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Pesquisa : D12.776.157.530.450.162.775.500 [Categoria DeCS]
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[PMID]:27771174
[Au] Autor:Takakuwa S; Mizuno N; Takano T; Asakawa S; Sato T; Hiratsuka M; Hirasawa N
[Ad] Endereço:Laboratory of Pharmacotherapy of Lifestyle Related Diseases, Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Miyagi 980-8578, Japan.
[Ti] Título:Down-regulation of Na /H exchanger 1 by Toll-like receptor stimulation in macrophages.
[So] Source:Immunobiology;222(2):176-182, 2017 02.
[Is] ISSN:1878-3279
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The role of Na /H exchanger 1 (NHE1) in various cell types, including inflammatory cells, has been extensively studied. However, regulation of NHE1 protein level in activated inflammatory cells is yet to be characterized. In this study, we investigated whether Toll-like receptor (TLR) ligands can regulate NHE1 protein level in the mouse macrophage-like RAW 264 cell line. We found that lipopolysaccharide (LPS), a TLR4 ligand, lowered NHE1 level and activity in RAW 264 cells and in primary murine macrophages. Other TLR ligands, such as zymosan A and poly(I:C), also displayed reduced NHE1 level. LPS promoted NHE1 ubiquitination and reduced the expression of calcineurin homologous protein 1 (CHP1), a regulator of NHE1 activity and stability. These responses were inhibited by c-Jun N-terminal kinase (JNK) inhibitor SP600125 and dexamethasone. A proteasome inhibitor, but not caspase-3 or lysosomal inhibitors, blocked the LPS-induced NHE1 down-regulation. These results suggested that LPS promotes the degranulation of NHE1 mediated by the ubiquitin-proteasome system and CHP1 downregulation resulting from activation of JNK.
[Mh] Termos MeSH primário: Macrófagos/metabolismo
Trocador 1 de Sódio-Hidrogênio/metabolismo
Receptores Toll-Like/agonistas
[Mh] Termos MeSH secundário: Animais
Biomarcadores
Linhagem Celular
Regulação para Baixo
Regulação da Expressão Gênica
Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo
Lipopolissacarídeos/imunologia
Macrófagos/imunologia
Masculino
Camundongos
Trocador 1 de Sódio-Hidrogênio/genética
Receptores Toll-Like/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Lipopolysaccharides); 0 (Sodium-Hydrogen Exchanger 1); 0 (Toll-Like Receptors); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180125
[Lr] Data última revisão:
180125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  2 / 463 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]:28704808
[Au] Autor:Singh Y; Zhou Y; Zhang S; Abdelazeem KNM; Elvira B; Salker MS; Lang F
[Ad] Endereço:Department of Internal Medicine III, Tuebingen University, Tuebingen, Germany.
[Ti] Título:Enhanced Reactive Oxygen Species Production, Acidic Cytosolic pH and Upregulated Na+/H+ Exchanger (NHE) in Dicer Deficient CD4+ T Cells.
[So] Source:Cell Physiol Biochem;42(4):1377-1389, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: MicroRNAs (miRNAs) negatively regulate gene expression at a post-transcriptional level. Dicer, a cytoplasmic RNase III enzyme, is required for the maturation of miRNAs from precursor miRNAs. Dicer, therefore, is a critical enzyme involved in the biogenesis and processing of miRNAs. Several biological processes are controlled by miRNAs, including the regulation of T cell development and function. T cells generate reactive oxygen species (ROS) with parallel H+ extrusion accomplished by the Na+/H+-exchanger 1 (NHE1). The present study explored whether ROS production, as well as NHE1 expression and function are sensitive to the lack of Dicer (miRNAs deficient) and could be modified by individual miRNAs. METHODS: CD4+ T cells were isolated from CD4 specific Dicer deficient (DicerΔ/Δ) mice and the respective control mice (Dicerfl/fl). Transcript and protein levels were quantified with RT-PCR and Western blotting, respectively. For determination of intracellular pH (pHi) cells were incubated with the pH sensitive dye bis-(2-carboxyethyl)-5-(and-6)-carboxyfluorescein (BCECF) and Na+/H+ exchanger (NHE) activity was calculated from re-alkalinization after an ammonium pulse. Changes in cell volume were measured using the forward scatter in flow cytometry, and ROS production utilizing 2',7' -dichlorofluorescin diacetate (DCFDA) fluorescence. Transfection of miRNA-control and mimics in T cells was performed using DharmaFECT3 reagent. RESULTS: ROS production, cytosolic H+ concentration, NHE1 transcript and protein levels, NHE activity, and cell volume were all significantly higher in CD4+ T cells from DicerΔ/Δ mice than in CD4+ T cells from Dicerfl/fl mice. Furthermore, individual miR-200b and miR-15b modify pHi and NHE activity in Dicerfl/fl and DicerΔ/Δ CD4+ T cells, respectively. CONCLUSIONS: Lack of Dicer leads to oxidative stress, cytosolic acidification, upregulated NHE1 expression and activity as well as swelling of CD4+ T cells, functions all reversed by miR-15b or miR-200b.
[Mh] Termos MeSH primário: Linfócitos T CD4-Positivos/metabolismo
Proteínas de Transporte de Cátions/genética
RNA Helicases DEAD-box/deficiência
MicroRNAs/genética
Espécies Reativas de Oxigênio/metabolismo
Ribonuclease III/deficiência
Trocadores de Sódio-Hidrogênio/genética
[Mh] Termos MeSH secundário: Animais
Linfócitos T CD4-Positivos/imunologia
Proteínas de Transporte de Cátions/imunologia
Citosol/imunologia
Citosol/metabolismo
RNA Helicases DEAD-box/genética
RNA Helicases DEAD-box/imunologia
Regulação da Expressão Gênica
Concentração de Íons de Hidrogênio
Transporte de Íons/imunologia
Camundongos
Camundongos Knockout
MicroRNAs/imunologia
Espécies Reativas de Oxigênio/imunologia
Ribonuclease III/genética
Ribonuclease III/imunologia
Transdução de Sinais
Trocador 1 de Sódio-Hidrogênio
Trocadores de Sódio-Hidrogênio/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cation Transport Proteins); 0 (MicroRNAs); 0 (Mirn15 microRNA, mouse); 0 (Mirn200 microRNA, mouse); 0 (Reactive Oxygen Species); 0 (Slc9a1 protein, mouse); 0 (Sodium-Hydrogen Exchanger 1); 0 (Sodium-Hydrogen Exchangers); EC 3.1.26.3 (Dicer1 protein, mouse); EC 3.1.26.3 (Ribonuclease III); EC 3.6.4.13 (DEAD-box RNA Helicases)
[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:170714
[St] Status:MEDLINE
[do] DOI:10.1159/000479201


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[PMID]:28648038
[Au] Autor:Li WP; Zhao GY; Yang XK
[Ad] Endereço:Student Brigade, the Fourth Military Medical University, Xi'an 710032, China.
[Ti] Título:[Effects of Na(+) /H(+) exchanger 1 inhibitor on intestinal injury of rats with burn sepsis and the mechanism].
[So] Source:Zhonghua Shao Shang Za Zhi;33(6):349-354, 2017 Jun 20.
[Is] ISSN:1009-2587
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:To observe the effects of Na(+) /H(+) exchanger 1 (NHE1) inhibitor on intestinal injury of rats with burn sepsis, and to explore the possible mechanism preliminarily. Ninety SD rats were divided into control group, pure sepsis group, and NHE1 inhibitor group according to the random number table, with 30 rats in each group. Full-thickness scald (hereinafter referred to as burn) model with 20% total body surface area were reproduced on the back of rats in pure sepsis and NHE1 inhibitor groups, and then 50 µL liquid of ATCC 27853 (2×10(5) colony forming unit/mL) were injected into the center of wounds on the back. Rats in NHE1 inhibitor group were intraperitoneally injected with 0.1 mmol/L NHE1 inhibitor cariporide (0.4 mg/kg) rapidly after the successful establishment of burn sepsis model, while rats in pure sepsis group were injected with the same volume of normal saline. Except for not being made burn wounds nor receiving bacterination, rats in control group were treated the same as those in pure sepsis group. Rats with burn sepsis in each group were laparotomized and injected with 200 mL fluorescein isothiocyanate (FITC)-dextran in the concentration of 0.1 mol/L in terminal ileum at 12 hours post injury, and their left ventricular blood and terminal ileum were collected 30 minutes later. The serum content of FITC-dextran was detected with fluorescence spectrophotometer ( =10); the morphology of intestinal tissue was observed with HE staining ( =10); the content of interleukin-6 (IL-6) and tumor necrosis factor-alpha (TNF-α) in serum and intestinal tissue was determined with enzyme-linked immunosorbent assay ( =20); the activity of myeloperoxidase (MPO) in serum and intestinal tissue was detected with colorimetric method ( =20); the protein expression of nuclear factor-kappa B-p65 (NF-κB-p65) and phosphorylation levels of mitogen-activated protein kinase (MAPK) signal pathway related proteins p38MAPK, extracellular signal-regulated kinase 1/2 (ERK1/2), and c-Jun N-terminal kinase 1/2 (JNK1/2) were determined by Western blotting ( =4). The same samples of rats in control group were collected for related detection at the same time point as above. Data were processed with one-way analysis of variance and SNK test. (1) The serum content of FITC-dextran of rats in pure sepsis group was significantly higher than that in control group ( <0.01), while the serum content of FITC-dextran of rats in NHE1 inhibitor group was significantly lower than that in pure sepsis group ( <0.01). Compared with that in control group, infiltration of a large number of inflammatory cells, ulcer and necrosis of intestinal mucosa of rats in pure sepsis group were observed. The injury condition of intestine of rats in NHE1 inhibitor group was better than that in pure sepsis group. (2) The serum content of IL-6, TNF-α, and MPO of rats in pure sepsis group was (387±42) and (164.7±10.1) ng/mL, and (7.5±1.5) U/mL, respectively, significantly higher than that in control group [(75±17) and (13.1±6.5) ng/mL, and (2.3±0.7) U/mL, respectively, with values below 0.01]. The serum content of IL-6, TNF-α, and MPO of rats in NHE1 inhibitor group was (176±37) and (64.9±9.3) ng/mL, and (5.9±0.8) U/mL, respectively, which was significantly lower than that in pure sepsis group (with values below 0.01). (3) The content of IL-6, TNF-α, and MPO in intestinal tissue of rats in pure sepsis group was (190±13) and (172.8±29.7) ng/mL, and (8.7±1.5) U/mL, respectively, significantly higher than that in control group [respectively (20±3) and (11.9±2.3) ng/mL, and (2.9±0.3) U/mL, with values below 0.01]. The content of IL-6, TNF-α, and MPO of intestinal tissue of rats in NHE1 inhibitor group was (35±6) and (45.2±6.1) ng/mL, and (5.3±0.6) U/mL, respectively, significantly lower than that in pure sepsis group (with values below 0.01). (4) The protein expression of NF-κB-p65 and phosphorylation levels of p38MAPK and ERK1/2 in intestinal tissue of rats in pure sepsis group were significantly higher than those in control group (with values below 0.01); the protein expression of NF-κB-p65 and the phosphorylation level of p38MAPK in intestinal tissue of rats in NHE1 inhibitor group were significantly lower than those in pure sepsis group (with values below 0.01); phosphorylation levels of JNK1/2 in intestinal tissue of rats in the three groups were similar (with values above 0.05). The inhibition of NHE1 can significantly alleviate the intestinal injury, and the mechanisms may be attributed to the regulation of NF-κB and p38MAPK signal pathway, resulting in inhibition of the inflammatory response of intestinal tract.
[Mh] Termos MeSH primário: Antiarrítmicos/farmacologia
Queimaduras/tratamento farmacológico
Guanidinas/farmacologia
Intestinos/efeitos dos fármacos
Intestinos/lesões
Sepse
Trocadores de Sódio-Hidrogênio/antagonistas & inibidores
Sulfonas/farmacologia
[Mh] Termos MeSH secundário: Animais
Western Blotting
Queimaduras/complicações
Queimaduras/metabolismo
Dextranos/sangue
Ensaio de Imunoadsorção Enzimática
Fluoresceína-5-Isotiocianato/análogos & derivados
Interleucina-6/sangue
Camundongos
NF-kappa B/sangue
NF-kappa B/metabolismo
Ratos
Ratos Sprague-Dawley
Transdução de Sinais
Trocador 1 de Sódio-Hidrogênio
Trocadores de Sódio-Hidrogênio/fisiologia
Lesões dos Tecidos Moles
Fator de Transcrição RelA
Fator de Necrose Tumoral alfa/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Arrhythmia Agents); 0 (Dextrans); 0 (Guanidines); 0 (IL6 protein, human); 0 (Interleukin-6); 0 (NF-kappa B); 0 (RELA protein, human); 0 (Slc9a1 protein, rat); 0 (Sodium-Hydrogen Exchanger 1); 0 (Sodium-Hydrogen Exchangers); 0 (Sulfones); 0 (Transcription Factor RelA); 0 (Tumor Necrosis Factor-alpha); 0 (fluorescein isothiocyanate dextran); 7E3392891K (cariporide); I223NX31W9 (Fluorescein-5-isothiocyanate)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170627
[St] Status:MEDLINE
[do] DOI:10.3760/cma.j.issn.1009-2587.2017.06.013


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[PMID]:28371597
[Au] Autor:Kobliakov VA
[Ad] Endereço:Blokhin Russian Cancer Research Center, Russian Ministry of Health, Moscow, 115478, Russia. kobliakov@rambler.ru.
[Ti] Título:Role of Proton Pumps in Tumorigenesis.
[So] Source:Biochemistry (Mosc);82(4):401-412, 2017 Apr.
[Is] ISSN:1608-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:One of the differences between normal and cancer cells is lower pH of the extracellular space in tumors. Low pH in the extracellular space activates proteases and stimulates tumor invasion and metastasis. Tumor cells display higher level of the HIF1α transcription factor that promotes cell switch from mitochondrial respiration to glycolysis. The terminal product of glycolysis is lactate. Lactate formation from pyruvate is catalyzed by the specific HIF1α-dependent isoform of lactate dehydrogenase A. Because lactate accumulation is deleterious for the cell, it is actively exported by monocarboxylate transporters. Lactate is cotransported with proton, which acidifies the extracellular space. Another protein that contributes to proton concentration increase in the extracellular space is tumor-specific HIF1α-dependent carbonic anhydrase IX, which generates a proton in the reaction between carbon dioxide and water. The activity of Na+/H+ exchanger (another protein pump) is stimulated by stress factors (e.g. osmotic shock) and proliferation stimuli. This review describes the mechanisms of proton pump activation and reviews results of studies on effects of various proton pump inhibitors on tumor functioning and growth in cell culture and in vivo. The prospects of combined application of proton pump inhibitors and cytostatics in cancer therapy are discussed.
[Mh] Termos MeSH primário: Carcinogênese
Bombas de Próton/fisiologia
[Mh] Termos MeSH secundário: Ácidos/metabolismo
Catálise
Proteínas de Transporte de Cátions/metabolismo
Seres Humanos
Concentração de Íons de Hidrogênio
Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo
L-Lactato Desidrogenase/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Trocador 1 de Sódio-Hidrogênio
Trocadores de Sódio-Hidrogênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Acids); 0 (Cation Transport Proteins); 0 (HIF1A protein, human); 0 (Hypoxia-Inducible Factor 1, alpha Subunit); 0 (Proton Pumps); 0 (SLC9A1 protein, human); 0 (Sodium-Hydrogen Exchanger 1); 0 (Sodium-Hydrogen Exchangers); EC 1.1.1.27 (L-Lactate Dehydrogenase); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.2 (pyruvate dehydrogenase (acetyl-transferring) kinase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1134/S0006297917040010


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[PMID]:28268168
[Au] Autor:Kaminota T; Yano H; Shiota K; Nomura N; Yaguchi H; Kirino Y; Ohara K; Tetsumura I; Sanada T; Ugumori T; Tanaka J; Hato N
[Ad] Endereço:Department of Otorhinolaryngology, Head and Neck Surgery, Ehime University Medical School, 454, Shitsukawa, To-on, Ehime, 791-0295, Japan. Electronic address: kaminota28@gmail.com.
[Ti] Título:Elevated Na /H exchanger-1 expression enhances the metastatic collective migration of head and neck squamous cell carcinoma cells.
[So] Source:Biochem Biophys Res Commun;486(1):101-107, 2017 Apr 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cancer cells can migrate as collectives during invasion and/or metastasis; however, the precise molecular mechanisms of this form of migration are less clear compared with single cell migration following epithelial-mesenchymal transition. Elevated Na /H exchanger1 (NHE1) expression has been suggested to have malignant roles in a number of cancer cell lines and in vivo tumor models. Furthermore, a metastatic human head and neck squamous cell carcinoma (HNSCC) cell line (SASL1m) that was isolated based on its increased metastatic potential also exhibited higher NHE1 expression than its parental line SAS. Time-lapse video recordings indicated that both cell lines migrate as collectives, although with different features, e.g., SASL1m was much more active and changed the direction of migration more frequently than SAS cells, whereas locomotive activities were comparable. SASL1m cells also exhibited higher invasive activity than SAS in Matrigel invasion assays. shRNA-mediated NHE1 knockdown in SASL1m led to reduced locomotive and invasive activities, suggesting a critical role for NHE1 in the collective migration of SASL1m cells. SASL1m cells also exhibited a higher metastatic rate than SAS cells in a mouse lymph node metastasis model, while NHE1 knockdown suppressed in vivo SASL1m metastasis. Finally, elevated NHE1 expression was observed in human HNSCC tissue, and Cariporide, a specific NHE1 inhibitor, reduced the invasive activity of SASL1m cells, implying NHE1 could be a target for anti-invasion/metastasis therapy.
[Mh] Termos MeSH primário: Carcinoma de Células Escamosas/metabolismo
Proteínas de Transporte de Cátions/metabolismo
Movimento Celular
Neoplasias de Cabeça e Pescoço/metabolismo
Trocadores de Sódio-Hidrogênio/metabolismo
[Mh] Termos MeSH secundário: Animais
Carcinoma de Células Escamosas/genética
Carcinoma de Células Escamosas/patologia
Proteínas de Transporte de Cátions/genética
Linhagem Celular Tumoral
Células HEK293
Neoplasias de Cabeça e Pescoço/genética
Neoplasias de Cabeça e Pescoço/patologia
Seres Humanos
Immunoblotting
Imuno-Histoquímica
Metástase Linfática
Masculino
Camundongos Nus
Microscopia de Fluorescência
Invasividade Neoplásica
Interferência de RNA
Trocador 1 de Sódio-Hidrogênio
Trocadores de Sódio-Hidrogênio/genética
Imagem com Lapso de Tempo/métodos
Transplante Heterólogo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cation Transport Proteins); 0 (SLC9A1 protein, human); 0 (Sodium-Hydrogen Exchanger 1); 0 (Sodium-Hydrogen Exchangers)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170308
[St] Status:MEDLINE


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[PMID]:28222424
[Au] Autor:Zeng N; Zhou Y; Zhang S; Singh Y; Shi B; Salker MS; Lang F
[Ti] Título:1α,25(OH) 2D3 Sensitive Cytosolic pH Regulation and Glycolytic Flux in Human Endometrial Ishikawa Cells.
[So] Source:Cell Physiol Biochem;41(2):678-688, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: Tumor cell proliferation is modified by 1,25-Dihydroxy-Vitamin D3 (1,25(OH)2D3), a steroid hormone predominantly known for its role in calcium and phosphorus metabolism. Key properties of tumor cells include enhanced glycolytic flux with excessive consumption of glucose and formation of lactate. As glycolysis is highly sensitive to cytosolic pH, maintenance of glycolysis requires export of H+ ions and lactate, which is in part accomplished by Na+/H+ exchangers, such as NHE1 and monocarboxylate transporters, such as MCT4. An effect of 1,25(OH)2D3 on those transport processes has, however, never been reported. As cytosolic pH impacts on apoptosis, the study further explored the effect of 1,25(OH)2D3 on apoptosis and on the apoptosis regulating kinase AKT, transcription factor Forkhead box O-3 (FOXO3A) and B-cell lymphoma protein BCL-2. METHODS: In human endometrial adenocarcinoma (Ishikawa) cells, cytosolic pH (pHi) was determined utilizing (2',7'-bis-(2-carboxyethyl)-5-(and-6)-carboxyfluorescein [BCECF] fluorescence, Na+/H+ exchanger activity from Na+ dependent realkalinization after an ammonium pulse, NHE1 and MCT4 transcript levels using qRT-PCR, NHE1, MCT4, total & phospho AKT, total & phospho-FOXO3A and BCL-2 protein abundance by Western blotting, lactate concentration in the supernatant utilizing a colorimetric enzyme assay and cell death quantification using CytoTox 96®, Annexin V and Propidium Iodide staining. RESULTS: A 24 hours treatment with 1,25(OH)2D3 (100 nM) significantly increased cytosolic pH (pHi), significantly decreased Na+/H+ exchanger activity, NHE1 and MCT4 transcript levels as well as protein abundance and significantly increased lactate concentration in the supernatant. Treatment of Ishikawa cells with 1,25(OH)2D3 (100 nM) further triggered apoptosis, an effect paralleled by decreased phosphorylation of AKT and FOXO3A as well as decreased abundance of BCL-2. CONCLUSIONS: In Ishikawa cells 1,25(OH)2D3 is a powerful stimulator of glycolysis, an effect presumably due to cytosolic alkalinization. Despite stimulation of glycolysis, 1,25(OH)2D3 stimulates slightly but significantly suicidal cell death, an effect presumably in part due to decreased activation of AKT with decreased inhibition of pro-apoptotic transcription factor FOXO3A and downregulation of the anti-apoptotic protein BCL-2.
[Mh] Termos MeSH primário: Citosol/metabolismo
Glicólise/efeitos dos fármacos
Vitamina D/análogos & derivados
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Proteínas de Transporte de Cátions/genética
Proteínas de Transporte de Cátions/metabolismo
Linhagem Celular Tumoral
Proteína Forkhead Box O3/metabolismo
Seres Humanos
Concentração de Íons de Hidrogênio
Ácido Láctico/análise
Transportadores de Ácidos Monocarboxílicos/genética
Transportadores de Ácidos Monocarboxílicos/metabolismo
Proteínas Musculares/genética
Proteínas Musculares/metabolismo
Fosforilação/efeitos dos fármacos
Proteínas Proto-Oncogênicas c-akt/metabolismo
Proteínas Proto-Oncogênicas c-bcl-2/metabolismo
Trocador 1 de Sódio-Hidrogênio
Trocadores de Sódio-Hidrogênio/genética
Trocadores de Sódio-Hidrogênio/metabolismo
Vitamina D/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cation Transport Proteins); 0 (FOXO3 protein, human); 0 (Forkhead Box Protein O3); 0 (Monocarboxylic Acid Transporters); 0 (Muscle Proteins); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (SLC16A4 protein, human); 0 (SLC9A1 protein, human); 0 (Sodium-Hydrogen Exchanger 1); 0 (Sodium-Hydrogen Exchangers); 0 (dihydroxy-vitamin D3); 1406-16-2 (Vitamin D); 33X04XA5AT (Lactic Acid); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170222
[St] Status:MEDLINE
[do] DOI:10.1159/000458427


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[PMID]:28098891
[Au] Autor:Xie R; Wang H; Jin H; Wen G; Tuo B; Xu J
[Ad] Endereço:Department of Gastroenterology, Affiliated Hospital, Zunyi Medical College, Zunyi, Guizhou 563003, P.R. China.
[Ti] Título:NHE1 is upregulated in gastric cancer and regulates gastric cancer cell proliferation, migration and invasion.
[So] Source:Oncol Rep;37(3):1451-1460, 2017 Mar.
[Is] ISSN:1791-2431
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Na+/H+ exchanger isoform 1 (NHE1) is known to play a key role in regulating intracellular pH and osmotic homeostasis and is involved in the development and progression of several types of cancer. However, the function and specific mechanism of NHE1 in gastric cancer (GC) are not clearly understood. In the present study, we report that NHE1 is overexpressed in tissues and cell lines from GC patients, and knockdown or inhibition of NHE1 suppressed GC cell proliferation via regulation of G1/S and G2/M cell cycle phase transitions, concomitant with a marked decrease in positive cell cycle regulators, including cyclin D1 and cyclin B1. Likewise, NHE1 was required for GC cell migration and invasion through the regulation of epithelial-mesenchymal transition (EMT) proteins, and NHE1 inhibition resulted in an acidic intracellular environment, providing possible mechanisms underlying NHE1-mediated GC progression both in vitro and in vivo. These data highlight the important role of NHE1 in GC progression and suggest that NHE1 may be a useful target for GC therapy.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/metabolismo
Proteínas de Transporte de Cátions/metabolismo
Movimento Celular
Proliferação Celular
Ciclina D1/metabolismo
Transição Epitelial-Mesenquimal
Trocadores de Sódio-Hidrogênio/metabolismo
Neoplasias Gástricas/patologia
[Mh] Termos MeSH secundário: Animais
Apoptose
Biomarcadores Tumorais/genética
Western Blotting
Proteínas de Transporte de Cátions/genética
Ciclina D1/genética
Imunofluorescência
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Técnicas Imunoenzimáticas
Masculino
Camundongos
Camundongos Nus
Invasividade Neoplásica
Estadiamento de Neoplasias
Prognóstico
RNA Mensageiro/genética
Reação em Cadeia da Polimerase em Tempo Real
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Trocador 1 de Sódio-Hidrogênio
Trocadores de Sódio-Hidrogênio/genética
Neoplasias Gástricas/genética
Neoplasias Gástricas/metabolismo
Células Tumorais Cultivadas
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (CCND1 protein, human); 0 (Cation Transport Proteins); 0 (RNA, Messenger); 0 (SLC9A1 protein, human); 0 (Sodium-Hydrogen Exchanger 1); 0 (Sodium-Hydrogen Exchangers); 136601-57-5 (Cyclin D1)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170119
[St] Status:MEDLINE
[do] DOI:10.3892/or.2017.5386


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[PMID]:28031107
[Au] Autor:Mo X; Wang L; Guo J; Hong W; Long S; Zhang L; Xiang N; Yang J
[Ad] Endereço:Comprehensive Ward, Affiliated Hospital of Guizhou Medical University, Guiyang 550004, China. *Corresponding author, E-mail:moxiangang123@126.com.
[Ti] Título:[Overexpression of NHE1 suppresses ABCA1 protein expression via increasing calpain activity in RAW264.7 cells].
[So] Source:Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi;33(1):12-16, 2017 Jan.
[Is] ISSN:1007-8738
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:Objective To investigate the effect of over-expressed Na /H exchanger 1 (NHE1) on the protein expression of adenosine three phosphate binding cassette transporter A1 (ABCA1) in RAW264.7 cells. Methods RAW264.7 cells were infected with the adenoviral vector encoding NHE1-EGFP (AdNHE1). The infected RAW264.7 cells were subjected to Western blot analysis for NHE1-EGFP fusion protein. The subcellular localization of NHE1-EGFP fusion protein was observed by confocal laser scanning microscopy. NHE1 activity was measured by the method of pH recovery in response to an acute acid pulse. Furthermore, Western blotting was performed to determine ABCA1 protein levels and calpain activity in NHE1-overexpressing RAW264.7 cells. The effect of calpain inhibitor N-acetyl-L-leucyl-L-leucyl-L-norleucinal (ALLN) on ABCA1 protein levels in the presence of TO-901317 was examined by Western blotting. Results NHE1-EGFP fusion protein was highly expressed and localized in cytoplasm and cell membrane of RAW264.7 cells infected with AdNHE1. NHE1-EGFP fusion protein reduced ABCA1 protein expression and increased calpain activity. The calpain inhibitor ALLN blocked the decrease of ABCA1 protein expression. Conclusion Overexpressed NHE1 suppresses the expression of ABCA1 protein via increasing the calpain activity in RAW264.7 cells.
[Mh] Termos MeSH primário: Transportador 1 de Cassete de Ligação de ATP/metabolismo
Calpaína/metabolismo
Proteínas de Transporte de Cátions/metabolismo
Trocadores de Sódio-Hidrogênio/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Camundongos
Trocador 1 de Sódio-Hidrogênio
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABCA1 protein, mouse); 0 (ATP Binding Cassette Transporter 1); 0 (Cation Transport Proteins); 0 (Slc9a1 protein, mouse); 0 (Sodium-Hydrogen Exchanger 1); 0 (Sodium-Hydrogen Exchangers); EC 3.4.22.- (Calpain)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161230
[St] Status:MEDLINE


  10 / 463 MEDLINE  
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[PMID]:28019659
[Au] Autor:Paehler Vor der Nolte A; Chodisetti G; Yuan Z; Busch F; Riederer B; Luo M; Yu Y; Menon MB; Schneider A; Stripecke R; Nikolovska K; Yeruva S; Seidler U
[Ad] Endereço:Departments of Gastroenterology, Hemostatsis, Oncology and Stem Cell Transplantation, Medical School of Hannover, Germany.
[Ti] Título:Na /H exchanger NHE1 and NHE2 have opposite effects on migration velocity in rat gastric surface cells.
[So] Source:J Cell Physiol;232(7):1669-1680, 2017 Jul.
[Is] ISSN:1097-4652
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Following superficial injury, neighbouring gastric epithelial cells close the wound by rapid cell migration, a process called epithelial restitution. Na /H exchange (NHE) inhibitors interfere with restitution, but the role of the different NHE isoforms expressed in gastric pit cells has remained elusive. The role of the basolaterally expressed NHE1 (Slc9a1) and the presumably apically expressed NHE2 (Slc9a2) in epithelial restitution was investigated in the nontransformed rat gastric surface cell line RGM1. Migration velocity was assessed by loading the cells with the fluorescent dye DiR and following closure of an experimental wound over time. Since RGM1 cells expressed very low NHE2 mRNA and have low transport activity, NHE2 was introduced by lentiviral gene transfer. In medium with pH 7.4, RGM1 cells displayed slow wound healing even in the absence of growth factors and independently of NHE activity. Growth factors accelerated wound healing in a partly NHE1-dependent fashion. Preincubation with acidic pH 7.1 stimulated restitution in a NHE1-dependent fashion. When pH 7.1 was maintained during the restitution period, migratory speed was reduced to ∼10% of the speed at pH 7,4, and the residual restitution was further inhibited by NHE1 inhibition. Lentiviral NHE2 expression increased the steady-state pH and reduced the restitution velocity after low pH preincubation, which was reversible by pharmacological NHE2 inhibition. The results demonstrate that in RGM1 cells, migratory velocity is increased by NHE1 activation, while NHE2 activity inhibit this process. A differential activation of NHE1 and NHE2 may therefore, play a role in the initiation and completion of the epithelial restitution process.
[Mh] Termos MeSH primário: Movimento Celular
Mucosa Gástrica/citologia
Trocadores de Sódio-Hidrogênio/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Proteínas de Fluorescência Verde/metabolismo
Células HEK293
Seres Humanos
Concentração de Íons de Hidrogênio
Lentivirus/metabolismo
Transporte Proteico
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Ratos
Trocador 1 de Sódio-Hidrogênio
Trocadores de Sódio-Hidrogênio/genética
Cicatrização
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (Slc9a1 protein, rat); 0 (Slc9a2 protein, rat); 0 (Sodium-Hydrogen Exchanger 1); 0 (Sodium-Hydrogen Exchangers); 147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161227
[St] Status:MEDLINE
[do] DOI:10.1002/jcp.25758



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