dos fármacos
Microcistinas/toxicidade
Poluentes Químicos da Água/toxicidade
Peixe-Zebra/metabolismo
Ácido gama-Aminobutírico/metabolismo
[Mh] Termos MeSH secundário: Animais
Encéfalo/efeitos dos fármacos
Encéfalo/metabolismo
Encéfalo/patologia
Embrião não Mamífero/metabolismo
Proteínas da Membrana Plasmática de Transporte de GABA/genética
Proteínas da Membrana Plasmática de Transporte de GABA/metabolismo
Glutamato Descarboxilase/genética
Glutamato Descarboxilase/metabolismo
Ácido Glutâmico/metabolismo
Glutaminase/genética
RNA Mensageiro/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Receptores de GABA-A/genética
Receptores de GABA-A/metabolismo
Peixe-Zebra/genética
Proteínas de Peixe-Zebra/genética
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GABA Plasma Membrane Transport Proteins); 0 (Microcystins); 0 (RNA, Messenger); 0 (Receptors, GABA-A); 0 (Water Pollutants, Chemical); 0 (Zebrafish Proteins); 3KX376GY7L (Glutamic Acid); 56-12-2 (gamma-Aminobutyric Acid); EC 3.5.1.2 (Glutaminase); EC 4.1.1.15 (Glutamate Decarboxylase); EC 4.1.1.15 (glutamate decarboxylase 1); EQ8332842Y (cyanoginosin LR)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170524
[St] Status:MEDLINE


  2 / 1027 MEDLINE  
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[PMID]:28303263
[Au] Autor:Zhang YV; Ormerod KG; Littleton JT
[Ad] Endereço:The Picower Institute for Learning and Memory, Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.
[Ti] Título:Astrocyte Ca Influx Negatively Regulates Neuronal Activity.
[So] Source:eNeuro;4(2), 2017 Mar-Apr.
[Is] ISSN:2373-2822
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Maintenance of neural circuit activity requires appropriate regulation of excitatory and inhibitory synaptic transmission. Recently, glia have emerged as key partners in the modulation of neuronal excitability; however, the mechanisms by which glia regulate neuronal signaling are still being elucidated. Here, we describe an analysis of how Ca signals within astrocyte-like glia regulate excitability in the nervous system. We find that astrocytes exhibit robust Ca oscillatory activity manifested by fast, recurrent microdomain Ca fluctuations within processes that infiltrate the synaptic neuropil. Unlike the enhanced neuronal activity and behavioral seizures that were previously observed during manipulations that trigger Ca influx into cortex glia, we find that acute induction of astrocyte Ca influx leads to a rapid onset of behavioral paralysis and a suppression of neuronal activity. We observe that Ca influx triggers rapid endocytosis of the GABA transporter (GAT) from astrocyte plasma membranes, suggesting that increased synaptic GABA levels contribute to the neuronal silencing and paralysis. We identify Rab11 as a novel regulator of GAT trafficking that is required for this form of activity regulation. Suppression of Rab11 function strongly offsets the reduction of neuronal activity caused by acute astrocyte Ca influx, likely by inhibiting GAT endocytosis. Our data provide new insights into astrocyte Ca signaling and indicate that distinct glial subtypes in the brain can mediate opposing effects on neuronal excitability.
[Mh] Termos MeSH primário: Astrócitos/metabolismo
Cálcio/metabolismo
Neurônios/metabolismo
Transmissão Sináptica/fisiologia
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Astrócitos/citologia
Encéfalo/citologia
Encéfalo/metabolismo
Cátions Bivalentes/metabolismo
Membrana Celular/metabolismo
Drosophila
Proteínas de Drosophila/metabolismo
Endocitose/fisiologia
Proteínas da Membrana Plasmática de Transporte de GABA/metabolismo
Neurônios/citologia
Paralisia/metabolismo
Canal de Cátion TRPA1
Canais de Cátion TRPC/metabolismo
Ácido gama-Aminobutírico/metabolismo
Proteínas rab de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
0 (Cations, Divalent); 0 (Drosophila Proteins); 0 (GABA Plasma Membrane Transport Proteins); 0 (TRPA1 Cation Channel); 0 (TRPC Cation Channels); 0 (TrpA1 protein, Drosophila); 56-12-2 (gamma-Aminobutyric Acid); EC 3.6.1.- (Rab11 protein, Drosophila); EC 3.6.5.2 (rab GTP-Binding Proteins); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170318
[St] Status:MEDLINE


  3 / 1027 MEDLINE  
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[PMID]:28296282
[Au] Autor:Agusti A; Hernández-Rabaza V; Balzano T; Taoro-Gonzalez L; Ibañez-Grau A; Cabrera-Pastor A; Fustero S; Llansola M; Montoliu C; Felipo V
[Ad] Endereço:Laboratory of Neurobiology, Centro de Investigación Príncipe Felipe, Valencia, Spain.
[Ti] Título:Sildenafil reduces neuroinflammation in cerebellum, restores GABAergic tone, and improves motor in-coordination in rats with hepatic encephalopathy.
[So] Source:CNS Neurosci Ther;23(5):386-394, 2017 May.
[Is] ISSN:1755-5949
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIMS: Patients with liver disease may develop hepatic encephalopathy (HE), with cognitive impairment and motor in-coordination. Rats with HE due to portacaval shunts (PCS) show motor in-coordination. We hypothesized that in PCS rats: (i) Motor in-coordination would be due to enhanced GABAergic tone in cerebellum; (ii) increased GABAergic tone would be due to neuroinflammation; (iii) increasing cGMP would reduce neuroinflammation and GABAergic tone and restore motor coordination. To assess these hypotheses, we assessed if (i) treatment with sildenafil reduces neuroinflammation; (ii) reduced neuroinflammation is associated with reduced GABAergic tone and restored motor coordination. METHODS: Rats were treated with sildenafil to increase cGMP. Microglia and astrocytes activation were analyzed by immunohistochemistry, extracellular GABA by microdialysis, and motor coordination in the beam walking. RESULTS: PCS rats show neuroinflammation in cerebellum, with microglia and astrocytes activation, increased IL-1b and TNF-a and reduced YM-1 and IL-4. Membrane expression of the GABA transporter GAT1 is reduced, while GAT3 is increased. Extracellular GABA and motor in-coordination are increased. Sildenafil treatment eliminates neuroinflammation, microglia and astrocytes activation; changes in membrane expression of GABA transporters; and restores motor coordination. CONCLUSIONS: This study supports an interplay between cGMP-neuroinflammation and GABAergic neurotransmission in impairing motor coordination in PCS rats.
[Mh] Termos MeSH primário: Anti-Inflamatórios não Esteroides/farmacologia
Cerebelo/efeitos dos fármacos
Encefalopatia Hepática/tratamento farmacológico
Destreza Motora/efeitos dos fármacos
Citrato de Sildenafila/farmacologia
[Mh] Termos MeSH secundário: Animais
Astrócitos/efeitos dos fármacos
Astrócitos/patologia
Astrócitos/fisiologia
Cerebelo/imunologia
Cerebelo/patologia
Modelos Animais de Doenças
Proteínas da Membrana Plasmática de Transporte de GABA/metabolismo
Encefalopatia Hepática/patologia
Encefalopatia Hepática/fisiopatologia
Interleucina-1beta/metabolismo
Interleucina-4/metabolismo
Masculino
Microglia/efeitos dos fármacos
Microglia/patologia
Microglia/fisiologia
Destreza Motora/fisiologia
Neuroimunomodulação/efeitos dos fármacos
Neuroimunomodulação/fisiologia
Ratos Wistar
Fator de Necrose Tumoral alfa/metabolismo
Ácido gama-Aminobutírico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents, Non-Steroidal); 0 (GABA Plasma Membrane Transport Proteins); 0 (IL1B protein, rat); 0 (Interleukin-1beta); 0 (Slc6a11 protein, rat); 0 (Tumor Necrosis Factor-alpha); 207137-56-2 (Interleukin-4); 56-12-2 (gamma-Aminobutyric Acid); BW9B0ZE037 (Sildenafil Citrate)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE
[do] DOI:10.1111/cns.12688


  4 / 1027 MEDLINE  
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[PMID]:28213519
[Au] Autor:Dayan O; Nagarajan A; Shah R; Ben-Yona A; Forrest LR; Kanner BI
[Ad] Endereço:From the Department of Biochemistry and Molecular Biology, Institute for Medical Research Israel-Canada, Hebrew University Hadassah Medical School, Jerusalem 91120, Israel and.
[Ti] Título:An Extra Amino Acid Residue in Transmembrane Domain 10 of the γ-Aminobutyric Acid (GABA) Transporter GAT-1 Is Required for Efficient Ion-coupled Transport.
[So] Source:J Biol Chem;292(13):5418-5428, 2017 Mar 31.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The GABA transporter GAT-1 mediates electrogenic transport of its substrate together with sodium and chloride. It is a member of the neurotransmitter:sodium:symporters, which are crucial for synaptic transmission. Compared with all other neurotransmitter:sodium:symporters, GAT-1 and other members of the GABA transporter subfamily all contain an extra amino acid residue at or near a conserved glycine in transmembrane segment 10. Therefore, we studied the functional impact of deletion and replacement mutants of Gly-457 and its two adjacent residues in GAT-1. The glycine replacement mutants were devoid of transport activity, but remarkably the deletion mutant was active, as were mutants obtained by deleting positions on either side of Gly-457. However, the inward rectification of GABA-induced transport currents by all three deletion mutants was diminished, and the charge-to-flux ratio was increased by more than 2.5-fold, both of which indicate substantial uncoupled transport. These observations suggest that the deletions render the transporters less tightly packed. Consistent with this interpretation, the inactive G457A mutant was partially rescued by removing the adjacent serine residue. Moreover, the activity of several gating mutants was also partially rescued upon deletion of Gly-457. Structural modeling showed that the stretch surrounding Gly-457 is likely to form a π-helix. Our data indicate that the "extra" residue in transmembrane domain 10 of the GABA transporter GAT-1 provides extra bulk, probably in the form of a π-helix, which is required for stringent gating and tight coupling of ion and substrate fluxes in the GABA transporter family.
[Mh] Termos MeSH primário: Proteínas da Membrana Plasmática de Transporte de GABA/química
Glicina/genética
Transporte de Íons
Mutagênese Sítio-Dirigida
[Mh] Termos MeSH secundário: Aminoácidos
Sequência Conservada/genética
Proteínas da Membrana Plasmática de Transporte de GABA/genética
Proteínas da Membrana Plasmática de Transporte de GABA/metabolismo
Células HeLa
Seres Humanos
Conformação Proteica
Domínios Proteicos
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (GABA Plasma Membrane Transport Proteins); TE7660XO1C (Glycine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170612
[Lr] Data última revisão:
170612
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170219
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.775189


  5 / 1027 MEDLINE  
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[PMID]:28129110
[Au] Autor:Li X; Wang Z; Tan L; Wang Y; Lu C; Chen R; Zhang S; Gao Y; Liu Y; Yin Y; Liu X; Liu E; Yang Y; Hu Y; Xu Z; Xu F; Wang J; Liu GP; Wang JZ
[Ad] Endereço:Department of Pathophysiology, School of Basic Medicine and Collaborative Innovation Center for Brain Science, Key Laboratory of Ministry of Education of China for Neurological Disorders, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China.
[Ti] Título:Correcting miR92a-vGAT-Mediated GABAergic Dysfunctions Rescues Human Tau-Induced Anxiety in Mice.
[So] Source:Mol Ther;25(1):140-152, 2017 Jan 04.
[Is] ISSN:1525-0024
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Patients with Alzheimer's disease (AD) commonly show anxiety behaviors, but the molecular mechanisms are not clear and no efficient intervention exists. Here, we found that overexpression of human wild-type, full-length tau (termed htau) in hippocampus significantly decreased the extracellular γ-aminobutyric acid (GABA) level with inhibition of γ oscillation and the evoked inhibitory postsynaptic potential (eIPSP). With tau accumulation, the mice show age-dependent anxiety behaviors. Among the factors responsible for GABA synthesis, release, uptake, and transport, we found that accumulation of htau selectively suppressed expression of the intracellular vesicular GABA transporter (vGAT). Tau accumulation increased miR92a, which targeted vGAT mRNA 3' UTR and inhibited vGAT translation. Importantly, we found that upregulating GABA tones by intraperitoneal injection of midazolam (a GABA agonist), ChR2-mediated photostimulating and overexpressing vGAT, or blocking miR92a by using specific antagomir or inhibitor efficiently rescued the htau-induced GABAergic dysfunctions with attenuation of anxiety. Finally, we also demonstrated that vGAT level decreased while the miR92a increased in the AD brains. These findings demonstrate that the AD-like tau accumulation induces anxiety through disrupting miR92a-vGAT-GABA signaling, which reveals molecular mechanisms underlying the anxiety behavior in AD patients and potentially leads to the development of new therapeutics for tauopathies.
[Mh] Termos MeSH primário: Ansiedade/genética
Ansiedade/metabolismo
Proteínas da Membrana Plasmática de Transporte de GABA/genética
Neurônios GABAérgicos/metabolismo
MicroRNAs/genética
Tauopatias/genética
Tauopatias/metabolismo
[Mh] Termos MeSH secundário: Doença de Alzheimer/genética
Animais
Análise por Conglomerados
Modelos Animais de Doenças
Perfilação da Expressão Gênica
Regulação da Expressão Gênica
Hipocampo/metabolismo
Hipocampo/patologia
Seres Humanos
Camundongos
Interferência de RNA
Tauopatias/patologia
Proteínas tau/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GABA Plasma Membrane Transport Proteins); 0 (MicroRNAs); 0 (Mirn92 microRNA, mouse); 0 (tau Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170614
[Lr] Data última revisão:
170614
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170128
[St] Status:MEDLINE


  6 / 1027 MEDLINE  
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[PMID]:28125164
[Au] Autor:Lutz T; Wein T; Höfner G; Wanner KT
[Ad] Endereço:Department for Pharmacy, Center for Drug Research, Ludwig-Maximilians-Universität München, Butenandtstr. 7-13, 81377, Munich, Germany.
[Ti] Título:Development of Highly Potent GAT1 Inhibitors: Synthesis of Nipecotic Acid Derivatives with N-Arylalkynyl Substituents.
[So] Source:ChemMedChem;12(5):362-371, 2017 Mar 07.
[Is] ISSN:1860-7187
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:A new scaffold of highly potent and mGAT1-selective inhibitors has been developed. Compounds in this class are characterized by an alkyne-type spacer connecting nipecotic acid with an aromatic moiety. Preliminary evaluations made it apparent that a nipecotic acid derivative with an N-butynyl linker and a terminal 2-biphenyl residue exhibiting a binding affinity (pK ) of 7.61±0.03 to mGAT1 and uptake inhibition (pIC ) of 7.00±0.06 selective for mGAT1 could serve as a hit compound. Docking calculations for compounds based on this structure in an hGAT1 homology modeling study indicated binding affinities similar to or even higher than that of the well-known mGAT1 inhibitor tiagabine. Synthesis of the designed compounds was readily carried out by two consecutive cross-coupling reactions, giving flexible access to variously substituted biphenyl subunits. With an appropriate substitution pattern of the biphenyl moiety, the binding affinity of enantiopure (R)-nipecotic acid derivatives to mGAT1 increased to pK =8.33±0.01, and the uptake inhibitory potency up to pIC =7.72±0.02.
[Mh] Termos MeSH primário: Proteínas da Membrana Plasmática de Transporte de GABA/química
Inibidores da Captação de GABA/química
Ácidos Nipecóticos/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Proteínas da Membrana Plasmática de Transporte de GABA/metabolismo
Inibidores da Captação de GABA/síntese química
Inibidores da Captação de GABA/metabolismo
Células HEK293
Seres Humanos
Concentração Inibidora 50
Simulação de Acoplamento Molecular
Ácidos Nipecóticos/síntese química
Ácidos Nipecóticos/metabolismo
Isoformas de Proteínas/antagonistas & inibidores
Isoformas de Proteínas/metabolismo
Estrutura Terciária de Proteína
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GABA Plasma Membrane Transport Proteins); 0 (GABA Uptake Inhibitors); 0 (Nipecotic Acids); 0 (Protein Isoforms)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170627
[Lr] Data última revisão:
170627
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170127
[St] Status:MEDLINE
[do] DOI:10.1002/cmdc.201600599


  7 / 1027 MEDLINE  
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[PMID]:28122715
[Au] Autor:Siroky BJ; Kleene NK; Kleene SJ; Varnell CD; Comer RG; Liu J; Lu L; Pachciarz NW; Bissler JJ; Dixon BP
[Ad] Endereço:Division of Nephrology and Hypertension, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio.
[Ti] Título:Primary cilia regulate the osmotic stress response of renal epithelial cells through TRPM3.
[So] Source:Am J Physiol Renal Physiol;312(4):F791-F805, 2017 Apr 01.
[Is] ISSN:1522-1466
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Primary cilia sense environmental conditions, including osmolality, but whether cilia participate in the osmotic response in renal epithelial cells is not known. The transient receptor potential (TRP) channels TRPV4 and TRPM3 are osmoresponsive. TRPV4 localizes to cilia in certain cell types, while renal subcellular localization of TRPM3 is not known. We hypothesized that primary cilia are required for maximal activation of the osmotic response of renal epithelial cells and that ciliary TRPM3 and TRPV4 mediate that response. Ciliated [murine epithelial cells from the renal inner medullary collecting duct (mIMCD-3) and 176-5] and nonciliated (176-5Δ) renal cells expressed and Ciliary expression of TRPM3 was observed in mIMCD-3 and 176-5 cells and in wild-type mouse kidney tissue. TRPV4 was identified in cilia and apical membrane of mIMCD-3 cells by electrophysiology and in the cell body by immunofluorescence. Hyperosmolal stress at 500 mOsm/kg (via NaCl addition) induced the osmotic response genes betaine/GABA transporter ( ) and aldose reductase ( ) in all ciliated cell lines. This induction was attenuated in nonciliated cells. A TRPV4 agonist abrogated and induction in ciliated and nonciliated cells. A TRPM3 agonist attenuated and induction in ciliated cells only. TRPM3 knockout attenuated induction. Viability under osmotic stress was greater in ciliated than nonciliated cells. induction was also less in nonciliated than ciliated cells when mannitol was used to induce hyperosmolal stress. These findings suggest that primary cilia are required for the maximal osmotic response in renal epithelial cells and that TRPM3 is involved in this mechanism. TRPV4 appears to modulate the osmotic response independent of cilia.
[Mh] Termos MeSH primário: Células Epiteliais/metabolismo
Túbulos Renais Coletores/metabolismo
Osmorregulação
Pressão Osmótica
Canais de Cátion TRPM/metabolismo
[Mh] Termos MeSH secundário: Animais
Sistemas CRISPR-Cas
Linhagem Celular
Cílios/metabolismo
Células Epiteliais/efeitos dos fármacos
Proteínas da Membrana Plasmática de Transporte de GABA/genética
Proteínas da Membrana Plasmática de Transporte de GABA/metabolismo
Edição de Genes
Hidroxiprostaglandina Desidrogenases/genética
Hidroxiprostaglandina Desidrogenases/metabolismo
Túbulos Renais Coletores/efeitos dos fármacos
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Osmorregulação/efeitos dos fármacos
Pressão Osmótica/efeitos dos fármacos
Solução Salina Hipertônica/farmacologia
Transdução de Sinais
Canais de Cátion TRPM/genética
Canais de Cátion TRPV/genética
Canais de Cátion TRPV/metabolismo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GABA Plasma Membrane Transport Proteins); 0 (Saline Solution, Hypertonic); 0 (Slc6a12 protein, mouse); 0 (TRPM Cation Channels); 0 (TRPM3 protein, mouse); 0 (TRPV Cation Channels); 0 (Trpv4 protein, mouse); EC 1.1.1.- (Hydroxyprostaglandin Dehydrogenases); EC 1.1.1.188 (prostaglandin-F synthase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170127
[St] Status:MEDLINE
[do] DOI:10.1152/ajprenal.00465.2015


  8 / 1027 MEDLINE  
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[PMID]:28108584
[Au] Autor:Ugbode C; Hu Y; Whalley B; Peers C; Rattray M; Dallas ML
[Ad] Endereço:Department of Biology, University of York, Heslington, York YO10 5DD, U.K.
[Ti] Título:Astrocytic transporters in Alzheimer's disease.
[So] Source:Biochem J;474(3):333-355, 2017 Feb 01.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Astrocytes play a fundamental role in maintaining the health and function of the central nervous system. Increasing evidence indicates that astrocytes undergo both cellular and molecular changes at an early stage in neurological diseases, including Alzheimer's disease (AD). These changes may reflect a change from a neuroprotective to a neurotoxic phenotype. Given the lack of current disease-modifying therapies for AD, astrocytes have become an interesting and viable target for therapeutic intervention. The astrocyte transport system covers a diverse array of proteins involved in metabolic support, neurotransmission and synaptic architecture. Therefore, specific targeting of individual transporter families has the potential to suppress neurodegeneration, a characteristic hallmark of AD. A small number of the 400 transporter superfamilies are expressed in astrocytes, with evidence highlighting a fraction of these are implicated in AD. Here, we review the current evidence for six astrocytic transporter subfamilies involved in AD, as reported in both animal and human studies. This review confirms that astrocytes are indeed a viable target, highlights the complexities of studying astrocytes and provides future directives to exploit the potential of astrocytes in tackling AD.
[Mh] Termos MeSH primário: Doença de Alzheimer/genética
Astrócitos/metabolismo
Proteínas de Membrana Transportadoras/genética
[Mh] Termos MeSH secundário: Transportadores de Cassetes de Ligação de ATP/genética
Transportadores de Cassetes de Ligação de ATP/metabolismo
Doença de Alzheimer/metabolismo
Doença de Alzheimer/patologia
Animais
Astrócitos/patologia
Proteínas da Membrana Plasmática de Transporte de GABA/genética
Proteínas da Membrana Plasmática de Transporte de GABA/metabolismo
Regulação da Expressão Gênica
Proteínas Facilitadoras de Transporte de Glucose/genética
Proteínas Facilitadoras de Transporte de Glucose/metabolismo
Proteínas de Transporte de Glutamato da Membrana Plasmática/genética
Proteínas de Transporte de Glutamato da Membrana Plasmática/metabolismo
Proteínas da Membrana Plasmática de Transporte de Glicina/genética
Proteínas da Membrana Plasmática de Transporte de Glicina/metabolismo
Seres Humanos
Proteínas de Membrana Transportadoras/metabolismo
Família Multigênica
Proteínas da Membrana Plasmática de Transporte de Serotonina/genética
Proteínas da Membrana Plasmática de Transporte de Serotonina/metabolismo
Transdução de Sinais
ATPase Trocadora de Sódio-Potássio/genética
ATPase Trocadora de Sódio-Potássio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (GABA Plasma Membrane Transport Proteins); 0 (Glucose Transport Proteins, Facilitative); 0 (Glutamate Plasma Membrane Transport Proteins); 0 (Glycine Plasma Membrane Transport Proteins); 0 (Membrane Transport Proteins); 0 (Serotonin Plasma Membrane Transport Proteins); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170616
[Lr] Data última revisão:
170616
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170122
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20160505


  9 / 1027 MEDLINE  
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[PMID]:28063512
[Au] Autor:Ostojic SM
[Ad] Endereço:Faculty of Sport and Physical Education, University of Novi Sad, Novi Sad, Serbia; University of Belgrade School of Medicine, Belgrade, Serbia. Electronic address: Sergej.ostojic@chess.edu.rs.
[Ti] Título:Tackling guanidinoacetic acid for advanced cellular bioenergetics.
[So] Source:Nutrition;34:55-57, 2017 Feb.
[Is] ISSN:1873-1244
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tissues with high-energy output, such as the brain and skeletal muscle, suffer the most from impaired or depleted energy levels, with innovative nutritional approaches needed to effectively tackle metabolic deficits in bioenergetics. Here, we highlight the role of guanidinoacetic acid in the control and provision of cellular energy by its interaction with cellular transporters for taurine (SLC6 A6) and γ-aminobutyric acid (SLC6 A13), previously dismissed as "untargetable" carriers by other bioenergetics therapeutics.
[Mh] Termos MeSH primário: Metabolismo Energético/efeitos dos fármacos
Glicina/análogos & derivados
[Mh] Termos MeSH secundário: Creatina/metabolismo
Proteínas da Membrana Plasmática de Transporte de GABA/genética
Proteínas da Membrana Plasmática de Transporte de GABA/metabolismo
Glicina/farmacologia
Seres Humanos
Glicoproteínas de Membrana/genética
Glicoproteínas de Membrana/metabolismo
Proteínas de Membrana Transportadoras/genética
Proteínas de Membrana Transportadoras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (GABA Plasma Membrane Transport Proteins); 0 (Membrane Glycoproteins); 0 (Membrane Transport Proteins); 0 (SLC6A13 protein, human); 148686-53-7 (taurine transporter); GO52O1A04E (glycocyamine); MU72812GK0 (Creatine); TE7660XO1C (Glycine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170109
[St] Status:MEDLINE


  10 / 1027 MEDLINE  
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[PMID]:27940054
[Au] Autor:Kunisawa K; Kido K; Nakashima N; Matsukura T; Nabeshima T; Hiramatsu M
[Ad] Endereço:Department of Chemical Pharmacology, Faculty of Pharmacy, Meijo University, Nagoya, Japan.
[Ti] Título:Betaine attenuates memory impairment after water-immersion restraint stress and is regulated by the GABAergic neuronal system in the hippocampus.
[So] Source:Eur J Pharmacol;796:122-130, 2017 Feb 05.
[Is] ISSN:1879-0712
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:GABA mediated neuronal system regulates hippocampus-dependent memory and stress responses by controlling plasticity and neuronal excitability. Here, we demonstrate that betaine ameliorates water-immersion restraint stress (WIRS)-induced memory impairments. This improvement was inhibited by a betaine/GABA transporter-1 (GABA transporter-2: GAT2) inhibitor, NNC 05-2090. In this study, we investigated whether memory amelioration by betaine was mediated by the GABAergic neuronal system. Adult male mice were co-administered betaine and GABA receptor antagonists after WIRS. We also examined whether memory impairment after WIRS was attenuated by GABA receptor agonists. The memory functions were evaluated using a novel object recognition test 3-6 days after WIRS and/or the step-down type passive avoidance test at 7-8 days. The co-administration of the GABA receptor antagonist bicuculline (1mg/kg) or the GABA receptor antagonist phaclofen (10mg/kg) 1h after WIRS suppressed the memory-improving effects induced by betaine. Additionally, the administration of the GABA receptor agonist muscimol (1mg/kg) or the GABA receptor agonist baclofen (10mg/kg) 1h after WIRS attenuated memory impairments. These results were similar to the data observed with betaine. The treatment with betaine after WIRS significantly decreased the expression of GABA transaminase, and this effect was partially blocked by NNC 05-2090 in the hippocampus. WIRS caused a transient increase in hippocampal GABA levels and the changes after WIRS were not affected by betaine treatment in an in vivo microdialysis study. These results suggest that the beneficial effects of betaine may be mediated in part by changing the GABAergic neuronal system.
[Mh] Termos MeSH primário: Betaína/farmacologia
Hipocampo/efeitos dos fármacos
Memória/efeitos dos fármacos
Neurônios/efeitos dos fármacos
Estresse Psicológico/patologia
Estresse Psicológico/fisiopatologia
Ácido gama-Aminobutírico/metabolismo
[Mh] Termos MeSH secundário: Animais
Espaço Extracelular/efeitos dos fármacos
Espaço Extracelular/metabolismo
Agonistas GABAérgicos/farmacologia
Antagonistas GABAérgicos/farmacologia
Proteínas da Membrana Plasmática de Transporte de GABA/metabolismo
Hipocampo/patologia
Hipocampo/fisiopatologia
Imersão
Masculino
Camundongos
Neurônios/patologia
Receptores de GABA/metabolismo
Estresse Psicológico/metabolismo
Água
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GABA Agonists); 0 (GABA Antagonists); 0 (GABA Plasma Membrane Transport Proteins); 0 (Receptors, GABA); 0 (Slc6a12 protein, mouse); 059QF0KO0R (Water); 3SCV180C9W (Betaine); 56-12-2 (gamma-Aminobutyric Acid)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170428
[Lr] Data última revisão:
170428
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE



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