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Pesquisa : D02.092.782.258.368.257 [Categoria DeCS]
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[PMID]:29217191
[Au] Autor:Yoshida K; Nakai A; Kaneshiro K; Hashimoto N; Suzuki K; Uchida K; Hashimoto T; Kawasaki Y; Tateishi K; Nakagawa N; Shibanuma N; Sakai Y; Hashiramoto A
[Ad] Endereço:Department of Biophysics, Kobe University Graduate School of Health Sciences, Kobe 654-0142, Japan.
[Ti] Título:TNF-α induces expression of the circadian clock gene Bmal1 via dual calcium-dependent pathways in rheumatoid synovial cells.
[So] Source:Biochem Biophys Res Commun;495(2):1675-1680, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tumor necrosis factor (TNF)-α is responsible for expressions of several clock genes and affects joint symptoms of rheumatoid arthritis (RA) with diurnal fluctuation. We tried to determine the mechanism involved in over-expression of Bmal1, induced by TNF-α, in primary cultured rheumatoid synovial cells. Cells were incubated with intra-cellular Ca chelator BAPTA-AM, calcineurin inhibitor FK506 and p300/CBP (CREB binding protein) inhibitor C646, respectively, or transfected with p300 and CBP small interfering RNA (siRNA) before stimulation with TNF-α. Oscillation phase and amplitude of Bmal1, transcriptional activator Rorα, transcriptional repressor Rev-erbα, and histone acetyltransferases (p300 and Cbp) were evaluated by quantitative real-time PCR. As results, TNF-α did not influence the oscillation phase of Rev-erbα, while enhanced those of Rorα, resulting in over-expression of Bmal1. When Ca influx was inhibited by BAPTA-AM, TNF-α-mediated up-regulation of Rorα was cancelled, however, that of Bmal1 was still apparent. When we further explored another pathway between TNF-α and Bmal1, TNF-α suppressed the expression of Rev-erbα in the absence of Ca influx, as well as those of p300 and Cbp genes. Finally, actions of TNF-α, in increasing Bmal1/Rorα and decreasing Rev-erbα, were cancelled by C646 treatment or silencing of both p300 and Cbp. In conclusion, we determined a novel role of TNF-α in inducing Bmal1 via dual calcium dependent pathways; Rorα was up-regulated in the presence of Ca influx and Rev-erbα was down-regulated in the absence of that. Results proposed that inhibition of p300/CBP could be new therapeutic targets for RA.
[Mh] Termos MeSH primário: Fatores de Transcrição ARNTL/genética
Artrite Reumatoide/genética
Artrite Reumatoide/metabolismo
Sinalização do Cálcio
Relógios Circadianos/genética
Membrana Sinovial/metabolismo
Fator de Necrose Tumoral alfa/metabolismo
[Mh] Termos MeSH secundário: Artrite Reumatoide/patologia
Benzoatos/farmacologia
Proteína de Ligação a CREB/antagonistas & inibidores
Proteína de Ligação a CREB/genética
Quelantes de Cálcio/farmacologia
Sinalização do Cálcio/efeitos dos fármacos
Células Cultivadas
Proteína p300 Associada a E1A/antagonistas & inibidores
Proteína p300 Associada a E1A/genética
Ácido Egtázico/análogos & derivados
Ácido Egtázico/farmacologia
Expressão Gênica/efeitos dos fármacos
Seres Humanos
Membro 1 do Grupo D da Subfamília 1 de Receptores Nucleares/genética
Membro 1 do Grupo F da Subfamília 1 de Receptores Nucleares/genética
Pirazóis/farmacologia
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
RNA Interferente Pequeno/genética
Membrana Sinovial/efeitos dos fármacos
Membrana Sinovial/patologia
Fator de Necrose Tumoral alfa/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ARNTL Transcription Factors); 0 (ARNTL protein, human); 0 (Benzoates); 0 (C646 compound); 0 (Calcium Chelating Agents); 0 (NR1D1 protein, human); 0 (Nuclear Receptor Subfamily 1, Group D, Member 1); 0 (Nuclear Receptor Subfamily 1, Group F, Member 1); 0 (Pyrazoles); 0 (RNA, Messenger); 0 (RNA, Small Interfering); 0 (RORA protein, human); 0 (Tumor Necrosis Factor-alpha); 139890-68-9 (1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester); 526U7A2651 (Egtazic Acid); EC 2.3.1.48 (CREB-Binding Protein); EC 2.3.1.48 (CREBBP protein, human); EC 2.3.1.48 (E1A-Associated p300 Protein); EC 2.3.1.48 (EP300 protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE


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[PMID]:29348419
[Au] Autor:Wentzel C; Delvendahl I; Sydlik S; Georgiev O; Müller M
[Ad] Endereço:Institute of Molecular Life Sciences, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.
[Ti] Título:Dysbindin links presynaptic proteasome function to homeostatic recruitment of low release probability vesicles.
[So] Source:Nat Commun;9(1):267, 2018 01 18.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Here we explore the relationship between presynaptic homeostatic plasticity and proteasome function at the Drosophila neuromuscular junction. First, we demonstrate that the induction of homeostatic plasticity is blocked after presynaptic proteasome perturbation. Proteasome inhibition potentiates release under baseline conditions but not during homeostatic plasticity, suggesting that proteasomal degradation and homeostatic plasticity modulate a common pool of vesicles. The vesicles that are regulated by proteasome function and recruited during homeostatic plasticity are highly EGTA sensitive, implying looser Ca influx-release coupling. Similar to homeostatic plasticity, proteasome perturbation enhances presynaptic Ca influx, readily-releasable vesicle pool size, and does not potentiate release after loss of specific homeostatic plasticity genes, including the schizophrenia-susceptibility gene dysbindin. Finally, we provide genetic evidence that Dysbindin levels regulate the access to EGTA-sensitive vesicles. Together, our data suggest that presynaptic protein degradation opposes the release of low-release probability vesicles that are potentiated during homeostatic plasticity and whose access is controlled by dysbindin.
[Mh] Termos MeSH primário: Disbindina/metabolismo
Junção Neuromuscular/metabolismo
Plasticidade Neuronal
Complexo de Endopeptidases do Proteassoma/metabolismo
Vesículas Sinápticas/fisiologia
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Cálcio/metabolismo
Drosophila
Proteínas de Drosophila/metabolismo
Ácido Egtázico
Homeostase
Proteínas rab3 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Dysbindin); 0 (RIM protein, Drosophila); 526U7A2651 (Egtazic Acid); EC 3.4.25.1 (Proteasome Endopeptidase Complex); EC 3.6.5.2 (rab3 GTP-Binding Proteins); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02494-0


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[PMID]:28458351
[Au] Autor:Yamaguchi M; Saito SY; Nishiyama R; Nakamura M; Todoroki K; Toyo'oka T; Ishikawa T
[Ad] Endereço:Department of Pharmacology, School of Pharmaceutical Sciences, University of Shizuoka.
[Ti] Título:Caffeine Suppresses the Activation of Hepatic Stellate Cells cAMP-Independently by Antagonizing Adenosine Receptors.
[So] Source:Biol Pharm Bull;40(5):658-664, 2017.
[Is] ISSN:1347-5215
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:During liver injury, hepatic stellate cells (HSCs) are activated by various cytokines and transdifferentiated into myofibroblast-like activated HSCs, which produce collagen, a major source of liver fibrosis. Therefore, the suppression of HSC activation is regarded as a therapeutic target for liver fibrosis. Several epidemiological reports have revealed that caffeine intake decreases the risk of liver disease. In this study, therefore, we investigated the effect of caffeine on the activation of primary HSCs isolated from mice. Caffeine suppressed the activation of HSC in a concentration-dependent manner. BAPTA-AM, an intracellular Ca chelator, had no effect on the caffeine-induced suppression of HSC activation. None of the isoform-selective inhibitors of phosphodiesterase1 to 5 affected changes in the morphology of HSC during activation, whereas CGS-15943, an adenosine receptor antagonist, inhibited them. Caffeine had no effect on intracellular cAMP level or on the phosphorylation of extracellular signal-regulated kinase (ERK)1/2. In contrast, caffeine significantly decreased the phosphorylation of Akt1. These results suggest that caffeine inhibits HSC activation by antagonizing adenosine receptors, leading to Akt1 signaling activation.
[Mh] Termos MeSH primário: Cafeína/farmacologia
AMP Cíclico/metabolismo
Células Estreladas do Fígado/efeitos dos fármacos
Inibidores de Fosfodiesterase/farmacologia
Receptores Purinérgicos P1/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Quelantes/farmacologia
Relação Dose-Resposta a Droga
Ácido Egtázico/análogos & derivados
Ácido Egtázico/farmacologia
Cirrose Hepática/tratamento farmacológico
Sistema de Sinalização das MAP Quinases/efeitos dos fármacos
Masculino
Camundongos
Fosforilação
Quinazolinas/farmacologia
Triazóis/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chelating Agents); 0 (Phosphodiesterase Inhibitors); 0 (Quinazolines); 0 (Receptors, Purinergic P1); 0 (Triazoles); 104615-18-1 (9-chloro-2-(2-furyl)-(1,2,4)triazolo(1,5-c)quinazolin-5-imine); 139890-68-9 (1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester); 3G6A5W338E (Caffeine); 526U7A2651 (Egtazic Acid); E0399OZS9N (Cyclic AMP)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE
[do] DOI:10.1248/bpb.b16-00947


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[PMID]:28410965
[Au] Autor:Tsuneoka Y; Irie M; Tanaka Y; Sugimoto T; Kobayashi Y; Kusakabe T; Kato K; Hamaguchi S; Namekata I; Tanaka H
[Ad] Endereço:Department of Pharmacology, Faculty of Pharmaceutical Sciences, Toho University, Funabashi, Chiba 274-8510, Japan; Laboratory of Pharmacology, Faculty of Pharmaceutical Science, Tokyo University of Sciences, Noda, Chiba 278-8510, Japan.
[Ti] Título:Permissive role of reduced inwardly-rectifying potassium current density in the automaticity of the guinea pig pulmonary vein myocardium.
[So] Source:J Pharmacol Sci;133(4):195-202, 2017 Apr.
[Is] ISSN:1347-8648
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:The electrophysiological properties underlying the automaticity of the guinea pig pulmonary vein myocardium were studied. About 30% of the isolated pulmonary vein tissue preparations showed spontaneous electrical activity, as shown by glass microelectrode recordings from their myocardial layer. The remaining quiescent preparations had a resting membrane potential less negative than that in the left atria. Blockade of the acetylcholine activated potassium current (I ) by tertiapin induced a depolarizing shift of the resting membrane potential and automatic electrical activity in the pulmonary vein, but not in the atria. The tertiapin-induced electrical activity, as well as the spontaneous activity, was inhibited by the application of carbachol or by chelation of intracellular Ca by BAPTA. The isolated pulmonary vein cardiomyocytes had an I density similar to that of the atrial cardiomyocytes, but a lower density of the inwardly-rectifying potassium current (I ). Spontaneous Ca transients were observed in about 30% of the isolated pulmonary vein cardiomyocytes, but not in atrial cardiomyocytes. The Ca transients in the pulmonary vein cardiomyocytes were induced by tertiapin and inhibited by carbachol. These results indicate that the pulmonary vein cardiomyocytes have a reduced density of the inwardly-rectifying potassium current, which plays a permissive role in their intracellular Ca -dependent automaticity.
[Mh] Termos MeSH primário: Cálcio/metabolismo
Miócitos Cardíacos/metabolismo
Potássio/metabolismo
Potássio/fisiologia
Veias Pulmonares/metabolismo
Veias Pulmonares/fisiologia
[Mh] Termos MeSH secundário: Acetilcolina/antagonistas & inibidores
Acetilcolina/farmacologia
Potenciais de Ação/efeitos dos fármacos
Animais
Venenos de Abelha/antagonistas & inibidores
Venenos de Abelha/farmacologia
Carbacol/farmacologia
Ácido Egtázico/análogos & derivados
Ácido Egtázico/farmacologia
Fenômenos Eletrofisiológicos/efeitos dos fármacos
Cobaias
Técnicas In Vitro
Potenciais da Membrana/efeitos dos fármacos
Microscopia Confocal
Bloqueadores dos Canais de Potássio/farmacologia
Veias Pulmonares/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bee Venoms); 0 (Potassium Channel Blockers); 3A7MX9B7E8 (tertiapin); 526U7A2651 (Egtazic Acid); 8Y164V895Y (Carbachol); K22DDW77C0 (1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid); N9YNS0M02X (Acetylcholine); RWP5GA015D (Potassium); SY7Q814VUP (Calcium)
[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:170416
[St] Status:MEDLINE


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[PMID]:28274857
[Au] Autor:Li FJ; Tan KS; He CY
[Ad] Endereço:Department of Biological Sciences, National University of Singapore, 117543, Singapore; Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University of Singapore, 117545, Singapore. Electronic address: miclfj@nus.edu.sg.
[Ti] Título:BAPTA-AM decreases cellular pH, inhibits acidocalcisome acidification and autophagy in amino acid-starved T. brucei.
[So] Source:Mol Biochem Parasitol;213:26-29, 2017 Apr.
[Is] ISSN:1872-9428
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:To investigate the role of Ca signaling in starvation-induced autophagy in Trypanosoma brucei, the causative agent of human African trypanosomiasis, we used cell-permeant Ca chelator BAPTA-AM and cell impermeant chelator EGTA, and examined the potential involvement of several intracellular Ca signaling pathways in T. brucei autophagy. The results showed an unexpected effect of BAPTA-AM in decreasing cellular pH and inhibiting acidocalcisome acidification in starved cells. The implication of these results in the role of Ca signaling and cellular/organellar pH in T. brucei autophagy is discussed.
[Mh] Termos MeSH primário: Aminoácidos/metabolismo
Autofagia
Quelantes/metabolismo
Ácido Egtázico/análogos & derivados
Organelas/metabolismo
Trypanosoma brucei brucei/efeitos dos fármacos
Trypanosoma brucei brucei/metabolismo
[Mh] Termos MeSH secundário: Sinalização do Cálcio/efeitos dos fármacos
Ácido Egtázico/metabolismo
Concentração de Íons de Hidrogênio
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Chelating Agents); 139890-68-9 (1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester); 526U7A2651 (Egtazic Acid)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170901
[Lr] Data última revisão:
170901
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170310
[St] Status:MEDLINE


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[PMID]:28242308
[Au] Autor:Lu W; Jin Y; Xu J; Greenwood MP; Balment RJ
[Ad] Endereço:Key Laboratory of Exploration and Utilization of Aquatic Genetic Resources, Ministry of Education, Shanghai 201306, China; College of Fisheries and Life Science, Shanghai Ocean University, Shanghai 201306, China. Electronic address: wqlv@shou.edu.cn.
[Ti] Título:Molecular characterisation and expression of parathyroid hormone-related protein in the caudal neurosecretory system of the euryhaline flounder, Platichthys flesus.
[So] Source:Gen Comp Endocrinol;249:24-31, 2017 Aug 01.
[Is] ISSN:1095-6840
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Parathyroid hormone-related protein (PTHrP) is a hypercalcemic factor in fish, but the source of circulating PTHrP remains unclear. In this study investigation of the caudal neurosecretory system (CNSS), considered one of major sources of PTHrP in fish, provided valuable insights into this regulatory system. We report pthrpa and pthrpb gene cloning, characterization, expression, and responses to low salinity and hypocalcemia challenge in flounder. The pthrpa and pthrpb precursors, isolated from a European flounder CNSS library, consist of 166 and 192 amino acid residues, respectively, with an overall homology of approximately 59.2%. Both precursors contain a signal peptide and a mature peptide with cleavage and amidation sites. The flounder PTHrPA and PTHrPB peptides share only 41% sequence identity with human PTHrPA. Quantitative PCR analysis demonstrated that the bone and bladder, are respectively major sites of pthrpa and pthrpb expression in flounder. Urophysectomy confirmed the CNSS as a likely contributor to circulating PTHrP peptides. There were no significant differences in CNSS pthrpa and pthrpb mRNA expression or plasma PTHrP levels between seawater (SW) and freshwater (FW)-adapted fish, though plasma total calcium concentrations were higher in FW animals. The intraperitonial administration of EGTA rapidly induced hypocalcemia and concomitant elevation in plasma PTHrP accompanied by increases in both pthrpa and pthrpb expression in the CNSS. Together, these findings support an evolutionary conserved role for PTHrP in the endocrine regulation of calcium.
[Mh] Termos MeSH primário: Linguado/genética
Sistemas Neurossecretores/metabolismo
Proteína Relacionada ao Hormônio Paratireóideo/genética
[Mh] Termos MeSH secundário: Aclimatação
Sequência de Aminoácidos
Animais
Cálcio/sangue
Clonagem Molecular
DNA Complementar/genética
Ácido Egtázico/administração & dosagem
Linguado/sangue
Linguado/metabolismo
Água Doce
Perfilação da Expressão Gênica
Hipocalcemia/sangue
Injeções Intraperitoneais
Proteína Relacionada ao Hormônio Paratireóideo/química
Proteína Relacionada ao Hormônio Paratireóideo/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Salinidade
Água do Mar
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Complementary); 0 (Parathyroid Hormone-Related Protein); 0 (RNA, Messenger); 526U7A2651 (Egtazic Acid); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170301
[St] Status:MEDLINE


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[PMID]:28154149
[Au] Autor:Johnson SL; Olt J; Cho S; von Gersdorff H; Marcotti W
[Ad] Endereço:Department of Biomedical Science, University of Sheffield, Sheffield S10 2TN, United Kingdom.
[Ti] Título:The Coupling between Ca Channels and the Exocytotic Ca Sensor at Hair Cell Ribbon Synapses Varies Tonotopically along the Mature Cochlea.
[So] Source:J Neurosci;37(9):2471-2484, 2017 Mar 01.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cochlea processes auditory signals over a wide range of frequencies and intensities. However, the transfer characteristics at hair cell ribbon synapses are still poorly understood at different frequency locations along the cochlea. Using recordings from mature gerbils, we report here a surprisingly strong block of exocytosis by the slow Ca buffer EGTA (10 mM) in basal hair cells tuned to high frequencies (∼30 kHz). In addition, using recordings from gerbil, mouse, and bullfrog auditory organs, we find that the spatial coupling between Ca influx and exocytosis changes from nanodomain in low-frequency tuned hair cells (∼<2 kHz) to progressively more microdomain in high-frequency cells (∼>2 kHz). Hair cell synapses have thus developed remarkable frequency-dependent tuning of exocytosis: accurate low-latency encoding of onset and offset of sound intensity in the cochlea's base and submillisecond encoding of membrane receptor potential fluctuations in the apex for precise phase-locking to sound signals. We also found that synaptic vesicle pool recovery from depletion was sensitive to high concentrations of EGTA, suggesting that intracellular Ca buffers play an important role in vesicle recruitment in both low- and high-frequency hair cells. In conclusion, our results indicate that microdomain coupling is important for exocytosis in high-frequency hair cells, suggesting a novel hypothesis for why these cells are more susceptible to sound-induced damage than low-frequency cells; high-frequency inner hair cells must have a low Ca buffer capacity to sustain exocytosis, thus making them more prone to Ca -induced cytotoxicity. In the inner ear, sensory hair cells signal reception of sound. They do this by converting the sound-induced movement of their hair bundles present at the top of these cells, into an electrical current. This current depolarizes the hair cell and triggers the calcium-induced release of the neurotransmitter glutamate that activates the postsynaptic auditory fibers. The speed and precision of this process enables the brain to perceive the vital components of sound, such as frequency and intensity. We show that the coupling strength between calcium channels and the exocytosis calcium sensor at inner hair cell synapses changes along the mammalian cochlea such that the timing and/or intensity of sound is encoded with high precision.
[Mh] Termos MeSH primário: Canais de Cálcio Tipo L/metabolismo
Cálcio/metabolismo
Cóclea/citologia
Exocitose/fisiologia
Células Ciliadas Auditivas/fisiologia
Sinapses/fisiologia
[Mh] Termos MeSH secundário: Fatores Etários
Animais
Animais Recém-Nascidos
Quelantes de Cálcio/farmacologia
Relação Dose-Resposta a Droga
Ácido Egtázico/farmacologia
Potenciais Pós-Sinápticos Excitadores/efeitos dos fármacos
Feminino
Gerbillinae
Técnicas In Vitro
Masculino
Camundongos
Técnicas de Patch-Clamp
Rana catesbeiana
Sinapses/efeitos dos fármacos
Vesículas Sinápticas/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calcium Channels, L-Type); 0 (Calcium Chelating Agents); 526U7A2651 (Egtazic Acid); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170204
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.2867-16.2017


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[PMID]:28130864
[Au] Autor:Fang W; Fa ZZ; Xie Q; Wang GZ; Yi J; Zhang C; Meng GX; Gu JL; Liao WQ
[Ad] Endereço:PLA Key Laboratory of Mycosis, Department of Dermatology and Venereology, Changzheng Hospital, Shanghai, China.
[Ti] Título:Complex Roles of Annexin A2 in Host Blood-Brain Barrier Invasion by Cryptococcus neoformans.
[So] Source:CNS Neurosci Ther;23(4):291-300, 2017 Apr.
[Is] ISSN:1755-5949
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Fungal transversal across the brain microvascular endothelial cells (BMECs) is the essential step for the development of cryptococcal meningoencephalitis. Annexin A2 (AnxA2) is an important signaling protein involved in several intracellular processes such as membrane trafficking, endocytosis, and exocytosis. AIM: To investigate the roles and mechanism of AnxA2 during cryptococcal transversal of BMECs. RESULTS: Cryptococcus neoformans infection initiated upregulation of AnxA2 in mouse BMECs. Blockade with anti-AnxA2 antibody led to a reduction in fungal transcytosis activity but no change in its adhesion efficiency. Intriguingly, AnxA2 depletion caused a significant increase in fungal association activity but had no effect on their transcytosis. AnxA2 suppression resulted in marked reduction in its partner protein S100A10, and S100A10 suppression in BMECs significantly reduced the cryptococcal transcytosis efficiency. Furthermore, AnxA2 dephosphorylation at Tyr23 and dephosphorylation of downstream cofilin were required for cryptococcal transversal of BMECs, both of which might be primarily involved in the association of C. neoformans with host cells. CONCLUSIONS: Our work indicated that AnxA2 played complex roles in traversal of C. neoformans across host BMECs, which might be dependent on downstream cofilin to inhibit fungal adhesion but rely on its partner S100A10 to promote cryptococcal transcytosis.
[Mh] Termos MeSH primário: Anexina A2/metabolismo
Barreira Hematoencefálica/metabolismo
Barreira Hematoencefálica/microbiologia
Encéfalo/citologia
Cryptococcus neoformans
Células Endoteliais/metabolismo
[Mh] Termos MeSH secundário: Fatores de Despolimerização de Actina/metabolismo
Animais
Anexina A2/genética
Anexina A2/imunologia
Anticorpos/farmacologia
Barreira Hematoencefálica/patologia
Quelantes/farmacologia
Ácido Egtázico/análogos & derivados
Ácido Egtázico/farmacologia
Células Endoteliais/efeitos dos fármacos
Células Endoteliais/microbiologia
Regulação Fúngica da Expressão Gênica/efeitos dos fármacos
Regulação Fúngica da Expressão Gênica/genética
Camundongos
Mutação/genética
Fosforilação
Pirimidinas/farmacologia
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Proteínas S100/metabolismo
Fatores de Tempo
Transcitose/efeitos dos fármacos
Transcitose/genética
Tirosina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AG 1879); 0 (Actin Depolymerizing Factors); 0 (Annexin A2); 0 (Antibodies); 0 (Chelating Agents); 0 (Pyrimidines); 0 (RNA, Small Interfering); 0 (S100 Proteins); 0 (S100 calcium binding protein A10); 139890-68-9 (1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester); 42HK56048U (Tyrosine); 526U7A2651 (Egtazic Acid)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170129
[St] Status:MEDLINE
[do] DOI:10.1111/cns.12673


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[PMID]:28130160
[Au] Autor:Saavedra A; Fernández-García S; Cases S; Puigdellívol M; Alcalá-Vida R; Martín-Flores N; Alberch J; Ginés S; Malagelada C; Pérez-Navarro E
[Ad] Endereço:Departament de Biomedicina, Facultat de Medicina, Institut de Neurociències, Universitat de Barcelona, Catalonia, Spain; Institut d'Investigacions Biomèdiques August Pi i Sunyer (IDIBAPS), Barcelona, Catalonia, Spain; Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas (CI
[Ti] Título:Chelerythrine promotes Ca -dependent calpain activation in neuronal cells in a PKC-independent manner.
[So] Source:Biochim Biophys Acta;1861(4):922-935, 2017 04.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Chelerythrine is widely used as a broad range protein kinase C (PKC) inhibitor, but there is controversy about its inhibitory effect. Moreover, it has been shown to exert PKC-independent effects on non-neuronal cells. METHODS: In this study we investigated possible off-target effects of chelerythrine on cultured cortical rodent neurons and a neuronal cell line. RESULTS: We found that 10µM chelerythrine, a commonly used concentration in neuronal cultures, reduces PKC and cAMP-dependent protein kinase substrates phosphorylation in mouse cultured cortical neurons, but not in rat primary cortical neurons or in a striatal cell line. Furthermore, we found that incubation with chelerythrine increases pERK1/2 levels in all models studied. Moreover, our results show that chelerythrine promotes calpain activation as assessed by the cleavage of spectrin, striatal-enriched protein tyrosine phosphatase and calcineurin A. Remarkably, chelerythrine induces a concentration-dependent increase in intracellular Ca levels that mediates calpain activation. In addition, we found that chelerythrine induces ERK1/2- and calpain-independent caspase-3 activation that can be prevented by the Ca chelator BAPTA-AM. CONCLUSIONS: This is the first report showing that chelerythrine promotes Ca -dependent calpain activation in neuronal cells, which has consequences for the interpretation of studies using this compound. GENERAL SIGNIFICANCE: Chelerythrine is still marketed as a specific PKC inhibitor and extensively used in signal transduction studies. We believe that the described off-target effects should preclude its use as a PKC inhibitor in future works.
[Mh] Termos MeSH primário: Benzofenantridinas/farmacologia
Cálcio/metabolismo
Calpaína/metabolismo
Proteínas de Membrana/farmacologia
Neurônios/efeitos dos fármacos
Neurônios/metabolismo
Proteína Quinase C/metabolismo
[Mh] Termos MeSH secundário: Animais
Calcineurina/metabolismo
Caspase 3/metabolismo
Células Cultivadas
Proteínas Quinases Dependentes de AMP Cíclico/metabolismo
Ácido Egtázico/análogos & derivados
Ácido Egtázico/farmacologia
Ativação Enzimática/efeitos dos fármacos
Sistema de Sinalização das MAP Quinases/efeitos dos fármacos
Camundongos
Proteínas Tirosina Fosfatases/metabolismo
Ratos
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Benzophenanthridines); 0 (Membrane Proteins); 0 (calpain activator); 139890-68-9 (1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl ester); 526U7A2651 (Egtazic Acid); E3B045W6X0 (chelerythrine); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases); EC 2.7.11.13 (Protein Kinase C); EC 3.1.3.16 (Calcineurin); EC 3.1.3.48 (Protein Tyrosine Phosphatases); EC 3.4.22.- (Calpain); EC 3.4.22.- (Caspase 3); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170129
[St] Status:MEDLINE


  10 / 9871 MEDLINE  
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[PMID]:28075020
[Au] Autor:Bader A; Bintig W; Begandt D; Klett A; Siller IG; Gregor C; Schaarschmidt F; Weksler B; Romero I; Couraud PO; Hell SW; Ngezahayo A
[Ad] Endereço:Institute of Biophysics, Leibniz University Hannover, Hannover, Germany.
[Ti] Título:Adenosine receptors regulate gap junction coupling of the human cerebral microvascular endothelial cells hCMEC/D3 by Ca influx through cyclic nucleotide-gated channels.
[So] Source:J Physiol;595(8):2497-2517, 2017 Apr 15.
[Is] ISSN:1469-7793
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:KEY POINTS: Gap junction channels are essential for the formation and regulation of physiological units in tissues by allowing the lateral cell-to-cell diffusion of ions, metabolites and second messengers. Stimulation of the adenosine receptor subtype A increases the gap junction coupling in the human blood-brain barrier endothelial cell line hCMEC/D3. Although the increased gap junction coupling is cAMP-dependent, neither the protein kinase A nor the exchange protein directly activated by cAMP were involved in this increase. We found that cAMP activates cyclic nucleotide-gated (CNG) channels and thereby induces a Ca influx, which leads to the increase in gap junction coupling. The report identifies CNG channels as a possible physiological link between adenosine receptors and the regulation of gap junction channels in endothelial cells of the blood-brain barrier. ABSTRACT: The human cerebral microvascular endothelial cell line hCMEC/D3 was used to characterize the physiological link between adenosine receptors and the gap junction coupling in endothelial cells of the blood-brain barrier. Expressed adenosine receptor subtypes and connexin (Cx) isoforms were identified by RT-PCR. Scrape loading/dye transfer was used to evaluate the impact of the A and A adenosine receptor subtype agonist 2-phenylaminoadenosine (2-PAA) on the gap junction coupling. We found that 2-PAA stimulated cAMP synthesis and enhanced gap junction coupling in a concentration-dependent manner. This enhancement was accompanied by an increase in gap junction plaques formed by Cx43. Inhibition of protein kinase A did not affect the 2-PAA-related enhancement of gap junction coupling. In contrast, the cyclic nucleotide-gated (CNG) channel inhibitor l-cis-diltiazem, as well as the chelation of intracellular Ca with BAPTA, or the absence of external Ca , suppressed the 2-PAA-related enhancement of gap junction coupling. Moreover, we observed a 2-PAA-dependent activation of CNG channels by a combination of electrophysiology and pharmacology. In conclusion, the stimulation of adenosine receptors in hCMEC/D3 cells induces a Ca influx by opening CNG channels in a cAMP-dependent manner. Ca in turn induces the formation of new gap junction plaques and a consecutive sustained enhancement of gap junction coupling. The report identifies CNG channels as a physiological link that integrates gap junction coupling into the adenosine receptor-dependent signalling of endothelial cells of the blood-brain barrier.
[Mh] Termos MeSH primário: Cálcio/metabolismo
Canais de Cátion Regulados por Nucleotídeos Cíclicos/metabolismo
Células Endoteliais/metabolismo
Junções Comunicantes/metabolismo
Microvasos/metabolismo
Receptor A2B de Adenosina/fisiologia
[Mh] Termos MeSH secundário: Adenosina/análogos & derivados
Adenosina/farmacologia
Barreira Hematoencefálica/efeitos dos fármacos
Barreira Hematoencefálica/metabolismo
Linhagem Celular
Ácido Egtázico/análogos & derivados
Ácido Egtázico/farmacologia
Células Endoteliais/efeitos dos fármacos
Junções Comunicantes/efeitos dos fármacos
Técnicas de Silenciamento de Genes
Seres Humanos
Microvasos/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cyclic Nucleotide-Gated Cation Channels); 0 (Receptor, Adenosine A2B); 526U7A2651 (Egtazic Acid); K22DDW77C0 (1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid); K40I59G1EF (2-phenylaminoadenosine); K72T3FS567 (Adenosine); SY7Q814VUP (Calcium)
[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:170112
[St] Status:MEDLINE
[do] DOI:10.1113/JP273150



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