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[PMID]:28441750
[Au] Autor:Stockwell J; Jakova E; Cayabyab FS
[Ad] Endereço:Department of Surgery, University of Saskatchewan, Saskatoon, SK S7N 5E5, Canada. jocelyn.stockwell@usask.ca.
[Ti] Título:Adenosine A1 and A2A Receptors in the Brain: Current Research and Their Role in Neurodegeneration.
[So] Source:Molecules;22(4), 2017 Apr 23.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The inhibitory adenosine A1 receptor (A1R) and excitatory A2A receptor (A2AR) are predominantly expressed in the brain. Whereas the A2AR has been implicated in normal aging and enhancing neurotoxicity in multiple neurodegenerative diseases, the inhibitory A1R has traditionally been ascribed to have a neuroprotective function in various brain insults. This review provides a summary of the emerging role of prolonged A1R signaling and its potential cross-talk with A2AR in the cellular basis for increased neurotoxicity in neurodegenerative disorders. This A1R signaling enhances A2AR-mediated neurodegeneration, and provides a platform for future development of neuroprotective agents in stroke, Parkinson's disease and epilepsy.
[Mh] Termos MeSH primário: Encéfalo/metabolismo
Doenças Neurodegenerativas/metabolismo
Receptor A1 de Adenosina/fisiologia
Receptor A2A de Adenosina/fisiologia
[Mh] Termos MeSH secundário: Animais
Encéfalo/patologia
Seres Humanos
Doenças Neurodegenerativas/tratamento farmacológico
Fármacos Neuroprotetores/farmacologia
Agonistas Purinérgicos/farmacologia
Antagonistas Purinérgicos/farmacologia
Receptor Cross-Talk
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Neuroprotective Agents); 0 (Purinergic Agonists); 0 (Purinergic Antagonists); 0 (Receptor, Adenosine A1); 0 (Receptor, Adenosine A2A)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170427
[St] Status:MEDLINE


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[PMID]:28179298
[Au] Autor:Lertsuwan K; Peters W; Johnson L; Lertsuwan J; Marwa I; Sikes RA
[Ad] Endereço:Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok, Thailand.
[Ti] Título:Purinergic Receptor Expression and Cellular Responses to Purinergic Agonists in Human Prostate Cancer Cells.
[So] Source:Anticancer Res;37(2):529-537, 2017 02.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Anticancer activity of extracellular nucleotides has been investigated in many types of cancer. Herein, the effects of extracellular nucleotides and the receptor profile for these nucleotides on prostate cancer (PCa) were elaborated. MATERIALS AND METHODS: PCa cell lines representing different stages of PCa were used. The effects of ATP and adenosine on PCa growth and migration on different extracellular matrix proteins were examined by MTT and wound-healing assays. Purinergic receptor profiling was carried out by reverse transcription-polymerase chain reaction (RT-PCR). RESULTS: A growth-inhibitory effect of ATP and adenosine was observed on all PCa cell lines tested. Several ATP-recognized P2 receptors and adenosine receptors were commonly expressed in PCa cell lines. Neither ATP nor adenosine had any significant effect on PCa migration. CONCLUSION: ATP and adenosine had an antiproliferative effect on PCa cells without affecting their motility, indicating their potential as a novel therapy for PCa.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/farmacologia
Adenosina/farmacologia
Neoplasias da Próstata/tratamento farmacológico
Neoplasias da Próstata/metabolismo
Agonistas Purinérgicos/farmacologia
Receptores Purinérgicos/biossíntese
[Mh] Termos MeSH secundário: Processos de Crescimento Celular/efeitos dos fármacos
Linhagem Celular Tumoral
Movimento Celular/efeitos dos fármacos
Relação Dose-Resposta a Droga
Seres Humanos
Masculino
Neoplasias da Próstata/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Purinergic Agonists); 0 (Receptors, Purinergic); 8L70Q75FXE (Adenosine Triphosphate); K72T3FS567 (Adenosine)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170213
[Lr] Data última revisão:
170213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170210
[St] Status:MEDLINE


  3 / 217 MEDLINE  
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[PMID]:27867013
[Au] Autor:Abdelrahman A; Namasivayam V; Hinz S; Schiedel AC; Köse M; Burton M; El-Tayeb A; Gillard M; Bajorath J; de Ryck M; Müller CE
[Ad] Endereço:PharmaCenter Bonn, Pharmaceutical Institute, Pharmaceutical Chemistry I, University of Bonn, An der Immenburg 4, D-53121 Bonn, Germany.
[Ti] Título:Characterization of P2X4 receptor agonists and antagonists by calcium influx and radioligand binding studies.
[So] Source:Biochem Pharmacol;125:41-54, 2017 Feb 01.
[Is] ISSN:1873-2968
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Antagonists for ATP-activated P2X4 ion channel receptors are currently in the focus as novel drug targets, in particular for the treatment of neuropathic and inflammatory pain. We stably expressed the human, rat and mouse P2X4 receptors in 1321N1 astrocytoma cells, which is devoid of functional nucleotide receptors, by retroviral transfection, and established monoclonal cell lines. Calcium flux assay conditions were optimized for high-throughput screening resulting in a Z'-factor of >0.8. The application of ready-to-use frozen cells did not negatively affect the results of the calcium assays, which is of great advantage for the screening of compound libraries. Species differences were observed, the rat P2X4 receptor being particularly insensitive to many ATP derivatives. Membrane preparations of the cell lines showed high levels of specific [ S]ATPγS binding with low nonspecific binding (<5% of total binding), while non-transfected cells were devoid of specific binding sites for the radioligand. Conditions were employed which allow binding studies to be performed at room temperature. While a variety of nucleotide-derived agonists and the antagonist TNP-ATP displaced [ S]ATPγS from its binding site at human P2X4 receptors, the non-nucleotidic antagonists paroxetine and 5-BDBD did not compete with radioligand binding and were therefore characterized as allosteric antagonists. Homology modeling was applied to find an explanation for the observed species differences.
[Mh] Termos MeSH primário: Cálcio/metabolismo
Agonistas Purinérgicos/farmacologia
Antagonistas Purinérgicos/farmacologia
Receptores Purinérgicos P2X4/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Seres Humanos
Transporte de Íons
Camundongos
Ensaio Radioligante
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Purinergic Agonists); 0 (Purinergic Antagonists); 0 (Receptors, Purinergic P2X4); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161122
[St] Status:MEDLINE


  4 / 217 MEDLINE  
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[PMID]:27626375
[Au] Autor:Mansoor SE; Lü W; Oosterheert W; Shekhar M; Tajkhorshid E; Gouaux E
[Ad] Endereço:Vollum Institute, Oregon Health &Science University, Portland, Oregon 97239, USA.
[Ti] Título:X-ray structures define human P2X(3) receptor gating cycle and antagonist action.
[So] Source:Nature;538(7623):66-71, 2016 10 06.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems. Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors. The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear. Here we report X-ray crystal structures of the human P2X receptor in apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states. The open state structure harbours an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress. The competitive antagonists TNP-ATP and A-317491 stabilize the apo/resting state and reveal the interactions responsible for competitive inhibition. These structures illuminate the conformational rearrangements that underlie P2X receptor gating and provide a foundation for the development of new pharmacological agents.
[Mh] Termos MeSH primário: Ativação do Canal Iônico/efeitos dos fármacos
Antagonistas do Receptor Purinérgico P2X/farmacologia
Receptores Purinérgicos P2X3/química
Receptores Purinérgicos P2X3/metabolismo
[Mh] Termos MeSH secundário: Apoproteínas/agonistas
Apoproteínas/antagonistas & inibidores
Apoproteínas/química
Apoproteínas/metabolismo
Sítios de Ligação/efeitos dos fármacos
Ligação Competitiva/efeitos dos fármacos
Cristalização
Cristalografia por Raios X
Seres Humanos
Transporte de Íons
Ligantes
Modelos Moleculares
Porosidade
Conformação Proteica
Agonistas Purinérgicos/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Apoproteins); 0 (Ligands); 0 (Purinergic Agonists); 0 (Purinergic P2X Receptor Antagonists); 0 (Receptors, Purinergic P2X3)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160915
[St] Status:MEDLINE
[do] DOI:10.1038/nature19367


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[PMID]:27620165
[Au] Autor:Benz PM; Laban H; Zink J; Günther L; Walter U; Gambaryan S; Dib K
[Ad] Endereço:Institute for Vascular Signalling, Centre for Molecular Medicine, Johann Wolfgang Goethe University and DZHK (German Centre for Cardiovascular Research) partner site Rhine-Main, 60590, Frankfurt, Germany.
[Ti] Título:Vasodilator-Stimulated Phosphoprotein (VASP)-dependent and -independent pathways regulate thrombin-induced activation of Rap1b in platelets.
[So] Source:Cell Commun Signal;14(1):21, 2016 09 13.
[Is] ISSN:1478-811X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Vasodilator-Stimulated Phosphoprotein (VASP) is involved in the inhibition of agonist-induced platelet aggregation by cyclic nucleotides and the adhesion of platelets to the vascular wall. αIIbß3 is the main integrin responsible for platelet activation and Rap1b plays a key role in integrin signalling. We investigated whether VASP is involved in the regulation of Rap1b in platelets since VASP-null platelets exhibit augmented adhesion to endothelial cells in vivo. METHODS: Washed platelets from wild type and VASP-deficient mice were stimulated with thrombin, the purinergic receptors agonist ADP, or the thromboxane A2 receptor agonist U46619 and Rap1b activation was measured using the GST-RalGDS-RBD binding assay. Interaction of VASP and Crkl was investigated by co-immunoprecipitation, confocal microscopy, and pull-down assays using Crkl domains expressed as GST-fusion proteins. RESULTS: Surprisingly, we found that activation of Rap1b in response to thrombin, ADP, or U46619 was significantly reduced in platelets from VASP-null mice compared to platelets from wild type mice. However, inhibition of thrombin-induced activation of Rap1b by nitric oxide (NO) was similar in platelets from wild type and VASP-null mice indicating that the NO/cGMP/PKG pathway controls inhibition of Rap1b independently from VASP. To understand how VASP regulated Rap1b, we investigated association between VASP and the Crk-like protein (Crkl), an adapter protein which activates the Rap1b guanine nucleotide exchange factor C3G. We demonstrated the formation of a Crkl/VASP complex by showing that: 1) Crkl co-immunoprecipitated VASP from platelet lysates; 2) Crkl and VASP dynamically co-localized at actin-rich protrusions reminiscent of focal adhesions, filopodia, and lamellipodia upon platelet spreading on fibronectin; 3) recombinant VASP bound directly to the N-terminal SH3 domain of Crkl; 4) Protein Kinase A (PKA) -mediated VASP phosphorylation on Ser157 abrogated the binding of Crkl. CONCLUSIONS: We identified Crkl as a novel protein interacting with VASP in platelets. We propose that the C3G/Crkl/VASP complex plays a role in the regulation of Rap1b and this explains, at least in part, the reduced agonist-induced activation of Rap1b in VASP-null platelets. In addition, the fact that PKA-dependent VASP phosphorylation abrogated its interaction with Crkl may provide, at least in part, a rationale for the PKA-dependent inhibition of Rap1b and platelet aggregation.
[Mh] Termos MeSH primário: Plaquetas/metabolismo
Moléculas de Adesão Celular/metabolismo
Proteínas dos Microfilamentos/metabolismo
Fosfoproteínas/metabolismo
Proteínas rap de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Animais
Plaquetas/efeitos dos fármacos
Moléculas de Adesão Celular/genética
Células Cultivadas
Fator 2 de Liberação do Nucleotídeo Guanina/metabolismo
Seres Humanos
Camundongos
Proteínas dos Microfilamentos/genética
Fosfoproteínas/genética
Ligação Proteica
Proteínas Proto-Oncogênicas c-crk/metabolismo
Agonistas Purinérgicos/farmacologia
Trombina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cell Adhesion Molecules); 0 (Guanine Nucleotide-Releasing Factor 2); 0 (Microfilament Proteins); 0 (Phosphoproteins); 0 (Proto-Oncogene Proteins c-crk); 0 (Purinergic Agonists); 0 (vasodilator-stimulated phosphoprotein); EC 3.4.21.5 (Thrombin); EC 3.6.1.- (Rap1b protein, mouse); EC 3.6.5.2 (rap GTP-Binding Proteins)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160914
[St] Status:MEDLINE
[do] DOI:10.1186/s12964-016-0144-z


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[PMID]:27384918
[Au] Autor:Ribeiro-Filho AC; Buri MV; Barros CC; Dreyfuss JL; Nader HB; Justo GZ; Craveiro RB; Pesquero JB; Miranda A; Ferreira AT; Paredes-Gamero EJ
[Ad] Endereço:Centro Interdisciplinar de Investigação Bioquímica, Universidade de Mogi das Cruzes, Av. Dr Cândido Xavier de Almeida Souza, 200, Mogi das Cruzes, São Paulo, Brazil.
[Ti] Título:Functional and molecular evidence for heteromeric association of P2Y1 receptor with P2Y2 and P2Y4 receptors in mouse granulocytes.
[So] Source:BMC Pharmacol Toxicol;17(1):29, 2016 Jul 07.
[Is] ISSN:2050-6511
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: All hematopoietic cells express P2 receptors, however pharmacological characteristics such as expression and affinity in granulocytes are unknown. METHODS: Pharmacological characteristics of P2 receptors were evaluated by Ca(2+) measurements using Fura-2 fluorophore. P2 receptors expression were analyzed by flow cytometry and RT-PCR. P2 interaction were shown by coimmunoprecipitation, western blotting and FRET. RESULTS: Granulocytes were responsive to P2Y agonists, whereas P2X agonists were ineffective. Ca(2+) increase, elicited by ADP and UTP was dependent on intracellular stocks and sensitive to G-coupled receptor inhibition. Moreover, MRS2179, a specific antagonist of the P2Y1 receptor, abolished ADP response. Interestingly, ADP and UTP exhibited full heterologous desensitization, suggesting that these agonists interact with the same receptor. The heteromeric association between P2Y1 receptor and the P2Y2 and P2Y4 receptors was shown by immunoprecipitation and FRET analysis. CONCLUSION: Clear evidence of heteromeric association of P2Y receptors was found during the evaluation of P2 receptors present in mice granulocytes, which could impact in the classical pharmacology of P2Y receptors in granulocytes.
[Mh] Termos MeSH primário: Granulócitos/fisiologia
Receptores Purinérgicos P2Y1/fisiologia
Receptores Purinérgicos P2Y2/fisiologia
Receptores Purinérgicos P2/fisiologia
[Mh] Termos MeSH secundário: Animais
Feminino
Citometria de Fluxo
Granulócitos/efeitos dos fármacos
Camundongos
Camundongos Endogâmicos C57BL
Ligação Proteica/fisiologia
Agonistas Purinérgicos/farmacologia
Receptores Purinérgicos P2/química
Receptores Purinérgicos P2Y1/química
Receptores Purinérgicos P2Y2/química
Células-Tronco/efeitos dos fármacos
Células-Tronco/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Purinergic Agonists); 0 (Receptors, Purinergic P2); 0 (Receptors, Purinergic P2Y1); 0 (Receptors, Purinergic P2Y2); 0 (purinoceptor P2Y4)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160708
[St] Status:MEDLINE
[do] DOI:10.1186/s40360-016-0072-y


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[PMID]:27318925
[Au] Autor:Fukuda T; Kuroda T; Kono M; Hyoguchi M; Tajiri S; Tanaka M; Mine Y; Matsui T
[Ad] Endereço:Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School of Kyushu University, 6-10-1 Hakozaki, Fukuoka, Higashi-ku, 812-8581, Japan.
[Ti] Título:Adenine attenuates the Ca(2+) contraction-signaling pathway via adenine receptor-mediated signaling in rat vascular smooth muscle cells.
[So] Source:Naunyn Schmiedebergs Arch Pharmacol;389(9):999-1007, 2016 Sep.
[Is] ISSN:1432-1912
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Our previous study demonstrated that adenine (6-amino-6H-purine) relaxed contracted rat aorta rings in an endothelial-independent manner. Although adenine receptors (AdeRs) are expressed in diverse tissues, aortic AdeR expression has not been ascertained. Thus, the aims of this study were to clarify the expression of AdeR in rat vascular smooth muscle cells (VSMCs) and to investigate the adenine-induced vasorelaxation mechanism(s). VSMCs were isolated from 8-week-old male Wistar-Kyoto rats and used in this study. Phosphorylation of myosin light chain (p-MLC) was measured by western blot. AdeR mRNA was detected by RT-PCR. Intracellular Ca(2+) concentration ([Ca(2+)]i) was measured by using Fura-2/AM. Vasorelaxant adenine (10-100 µM) significantly reduced p-MLC by angiotensin II (Ang II, 10 µM) in VSMCs (P < 0.05). We confirmed the expression of aortic AdeR mRNA and the activation of PKA in VSMCs through stimulation of AdeR by adenine by ELISA. Intracellular Ca(2+) concentration ([Ca(2+)]i) measurement demonstrated that adenine inhibits Ang II- and m-3M3FBS (PLC agonist)-induced [Ca(2+)]i elevation. In AdeR-knockdown VSMCs, PKA activation and p-MLC reduction by adenine were completely abolished. These results firstly demonstrated that vasorelaxant adenine can suppress Ca(2+) contraction signaling pathways via aortic AdeR/PKA activation in VSMCs.
[Mh] Termos MeSH primário: Adenina/farmacologia
Acoplamento Excitação-Contração/efeitos dos fármacos
Músculo Liso Vascular/efeitos dos fármacos
Miócitos de Músculo Liso/efeitos dos fármacos
Agonistas Purinérgicos/farmacologia
Receptores Purinérgicos/efeitos dos fármacos
Vasodilatação/efeitos dos fármacos
Vasodilatadores/farmacologia
[Mh] Termos MeSH secundário: Angiotensina II/farmacologia
Animais
Aorta/efeitos dos fármacos
Aorta/metabolismo
Células Cultivadas
Proteínas Quinases Dependentes de AMP Cíclico/metabolismo
Relação Dose-Resposta a Droga
Ativação Enzimática
Masculino
Músculo Liso Vascular/metabolismo
Miócitos de Músculo Liso/metabolismo
Cadeias Leves de Miosina/metabolismo
Fosforilação
Interferência de RNA
Ratos Endogâmicos WKY
Receptores Purinérgicos/genética
Receptores Purinérgicos/metabolismo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Myosin Light Chains); 0 (Purinergic Agonists); 0 (Receptors, Purinergic); 0 (Vasodilator Agents); 0 (adenine receptor, rat); 11128-99-7 (Angiotensin II); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases); JAC85A2161 (Adenine)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160620
[St] Status:MEDLINE
[do] DOI:10.1007/s00210-016-1264-0


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[PMID]:25502294
[Au] Autor:Gubert C; Fries GR; Pfaffenseller B; Ferrari P; Coutinho-Silva R; Morrone FB; Kapczinski F; Battastini AMO
[Ad] Endereço:Programa de Pós-Graduação Ciências Biológicas: Bioquímica, Departamento de Bioquímica, Instituto de Ciências Básicas da Saúde, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, 90035-003, Brazil.
[Ti] Título:Role of P2X7 Receptor in an Animal Model of Mania Induced by D-Amphetamine.
[So] Source:Mol Neurobiol;53(1):611-620, 2016 Jan.
[Is] ISSN:1559-1182
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The objective of this study was to explore the association between the P2X7 purinergic receptor (P2X7R) and neuroinflammation using a preclinical model of acute bipolar mania. We analyzed the modulatory effects of P2X7R agonist (3'-O-(4-benzoyl)benzoyl-adenosine 5'-triphosphate, BzATP) and antagonists (brilliant blue, BBG and 3-[[5-(2,3 dichlorophenyl)-1H-tetrazol-1-yl]methyl]pyridine hydrochloride, A438079) on assessments related to behavior (locomotor activity), neuroinflammation (interleukin-1 beta, IL-1ß; tumor necrosis factor alpha, TNF-α; and interleukin- 6, IL-6), oxidative stress (thiobarbituric acid reactive substances, TBARS) and neuroplasticity (brain-derived neurotrophic factor, BDNF) markers in a pharmacological model of mania induced by acute and chronic treatment with D-amphetamine (AMPH) (2 mg/kg) in mice. An apparent lack of responsiveness to AMPH was observed in terms of the locomotor activity in animals with blocked P2X7R or with genetic deletion of P2X7R in knockout (P2X7R(-/-)) mice. Likewise, P2X7R participated in the AMPH-induced increase of the proinflammatory and excitotoxic environment, as demonstrated by the reversal of IL-1ß, TNF-α, and TBARS levels caused by P2X7R blocking. Our results support the hypothesis that P2X7R plays a role in the neuroinflammation induced by AMPH in a preclinical model of mania, which could explain the altered behavior. The present data suggest that P2X7R may be a therapeutic target related to the neuroinflammation reported in bipolar disorder.
[Mh] Termos MeSH primário: Transtorno Bipolar/induzido quimicamente
Transtorno Bipolar/metabolismo
Dextroanfetamina/toxicidade
Modelos Animais de Doenças
Receptores Purinérgicos P2X7/fisiologia
[Mh] Termos MeSH secundário: Animais
Encéfalo/efeitos dos fármacos
Encéfalo/metabolismo
Mediadores da Inflamação/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Endogâmicos CBA
Camundongos Knockout
Agonistas Purinérgicos/farmacologia
Antagonistas Purinérgicos/farmacologia
Substâncias Reativas com Ácido Tiobarbitúrico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Inflammation Mediators); 0 (Purinergic Agonists); 0 (Purinergic Antagonists); 0 (Receptors, Purinergic P2X7); 0 (Thiobarbituric Acid Reactive Substances); TZ47U051FI (Dextroamphetamine)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141216
[St] Status:MEDLINE
[do] DOI:10.1007/s12035-014-9031-z


  9 / 217 MEDLINE  
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[PMID]:26559728
[Au] Autor:Yao D; Yoshida M; Sessle BJ
[Ad] Endereço:aJiangxi Mental Hospital and School of Pharmaceutical Science, Nanchang University, Nanchang, Jiangxi, People's Republic of China bFaculty of Dentistry, University of Toronto, Toronto, Ontario, Canada cSection of Dental Anesthesiology, Department of Oral and Maxillofacial Surgery and Oral Medicine, Hiroshima University Hospital, Hiroshima, Japan.
[Ti] Título:Dura-evoked neck muscle activity involves purinergic and N-methyl-D-aspartate receptor mechanisms.
[So] Source:Neuroreport;26(18):1155-60, 2015 Dec 16.
[Is] ISSN:1473-558X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We have previously demonstrated that noxious stimulation of craniofacial tissues including the frontal dura reflexly evokes significant increases in neck muscle electromyographic (EMG) activity. The primary aim of this study was to determine whether purinergic receptor mechanisms may be involved in these EMG effects, and whether N-methyl-D-aspartate (NMDA) receptor processes modulate the purinergic mechanisms. Application of the P2X1, P2X3 and P2X2/3 receptor agonist α,ß-methylene ATP (but not vehicle) to the dural surface evoked a significant (P<0.05) increase in ipsilateral neck EMG activity that could be suppressed by dural or intrathecal application of the selective P2X1, P2X3 and P2X2/3 receptor antagonist 2',3'-O-(2,4,6-trinitrophenyl) ATP (TNP-ATP) but not by vehicle; the intrathecal application of 2-amino-5-phosphonopentanoic acid, an NMDA receptor antagonist, also significantly reduced the neck EMG activity evoked by dural application of α,ß-methylene ATP. These data suggest that purinergic receptor mechanisms contribute to the increased neck activity that can be reflexly evoked by noxious stimulation of the frontal dura, and that NMDA as well as purinergic receptor mechanisms in the medulla may modulate these purinergic-related effects.
[Mh] Termos MeSH primário: Dura-Máter/fisiologia
Músculos do Pescoço/fisiologia
Receptores de N-Metil-D-Aspartato/fisiologia
Receptores Purinérgicos/fisiologia
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/análogos & derivados
Trifosfato de Adenosina/farmacologia
Animais
Dura-Máter/efeitos dos fármacos
Eletromiografia
Masculino
Bulbo/efeitos dos fármacos
Agonistas Purinérgicos/farmacologia
Antagonistas Purinérgicos/farmacologia
Ratos Sprague-Dawley
Receptores de N-Metil-D-Aspartato/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Purinergic Agonists); 0 (Purinergic Antagonists); 0 (Receptors, N-Methyl-D-Aspartate); 0 (Receptors, Purinergic); 61368-63-6 (2',3'-O-(2,4,6-trinitro-cyclohexadienylidine)adenosine 5'-triphosphate); 8L70Q75FXE (Adenosine Triphosphate); NYX13NT29D (alpha,beta-methyleneadenosine 5'-triphosphate)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:161216
[Lr] Data última revisão:
161216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151113
[St] Status:MEDLINE
[do] DOI:10.1097/WNR.0000000000000489


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[PMID]:26072377
[Au] Autor:Yu Y
[Ad] Endereço:Department of Biological and Chemical Sciences, Illinois Institute of Technology, Chicago, IL 60616, USA. Electronic address: yyu17@iit.edu.
[Ti] Título:Nucleotide modulates odor response through activation of purinergic receptor in olfactory sensory neuron.
[So] Source:Biochem Biophys Res Commun;463(4):1006-11, 2015 Aug 07.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Extracellular nucleotides are important neurotransmitters, neuromodulators and paracrine factors in the neural sensory system [16]. Most of purines and pyrimidines act on the associated purinergic cell-surface receptors to mediate sensory transduction and modulation. Previously, we reported a subgroup of heptaldehyde (H)/2-hepatanone (Ho)-responsive olfactory sensory neurons (H/Ho-OSNs) in the ventral endoturbinates [31]. Through the calcium image recording, we characterized that ATP elicited [Ca(2+)]i increase in the presence of extracellular calcium, while depletion of intracellular calcium stores blocked UTP-evoked [Ca(2+)]i increase. Pharmacological studies indicated that P2X3 was expressed in the H/Ho-OSNs, modulating both heptaldehyde (H) and 2-hepatanone (Ho)-induced responses. These data indicated that activation of purinergic receptor negatively modulated odor response, providing the evidence to support the possible protective effect of purinergic receptor in OSNs.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/fisiologia
Odorantes
Receptores Purinérgicos/fisiologia
Células Receptoras Sensoriais/fisiologia
Uridina Trifosfato/fisiologia
[Mh] Termos MeSH secundário: Animais
Cálcio/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Agonistas Purinérgicos/farmacologia
Células Receptoras Sensoriais/efeitos dos fármacos
Células Receptoras Sensoriais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Purinergic Agonists); 0 (Receptors, Purinergic); 8L70Q75FXE (Adenosine Triphosphate); SY7Q814VUP (Calcium); UT0S826Z60 (Uridine Triphosphate)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150615
[St] Status:MEDLINE



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