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[PMID]:29362376
[Au] Autor:Ullman JC; Yang J; Sullivan M; Bendor J; Levy J; Pham E; Silm K; Seifikar H; Sohal VS; Nicoll RA; Edwards RH
[Ad] Endereço:Departments of Neurology and Physiology, UCSF School of Medicine, San Francisco, CA, 94143, USA.
[Ti] Título:A mouse model of autism implicates endosome pH in the regulation of presynaptic calcium entry.
[So] Source:Nat Commun;9(1):330, 2018 01 23.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Psychoactive compounds such as chloroquine and amphetamine act by dissipating the pH gradient across intracellular membranes, but the physiological mechanisms that normally regulate organelle pH remain poorly understood. Interestingly, recent human genetic studies have implicated the endosomal Na /H exchanger NHE9 in both autism spectrum disorders (ASD) and attention deficit hyperactivity disorder (ADHD). Plasma membrane NHEs regulate cytosolic pH, but the role of intracellular isoforms has remained unclear. We now find that inactivation of NHE9 in mice reproduces behavioral features of ASD including impaired social interaction, repetitive behaviors, and altered sensory processing. Physiological characterization reveals hyperacidic endosomes, a cell-autonomous defect in glutamate receptor expression and impaired neurotransmitter release due to a defect in presynaptic Ca entry. Acute inhibition of synaptic vesicle acidification rescues release but without affecting the primary defect due to loss of NHE9.
[Mh] Termos MeSH primário: Transtorno do Deficit de Atenção com Hiperatividade/metabolismo
Transtorno do Espectro Autista/metabolismo
Cálcio/metabolismo
Endossomos/metabolismo
Neurônios/metabolismo
Trocadores de Sódio-Hidrogênio/genética
[Mh] Termos MeSH secundário: Animais
Transtorno do Deficit de Atenção com Hiperatividade/genética
Transtorno do Deficit de Atenção com Hiperatividade/fisiopatologia
Transtorno do Espectro Autista/genética
Transtorno do Espectro Autista/fisiopatologia
Comportamento Animal
Modelos Animais de Doenças
Eletroencefalografia
Endossomos/patologia
Feminino
Expressão Gênica
Ácido Glutâmico/metabolismo
Hipocampo/metabolismo
Hipocampo/fisiopatologia
Seres Humanos
Concentração de Íons de Hidrogênio
Masculino
Camundongos
Camundongos Knockout
Neurônios/patologia
Terminações Pré-Sinápticas/metabolismo
Terminações Pré-Sinápticas/patologia
Cultura Primária de Células
Trocadores de Sódio-Hidrogênio/deficiência
Transmissão Sináptica/fisiologia
Vesículas Sinápticas/metabolismo
Vesículas Sinápticas/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (NHE9 protein, mouse); 0 (Sodium-Hydrogen Exchangers); 3KX376GY7L (Glutamic Acid); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180125
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02716-5


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[PMID]:29236392
[Au] Autor:Rudnytska MV; Palladina TA
[Ti] Título:Effect of preparations Methyure and Ivine on Са(2+)-ATPases activity in plasma and vacuolar membrane of corn seedling roots under salt stress conditions.
[So] Source:Ukr Biochem J;89(1):76-81, 2017 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:Ca2+-ATPases regulate the functioning of Ca2+-dependent signaling pathway SOS which provides removal of Na+ from the cytoplasm of cells via Na+/H+-antiporters in saline conditions. The influence of synthetic preparations Methyure and Ivine on the Ca2+-ATPase activity was investigated. It was shown that exposition of corn seedlings in the presence of 0.1 M NaCl rather enhanced hydrolytic than transport activity of Ca2+-ATPases in plasma and vacuolar membrane of root cells. It was found that seed treatment with such preparations, especially Methyure, caused intensification of the both activities of Ca2+-ATPases, mainly in vacuolar membrane. The results indicate than salt protective activity of preparations, especially Methyure, is associated with increased Ca2+-ATPase activity, which regulates the functioning of Na+/H+-antiporters.
[Mh] Termos MeSH primário: ATPases Transportadoras de Cálcio/metabolismo
Membrana Celular/efeitos dos fármacos
Substâncias Protetoras/farmacologia
Pirimidinas/farmacologia
Trocadores de Sódio-Hidrogênio/metabolismo
Vacúolos/efeitos dos fármacos
Zea mays/efeitos dos fármacos
[Mh] Termos MeSH secundário: Adaptação Fisiológica
Membrana Celular/metabolismo
Membranas Intracelulares/efeitos dos fármacos
Membranas Intracelulares/metabolismo
Transporte de Íons
Células Vegetais/efeitos dos fármacos
Células Vegetais/metabolismo
Raízes de Plantas/efeitos dos fármacos
Raízes de Plantas/metabolismo
Salinidade
Plântulas/efeitos dos fármacos
Plântulas/metabolismo
Cloreto de Sódio/farmacologia
Trocadores de Sódio-Hidrogênio/agonistas
Estresse Fisiológico
Vacúolos/metabolismo
Zea mays/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protective Agents); 0 (Pyrimidines); 0 (Sodium-Hydrogen Exchangers); 451W47IQ8X (Sodium Chloride); EC 3.6.3.8 (Calcium-Transporting ATPases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj89.01.076


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[PMID]:28466186
[Au] Autor:Tai F; Lv S; Jiang P; Wang J; Feng J; Li Y
[Ad] Endereço:Key Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, No. 20 Nanxincun, Xiangshan, Beijing, 100093, China.
[Ti] Título:Establishment of a gene function analysis system for the euhalophyte Salicornia europaea L.
[So] Source:Plant Cell Rep;36(8):1251-1261, 2017 Aug.
[Is] ISSN:1432-203X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:KEY MESSAGE: A Salicornia europaea L. in vitro cell transformation system was developed and further applied to SeNHX1 function investigation. The exploration of salt-tolerant genes from halophyte has seriously been limited by the lack of self-dependent transformation system. Here, an Agrobacterium tumefaciens-mediated in vitro cell transformation system of euhalophyte Salicornia europaea L. was developed. Calli derived from hypocotyl of S. europaea were co-cultured for 3 days with Agrobacterium at OD ranging from 1.0 to 1.5 and then selected with 25 mg/L hygromycin (Hyg). The transformed cells were identified from Hyg positive calli by GUS assay and qRT-PCR, and the transformation efficiency was up to 74.4%. The practicality of this system was further tested via genetic manipulation of S. europaea Na /H antiporter 1 (SeNHX1) gene by creating the overexpressing, silencing, and empty vector cells. Survival ratio and Na distribution under salt treatment showed obvious differences in SeNHX1-overexpressing, -silencing, and empty vector cells, indicating the feasibility of this system to analyze gene function. This investigation is enlightening for studies in other non-model plants lacking of self-dependent transformation system.
[Mh] Termos MeSH primário: Chenopodiaceae/metabolismo
[Mh] Termos MeSH secundário: Agrobacterium tumefaciens/genética
Chenopodiaceae/efeitos dos fármacos
Chenopodiaceae/genética
Hipocótilo/efeitos dos fármacos
Hipocótilo/genética
Hipocótilo/metabolismo
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Plantas Geneticamente Modificadas/efeitos dos fármacos
Plantas Geneticamente Modificadas/genética
Plantas Geneticamente Modificadas/metabolismo
Tolerância a Sal/genética
Plantas Tolerantes a Sal/efeitos dos fármacos
Plantas Tolerantes a Sal/genética
Plantas Tolerantes a Sal/metabolismo
Cloreto de Sódio/farmacologia
Trocadores de Sódio-Hidrogênio/genética
Trocadores de Sódio-Hidrogênio/metabolismo
Transformação Genética/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); 0 (Sodium-Hydrogen Exchangers); 451W47IQ8X (Sodium Chloride)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180102
[Lr] Data última revisão:
180102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1007/s00299-017-2150-z


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[PMID]:27777302
[Au] Autor:Cheng B; Meng Y; Cui Y; Li C; Tao F; Yin H; Yang C; Xu P
[Ad] Endereço:From the State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100 and.
[Ti] Título:Alkaline Response of a Halotolerant Alkaliphilic Halomonas Strain and Functional Diversity of Its Na+(K+)/H+ Antiporters.
[So] Source:J Biol Chem;291(50):26056-26065, 2016 Dec 09.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Halomonas sp. Y2 is a halotolerant alkaliphilic strain from Na -rich pulp mill wastewater with high alkalinity (pH >11.0). Transcriptome analysis of this isolate revealed this strain may use various transport systems for pH homeostasis. In particular, the genes encoding four putative Na /H antiporters were differentially expressed upon acidic or alkaline conditions. Further evidence, from heterologous expression and mutant studies, suggested that Halomonas sp. Y2 employs its Na /H antiporters in a labor division way to deal with saline and alkaline environments. Ha-NhaD2 displayed robust Na (Li ) resistance and high transport activities in Escherichia coli; a ΔHa-nhaD2 mutant exhibited growth inhibition at high Na (Li ) concentrations at pH values of 6.2, 8.0, and 10.0, suggesting its physiological role in osmotic homeostasis. In contrast, Ha-NhaD1 showed much weaker activities in ion exporting and pH homeostasis. Ha-Mrp displayed a combination of properties similar to those of Mrp transporters from some Bacillus alkaliphiles and neutrophiles. This conferred obvious Na (Li , K ) resistance in E. coli-deficient strains, as those ion transport spectra of some neutrophil Mrp antiporters. Conversely, similar to the Bacillus alkaliphiles, Ha-Mrp showed central roles in the pH homeostasis of Halomonas sp. Y2. An Ha-mrp-disrupted mutant was seriously inhibited by high concentrations of Na (Li , K ) but only under alkaline conditions. Ha-NhaP was determined to be a K /H antiporter and shown to confer strong K resistance both at acidic and alkaline stresses.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Halomonas/metabolismo
Antiportadores de Potássio-Hidrogênio/metabolismo
Trocadores de Sódio-Hidrogênio/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Halomonas/química
Halomonas/genética
Concentração de Íons de Hidrogênio
Mutação
Antiportadores de Potássio-Hidrogênio/química
Antiportadores de Potássio-Hidrogênio/genética
Trocadores de Sódio-Hidrogênio/química
Trocadores de Sódio-Hidrogênio/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Potassium-Hydrogen Antiporters); 0 (Sodium-Hydrogen Exchangers)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171209
[Lr] Data última revisão:
171209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


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[PMID]:29038209
[Au] Autor:Packer M
[Ad] Endereço:From Baylor Heart and Vascular Institute, Baylor University Medical Center, Dallas, TX. milton.packer@baylorhealth.edu.
[Ti] Título:Activation and Inhibition of Sodium-Hydrogen Exchanger Is a Mechanism That Links the Pathophysiology and Treatment of Diabetes Mellitus With That of Heart Failure.
[So] Source:Circulation;136(16):1548-1559, 2017 Oct 17.
[Is] ISSN:1524-4539
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mechanisms underlying the progression of diabetes mellitus and heart failure are closely intertwined, such that worsening of one condition is frequently accompanied by worsening of the other; the degree of clinical acceleration is marked when the 2 coexist. Activation of the sodium-hydrogen exchanger in the heart and vasculature (NHE1 isoform) and the kidneys (NHE3 isoform) may serve as a common mechanism that links both disorders and may underlie their interplay. Insulin insensitivity and adipokine abnormalities (the hallmarks of type 2 diabetes mellitus) are characteristic features of heart failure; conversely, neurohormonal systems activated in heart failure (norepinephrine, angiotensin II, aldosterone, and neprilysin) impair insulin sensitivity and contribute to microvascular disease in diabetes mellitus. Each of these neurohormonal derangements may act through increased activity of both NHE1 and NHE3. Drugs used to treat diabetes mellitus may favorably affect the pathophysiological mechanisms of heart failure by inhibiting either or both NHE isoforms, and drugs used to treat heart failure may have beneficial effects on glucose tolerance and the complications of diabetes mellitus by interfering with the actions of NHE1 and NHE3. The efficacy of NHE inhibitors on the risk of cardiovascular events may be enhanced when heart failure and glucose intolerance coexist and may be attenuated when drugs with NHE inhibitory actions are given concomitantly. Therefore, the sodium-hydrogen exchanger may play a central role in the interplay of diabetes mellitus and heart failure, contribute to the physiological and clinical progression of both diseases, and explain certain drug-drug and drug-disease interactions that have been reported in large-scale randomized clinical trials.
[Mh] Termos MeSH primário: Proteínas de Transporte de Cátions/metabolismo
Diabetes Mellitus/metabolismo
Insuficiência Cardíaca/metabolismo
Trocadores de Sódio-Hidrogênio/metabolismo
[Mh] Termos MeSH secundário: Animais
Fármacos Cardiovasculares/efeitos adversos
Proteínas de Transporte de Cátions/antagonistas & inibidores
Comorbidade
Diabetes Mellitus/tratamento farmacológico
Diabetes Mellitus/epidemiologia
Diabetes Mellitus/fisiopatologia
Progressão da Doença
Interações Medicamentosas
Insuficiência Cardíaca/tratamento farmacológico
Insuficiência Cardíaca/epidemiologia
Insuficiência Cardíaca/fisiopatologia
Seres Humanos
Hipoglicemiantes/efeitos adversos
Polimedicação
Fatores de Risco
Trocador 1 de Sódio-Hidrogênio
Trocador 3 de Sódio-Hidrogênio
Trocadores de Sódio-Hidrogênio/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Cardiovascular Agents); 0 (Cation Transport Proteins); 0 (Hypoglycemic Agents); 0 (SLC9A1 protein, human); 0 (SLC9A3 protein, human); 0 (Sodium-Hydrogen Exchanger 1); 0 (Sodium-Hydrogen Exchanger 3); 0 (Sodium-Hydrogen Exchangers)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171018
[St] Status:MEDLINE
[do] DOI:10.1161/CIRCULATIONAHA.117.030418


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[PMID]:28768665
[Au] Autor:Hu MC; Bobulescu IA; Quiñones H; Gisler SM; Moe OW
[Ad] Endereço:Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, Texas; Ming-Chang.Hu@UTSouthwestern.edu.
[Ti] Título:Dopamine reduces cell surface Na /H exchanger-3 protein by decreasing NHE3 exocytosis and cell membrane recycling.
[So] Source:Am J Physiol Renal Physiol;313(4):F1018-F1025, 2017 Oct 01.
[Is] ISSN:1522-1466
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The intrarenal autocrine-paracrine dopamine (DA) system mediates a significant fraction of the natriuresis in response to a salt load. DA inhibits a number of Na transporters to effect sodium excretion, including the proximal tubule Na /H exchanger-3 (NHE3). DA represent a single hormone that regulates NHE3 at multiple levels, including translation, degradation, endocytosis, and protein phosphorylation. Because cell surface NHE3 protein is determined by the balance between exocytotic insertion and endocytotic retrieval, we examined whether DA acutely affects the rate of NHE3 exocytosis in a cell culture model. DA inhibited NHE3 exocytosis at a dose-dependent manner with a half maximal around 10 M. The DA effect on NHE3 exocytosis was blocked by inhibition of protein kinase A and by brefeldin A, which inhibits endoplasmic reticulum-to-Golgi transport. NHE3 directly interacts with the ε-subunit of coatomer protein based on yeast-two-hybrid and coimmunoprecipitation. Because NHE3 has been shown to be recycled back to the cell membrane after endocytosis, we measured NHE3 recycling using a biochemical reinsertion assay and showed that reinsertion of NHE3 back to the membrane is also inhibited by DA. In conclusion, among the many mechanisms by which DA reduces apical membrane NHE3 and induces proximal tubule natriuresis, one additional mechanism is inhibition of exocytotic insertion and reinsertion of NHE3 in the apical cell surface.
[Mh] Termos MeSH primário: Membrana Celular/efeitos dos fármacos
Dopamina/farmacologia
Exocitose/efeitos dos fármacos
Rim/efeitos dos fármacos
Trocadores de Sódio-Hidrogênio/metabolismo
[Mh] Termos MeSH secundário: Animais
Membrana Celular/metabolismo
Células Cultivadas
Didelphis
Relação Dose-Resposta a Droga
Regulação para Baixo
Rim/metabolismo
Natriurese/efeitos dos fármacos
Transporte Proteico
Trocador 3 de Sódio-Hidrogênio
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Sodium-Hydrogen Exchanger 3); 0 (Sodium-Hydrogen Exchangers); VTD58H1Z2X (Dopamine)
[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:170804
[St] Status:MEDLINE
[do] DOI:10.1152/ajprenal.00251.2017


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[PMID]:28750048
[Au] Autor:Patiño-Ruiz M; Ganea C; Fendler K; Calinescu O
[Ad] Endereço:Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
[Ti] Título:Competition is the basis of the transport mechanism of the NhaB Na+/H+ exchanger from Klebsiella pneumoniae.
[So] Source:PLoS One;12(7):e0182293, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Na+/H+ exchange is essential for survival of all organisms, having a role in the regulation of the intracellular Na+ concentration, pH and cell volume. Furthermore, Na+/H+ exchangers were shown to be involved in the virulence of the bacterium Yersinia pestis, indicating they might be potential targets for novel antibiotic treatments. The model system for Na+/H+ exchangers is the NhaA transporter from Escherichia coli, EcNhaA. Therefore, the general transport mechanism of NhaA exchangers is currently well characterized. However, much less is known about NhaB exchangers, with only a limited number of studies available. The pathogen Klebsiella pneumoniae, which is a major source of nosocomial infection, possesses three electrogenic Na+/H+ exchangers, KpNhaA1, KpNhaA2 and KpNhaB, none of which have been previously investigated. Our aim in this study was to functionally characterize KpNhaB using solid supported membrane-based electrophysiology as the main investigation technique, and thus provide the first electrophysiological investigation of an NhaB Na+/H+ exchanger. We found that NhaB can be described by the same competition-based mechanism that was shown to be valid for electrogenic NhaA and NapA, and for electroneutral NhaP Na+/H+ exchangers. For comparison we also characterized the activity of KpNhaA1 and KpNhaA2 and found that the three exchangers have complementary activity profiles, which is likely a survival advantage for K. pneumoniae when faced with environments of different salinity and pH. This underlines their importance as potential antibiotic drug targets.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Klebsiella pneumoniae/metabolismo
Trocadores de Sódio-Hidrogênio/metabolismo
[Mh] Termos MeSH secundário: Laranja Acridina/metabolismo
Sequência de Aminoácidos
Proteínas de Bactérias/química
Transporte Biológico/efeitos dos fármacos
Membrana Celular/efeitos dos fármacos
Membrana Celular/metabolismo
Escherichia coli/metabolismo
Concentração de Íons de Hidrogênio
Cinética
Lítio/farmacologia
Viabilidade Microbiana/efeitos dos fármacos
Alinhamento de Sequência
Sódio/farmacologia
Trocadores de Sódio-Hidrogênio/química
Especificidade por Substrato/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Sodium-Hydrogen Exchangers); 9FN79X2M3F (Lithium); 9NEZ333N27 (Sodium); F30N4O6XVV (Acridine Orange)
[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:170728
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182293


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[PMID]:28739734
[Au] Autor:Yang F; Gu Y; Zhao Z; Huang J; Jiang WG; Cheng S
[Ad] Endereço:Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Capital Medical University, Beijing, P.R. China.
[Ti] Título:NHERF1 Suppresses Lung Cancer Cell Migration by Regulation of Epithelial-Mesenchymal Transition.
[So] Source:Anticancer Res;37(8):4405-4414, 2017 08.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: Na(+)/H(+) exchanger regulatory factor 1 (NHERF1) has been reported to interact with many cancer-related proteins and plays an important role in cancer progression. However, little is known about the biological functions of NHERF1 in lung cancer cells. The aim of the current study was to explore whether NHERF1 is involved in transforming growth factor (TGF)-ß1-induced epithelial-mesenchymal transition (EMT) in non-small-cell lung cancer cells. MATERIALS AND METHODS: The expression of NHERF1 and EMT-associated markers including E-cadherin, N-cadherin, snail family transcriptional repressor 1 (SNAI1) and snail family transcriptional repressor 2 (SLUG) were analyzed by reverse transcription polymerase chain reaction (RT-PCR) and western blotting. The migratory properties of cells were assessed using a wound-healing assay. RESULTS: TGF-ß1-induced a pro-migratory response in the A549 lung cancer cell line, that was consistently associated with corresponding changes in the expression levels of EMT-related genes. The expression of NHERF1 significantly decreased in the TGF-ß1-induced A549 cells. Overexpression of NHERF1 significantly inhibited the migratory ability of cells and reversed the TGF-ß1-induced mesenchymal phenotype of A549 cells. CONCLUSION: These data showed an important role of NHERF1 in the EMT of non-small-cell lung cancer cells, as well as migration.
[Mh] Termos MeSH primário: Carcinoma Pulmonar de Células não Pequenas/metabolismo
Neoplasias Pulmonares/metabolismo
Fosfoproteínas/genética
Fosfoproteínas/metabolismo
Trocadores de Sódio-Hidrogênio/genética
Trocadores de Sódio-Hidrogênio/metabolismo
[Mh] Termos MeSH secundário: Células A549
Biomarcadores Tumorais
Carcinoma Pulmonar de Células não Pequenas/genética
Movimento Celular/efeitos dos fármacos
Regulação para Baixo/efeitos dos fármacos
Transição Epitelial-Mesenquimal/efeitos dos fármacos
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Neoplasias Pulmonares/genética
Fator de Crescimento Transformador beta/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Phosphoproteins); 0 (Sodium-Hydrogen Exchangers); 0 (Transforming Growth Factor beta); 0 (sodium-hydrogen exchanger regulatory factor)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE


  9 / 6675 MEDLINE  
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[PMID]:28739728
[Au] Autor:Wang L; Qi Y; Xiong Y; Peng Z; Ma Q; Zhang Y; Song J; Zheng J
[Ad] Endereço:Department of Urology, Beijing Friendship Hospital, Capital Medical University, Beijing, P.R. China.
[Ti] Título:Ezrin-Radixin-Moesin Binding Phosphoprotein 50 (EBP50) Suppresses the Metastasis of Breast Cancer and HeLa Cells by Inhibiting Matrix Metalloproteinase-2 Activity.
[So] Source:Anticancer Res;37(8):4353-4360, 2017 08.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Expression of ezrin-radixin-moesin-binding phosphoprotein-50 (EBP50) is correlated with human breast and cervical cancer development, but its effects on the metastasis of breast and cervical cancer and the underlying mechanism are not fully understood. MATERIALS AND METHODS: In this study, EBP50 was overexpressed in MDA-MB-231 breast cancer and HeLa cervical cancer cells; moreover, EBP50 was knocked-down in MCF-7 breast cancer cells and HeLa cells. Metastasis-related ability and matrix metalloproteinase-2 (MMP-2) activity of these cells were investigated. RESULTS: Cell adhesion, wound-healing and invasion were significantly suppressed in EBP50-overexpressing cells. Contrarily, EBP50-knockdown promoted cell adhesion, wound healing and invasion. EBP50 overexpression inhibited MMP-2 activity, and the knockdown of EBP50 promoted the activity of MMP-2, suggesting that EBP50 inhibited cell metastasis via suppression of MMP-2 activity. CONCLUSION: Our work reveals the anti-metastatic effect and a new mechanism of EBP50 action in breast and cervical cancer cells.
[Mh] Termos MeSH primário: Neoplasias da Mama/patologia
Metaloproteinase 2 da Matriz/metabolismo
Fosfoproteínas/metabolismo
Trocadores de Sódio-Hidrogênio/metabolismo
Neoplasias do Colo do Útero/patologia
[Mh] Termos MeSH secundário: Neoplasias da Mama/metabolismo
Adesão Celular
Movimento Celular
Proliferação Celular
Feminino
Regulação Neoplásica da Expressão Gênica
Técnicas de Silenciamento de Genes
Células HeLa
Seres Humanos
Células MCF-7
Metástase Neoplásica
Fosfoproteínas/genética
Trocadores de Sódio-Hidrogênio/genética
Regulação para Cima
Neoplasias do Colo do Útero/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phosphoproteins); 0 (Sodium-Hydrogen Exchangers); 0 (sodium-hydrogen exchanger regulatory factor); EC 3.4.24.24 (MMP2 protein, human); EC 3.4.24.24 (Matrix Metalloproteinase 2)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE


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[PMID]:28723926
[Au] Autor:Chen X; Lu X; Shu N; Wang D; Wang S; Wang J; Guo L; Guo X; Fan W; Lin Z; Ye W
[Ad] Endereço:State Key Laboratory of Cotton Biology/Institute of Cotton Research of Chinese Academy of Agricultural Sciences, Anyang, Henan, China.
[Ti] Título:GhSOS1, a plasma membrane Na+/H+ antiporter gene from upland cotton, enhances salt tolerance in transgenic Arabidopsis thaliana.
[So] Source:PLoS One;12(7):e0181450, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Upland cotton (Gossypium hirsutum L.), an important source of natural fiber, can tolerate relatively high salinity and drought stresses. In the present study, a plasma membrane Na+/H+ antiporter gene, GhSOS1, was cloned from a salt-tolerant genotype of G. hirsutum, Zhong 9807. The expression level of GhSOS1 in cotton roots was significantly upregulated in the presence of high concentrations of NaCl (200 mM), while its transcript abundance was increased when exposed to low temperature and drought stresses. Localization analysis using onion epidermal cells showed that the GhSOS1 protein was localized to the plasma membrane. The overexpression of GhSOS1 in Arabidopsis enhanced tolerance to salt stress, as indicated by a lower MDA content and decreased Na+/K+ ratio in transgenic plants. Moreover, the transcript levels of stress-related genes were significantly higher in GhSOS1 overexpression lines than in wild-type plants under salt treatment. Hence, GhSOS1 may be a potential target gene for enhancing salt tolerance in transgenic plants.
[Mh] Termos MeSH primário: Arabidopsis/genética
Gossypium/genética
Tolerância a Sal/genética
Plantas Tolerantes a Sal/genética
Trocadores de Sódio-Hidrogênio/genética
Estresse Fisiológico/genética
[Mh] Termos MeSH secundário: Secas
Regulação da Expressão Gênica de Plantas
Plantas Geneticamente Modificadas
Salinidade
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Sodium-Hydrogen Exchangers)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170721
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181450



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