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Pesquisa : D12.776.157.530.400.875.200 [Categoria DeCS]
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  1 / 2306 MEDLINE  
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[PMID]:29179210
[Au] Autor:Ding Y; Zhao R; Zhao X; Matthay MA; Nie HG; Ji HL
[Ad] Endereço:Institute of Metabolic Disease Research and Drug Development, China Medical University, Shenyang, China.
[Ti] Título:ENaCs as Both Effectors and Regulators of MiRNAs in Lung Epithelial Development and Regeneration.
[So] Source:Cell Physiol Biochem;44(3):1120-1132, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Epithelial sodium channels (ENaC) play an important role in re-absorbing excessive luminal fluid by building up an osmotic Na+ gradient across the tight epithelium in the airway, the lung, the kidney, and the colon. The ENaC is a major pathway for retention of salt in kidney too. MicroRNAs (miRs), a group of non-coding RNAs that regulate gene expression at the post-transcriptional level, have emerged as a novel class of regulators for ENaC. Given the ENaC pathway is crucial for maintaining fluid homeostasis in the lung and the kidney and other cavities, we summarized the cross-talk between ENaC and miRs and recapitulated the underlying regulatory factors, including aldosterone, transforming growth factor-ß1, and vascular endothelial growth factor-A in the lung and other epithelial tissues/organs. We have compared the profiling of miRs between normal and injured mice and human lungs, which showed a significant alteration in numerous miRs in mouse models of LPS and ventilator induced ARDS. In addition, we reiterated the potential regulation of the ENaC by miRs in stem/ progenitor cell-based re-epithelialization, and identified a promising pharmaceutic target of ENaC for removing edema fluid in ARDS by mesenchymal stem cells-released paracrine. In conclusion, it seems that the interactions between miRs and scnn1s/ENaCs are critical for lung development, epithelial cell turnover in adult lungs, and re-epithelialization for repair.
[Mh] Termos MeSH primário: Canais Epiteliais de Sódio/metabolismo
Epitélio/fisiologia
Pulmão/fisiologia
MicroRNAs/metabolismo
[Mh] Termos MeSH secundário: Animais
Epitélio/crescimento & desenvolvimento
Seres Humanos
Regeneração
Células-Tronco/citologia
Células-Tronco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Epithelial Sodium Channels); 0 (MicroRNAs)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180203
[Lr] Data última revisão:
180203
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1159/000485417


  2 / 2306 MEDLINE  
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[PMID]:28468944
[Au] Autor:Montgomery DS; Yu L; Ghazi ZM; Thai TL; Al-Khalili O; Ma HP; Eaton DC; Alli AA
[Ad] Endereço:Department of Physiology and Functional Genomics and Department of Medicine Division of Nephrology, Hypertension, and Renal Transplantation, University of Florida College of Medicine, Gainesville, Florida.
[Ti] Título:ENaC activity is regulated by calpain-2 proteolysis of MARCKS proteins.
[So] Source:Am J Physiol Cell Physiol;313(1):C42-C53, 2017 Jul 01.
[Is] ISSN:1522-1563
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We previously demonstrated a role for the myristoylated alanine-rich C kinase substrate (MARCKS) to serve as an adaptor protein in the anionic phospholipid phosphate-dependent regulation of the epithelial sodium channel (ENaC). Both MARCKS and ENaC are regulated by proteolysis. Calpains are a family of ubiquitously expressed intracellular Ca -dependent cysteine proteases involved in signal transduction. Here we examine the role of calpain-2 in regulating MARCKS and ENaC in cultured renal epithelial cells and in the mouse kidney. Using recombinant fusion proteins, we show that MARCKS, but not the ENaC subunits, are a substrate of calpain-2 in the presence of Ca Pharmacological inhibition of calpain-2 alters MARCKS protein expression in light-density sucrose gradient fractions from cell lysates of mouse cortical collecting duct cells. Calpain-dependent cleaved products of MARCKS are detectable in cultured renal cells. Ca mobilization and calpain-2 inhibition decrease the association between ENaC and MARCKS. The inhibition of calpain-2 reduces ENaC activity as demonstrated by single-channel patch-clamp recordings and transepithelial current measurements. These results suggest that calpain-2 proteolysis of MARCKS promotes its interaction with lipids and ENaC at the plasma membrane to allow for the phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent regulation of ENaC activity in the kidney.
[Mh] Termos MeSH primário: Calpaína/genética
Canais Epiteliais de Sódio/genética
Peptídeos e Proteínas de Sinalização Intracelular/genética
Proteínas de Membrana/genética
Fosfatidilinositol 4,5-Difosfato/metabolismo
[Mh] Termos MeSH secundário: Potenciais de Ação/efeitos dos fármacos
Amilorida/farmacologia
Animais
Cálcio/metabolismo
Calpaína/metabolismo
Fracionamento Celular
Linhagem Celular
Membrana Celular/efeitos dos fármacos
Membrana Celular/metabolismo
Inibidores de Cisteína Proteinase/farmacologia
Citocalasina D/farmacologia
Células Epiteliais/citologia
Células Epiteliais/efeitos dos fármacos
Células Epiteliais/metabolismo
Canais Epiteliais de Sódio/metabolismo
Regulação da Expressão Gênica
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Túbulos Renais Coletores/citologia
Túbulos Renais Coletores/efeitos dos fármacos
Túbulos Renais Coletores/metabolismo
Proteínas de Membrana/metabolismo
Camundongos
Substrato Quinase C Rico em Alanina Miristoilada
Técnicas de Patch-Clamp
Proteólise/efeitos dos fármacos
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Transdução de Sinais
Xenopus laevis
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cysteine Proteinase Inhibitors); 0 (Epithelial Sodium Channels); 0 (Intracellular Signaling Peptides and Proteins); 0 (Marcks protein, mouse); 0 (Membrane Proteins); 0 (Phosphatidylinositol 4,5-Diphosphate); 0 (Recombinant Fusion Proteins); 125267-21-2 (Myristoylated Alanine-Rich C Kinase Substrate); 22144-77-0 (Cytochalasin D); 7DZO8EB0Z3 (Amiloride); EC 3.4.22.- (Calpain); EC 3.4.22.53 (Capn2 protein, mouse); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171212
[Lr] Data última revisão:
171212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1152/ajpcell.00244.2016


  3 / 2306 MEDLINE  
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[PMID]:28950003
[Au] Autor:Tarjus A; Maase M; Jeggle P; Martinez-Martinez E; Fassot C; Loufrani L; Henrion D; Hansen PBL; Kusche-Vihrog K; Jaisser F
[Ad] Endereço:Inserm U1138, Centre de Recherches des Cordeliers, Paris, France.
[Ti] Título:The endothelial αENaC contributes to vascular endothelial function in vivo.
[So] Source:PLoS One;12(9):e0185319, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Epithelial Sodium Channel (ENaC) is a key player in renal sodium homeostasis. The expression of α ß Î³ ENaC subunits has also been described in the endothelium and vascular smooth muscle, suggesting a role in vascular function. We recently demonstrated that endothelial ENaC is involved in aldosterone-modulated endothelial stiffness. Here we explore the functional role of the endothelial αENaC subunit in vascular function in vivo. Compared to littermates, mice with conditional αENaC subunit gene inactivation in the endothelium only (endo-αENaC Knock Out mice) had no difference in their physiological parameters such as systolic blood pressure or heart rate. Acute and long-term renal Na+ handlings were not affected, indicating that endothelial αENaC subunit is not involved in renal sodium balance. Pharmacological inhibition of ENaC with benzamil blunted acetylcholine-induced nitric oxide production in mesenteric arteries from wild type mice but not in endo-αENaC KO mice, suggesting a critical role of endothelial ENaC in agonist-induced nitric oxide production. In endo-αENaC KO mice, compensatory mechanisms occurred and steady state vascular function was not altered except for flow-mediated dilation. Our data suggest that endothelial αENaC contributes to vascular endothelial function in vivo.
[Mh] Termos MeSH primário: Endotélio Vascular/fisiologia
Canais Epiteliais de Sódio/fisiologia
[Mh] Termos MeSH secundário: Animais
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Epithelial Sodium Channels)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170927
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185319


  4 / 2306 MEDLINE  
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[PMID]:28768768
[Au] Autor:Shi S; Buck TM; Kinlough CL; Marciszyn AL; Hughey RP; Chalfie M; Brodsky JL; Kleyman TR
[Ad] Endereço:From the Renal-Electrolyte Division, Department of Medicine.
[Ti] Título:Regulation of the epithelial Na channel by paraoxonase-2.
[So] Source:J Biol Chem;292(38):15927-15938, 2017 Sep 22.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Paraoxonase-2 (PON-2) is a membrane-bound lactonase with unique anti-oxidative and anti-atherosclerotic properties. PON-2 shares key structural elements with MEC-6, an endoplasmic reticulum-resident molecular chaperone in MEC-6 modulates the expression of a mechanotransductive ion channel comprising MEC-4 and MEC-10 in touch-receptor neurons. Because mRNA resides in multiple rat nephron segments, including the aldosterone-sensitive distal nephron where the epithelial Na channel (ENaC) is expressed, we hypothesized that PON-2 would similarly regulate ENaC expression. We observed PON-2 expression in aquaporin 2-positive principal cells of the distal nephron of adult human kidney. PON-2 also co-immunoprecipitated with ENaC when co-expressed in HEK293 cells. When PON-2 was co-expressed with ENaC in oocytes, ENaC activity was reduced, reflecting a reduction in ENaC surface expression. MEC-6 also reduced ENaC activity when co-expressed in oocytes. The PON-2 inhibitory effect was ENaC-specific, as PON-2 had no effect on functional expression of the renal outer medullary potassium channel. PON-2 did not alter the response of ENaC to extracellular Na , mechanical shear stress, or α-chymotrypsin-mediated proteolysis, suggesting that PON-2 did not alter the regulation of ENaC by these factors. Together, our data suggest that PON-2 regulates ENaC activity by modulating its intracellular trafficking and surface expression.
[Mh] Termos MeSH primário: Arildialquilfosfatase/metabolismo
Canais Epiteliais de Sódio/metabolismo
[Mh] Termos MeSH secundário: Adulto
Animais
Proteínas de Caenorhabditis elegans/metabolismo
Sequência Conservada
Canais Epiteliais de Sódio/química
Evolução Molecular
Regulação da Expressão Gênica
Células HEK293
Seres Humanos
Túbulos Renais Distais/metabolismo
Camundongos
Oócitos/metabolismo
Subunidades Proteicas/metabolismo
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Epithelial Sodium Channels); 0 (Protein Subunits); EC 3.1.1.2 (MEC-6 protein, C elegans); EC 3.1.8.1 (Aryldialkylphosphatase); EC 3.1.8.1 (PON1 protein, human); EC 3.1.8.1 (PON2 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.785253


  5 / 2306 MEDLINE  
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[PMID]:28710092
[Au] Autor:Salih M; Gautschi I; van Bemmelen MX; Di Benedetto M; Brooks AS; Lugtenberg D; Schild L; Hoorn EJ
[Ad] Endereço:Departments of Internal Medicine and.
[Ti] Título:A Missense Mutation in the Extracellular Domain of ENaC Causes Liddle Syndrome.
[So] Source:J Am Soc Nephrol;28(11):3291-3299, 2017 Nov.
[Is] ISSN:1533-3450
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Liddle syndrome is an autosomal dominant form of hypokalemic hypertension due to mutations in the - or -subunit of the epithelial sodium channel (ENaC). Here, we describe a family with Liddle syndrome due to a mutation in ENaC. The proband was referred because of resistant hypokalemic hypertension, suppressed renin and aldosterone, and no mutations in the genes encoding - or ENaC. Exome sequencing revealed a heterozygous, nonconservative T>C single-nucleotide mutation in ENaC that substituted Cys479 with Arg (C479R). C479 is a highly conserved residue in the extracellular domain of ENaC and likely involved in a disulfide bridge with the partner cysteine C394. In oocytes, the C479R and C394S mutations resulted in similar twofold increases in amiloride-sensitive ENaC current. Quantification of mature cleaved ENaC in membrane fractions showed that the number of channels did not increase with these mutations. Trypsin, which increases open probability of the channel by proteolytic cleavage, resulted in significantly higher currents in the wild type than in C479R or C394S mutants. In summary, a mutation in the extracellular domain of ENaC causes Liddle syndrome by increasing intrinsic channel activity. This mechanism differs from that of the - and -mutations, which result in an increase in channel density at the cell surface. This mutation may explain other cases of patients with resistant hypertension and also provides novel insight into ENaC activation, which is relevant for kidney sodium reabsorption and salt-sensitive hypertension.
[Mh] Termos MeSH primário: Canais Epiteliais de Sódio/genética
Síndrome de Liddle/genética
Mutação de Sentido Incorreto
[Mh] Termos MeSH secundário: Seres Humanos
Linhagem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Epithelial Sodium Channels)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170716
[St] Status:MEDLINE
[do] DOI:10.1681/ASN.2016111163


  6 / 2306 MEDLINE  
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[PMID]:28678861
[Au] Autor:de Bragança AC; Moreau RLM; de Brito T; Shimizu MHM; Canale D; de Jesus DA; Silva AMG; Gois PH; Seguro AC; Magaldi AJ
[Ad] Endereço:Clinical Hospital, School of Medicine-Department of Nephrology- Basic Research Laboratory-LIM12, University of Sâo Paulo, SP, Brazil.
[Ti] Título:Ecstasy induces reactive oxygen species, kidney water absorption and rhabdomyolysis in normal rats. Effect of N-acetylcysteine and Allopurinol in oxidative stress and muscle fiber damage.
[So] Source:PLoS One;12(7):e0179199, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Ecstasy (Ec) use produces hyperthermia, excessive sweating, intense thirst, an inappropriate antidiuretic hormone secretion (SIADH) and a multisystemic toxicity due to oxidative stress (OS). Intense thirst induces high intake of pure water, which associated with SIADH, usually develops into acute hyponatremia (Hn). As Hn is induced rapidly, experiments to check if Ec acted directly on the Inner Medullary Collecting Ducts (IMCD) of rats were conducted. Rhabdomyolysis and OS were also studied because Ec is known to induce Reactive Oxygen Species (ROS) and tissue damage. To decrease OS, the antioxidant inhibitors N-acetylcysteine (NAC) and Allopurinol (Allo) were used. METHODS: Rats were maintained on a lithium (Li) diet to block the Vasopressin action before Ec innoculation. AQP2 (Aquaporin 2), ENaC (Epitheliun Sodium Channel) and NKCC2 (Sodium, Potassium, 2 Chloride) expression were determined by Western Blot in isolated IMCDs. The TBARS (thiobarbituric acid reactive substances) and GSH (reduced form of Glutathione) were determined in the Ec group (6 rats injected with Ec-10mg/kg), in Ec+NAC groups (NAC 100mg/Kg/bw i.p.) and in Allo+Ec groups (Allo 50mg/Kg/i.p.). RESULTS: Enhanced AQP2 expression revealed that Ec increased water transporter expression, decreased by Li diet, but the expression of the tubular transporters did not change. The Ec, Ec+NAC and Allo+Ec results showed that Ec increased TBARS and decreased GSH, showing evidence of ROS occurrence, which was protected by NAC and Allo. Rhabdomyolysis was only protected by Allo. CONCLUSION: Results showed that Ec induced an increase in AQP2 expression, evidencing another mechanism that might contribute to cause rapid hyponatremia. In addition, they showed that NAC and Allo protected against OS, but only Allo decreased rhabdomyolysis and hyperthermia.
[Mh] Termos MeSH primário: Depuradores de Radicais Livres/farmacologia
Rim/efeitos dos fármacos
Fibras Musculares Esqueléticas/efeitos dos fármacos
N-Metil-3,4-Metilenodioxianfetamina/toxicidade
Estresse Oxidativo/efeitos dos fármacos
Espécies Reativas de Oxigênio/metabolismo
Rabdomiólise/induzido quimicamente
[Mh] Termos MeSH secundário: Acetilcisteína/farmacologia
Alopurinol/farmacologia
Animais
Aquaporina 2/metabolismo
Western Blotting
Canais Epiteliais de Sódio/metabolismo
Glutationa/metabolismo
Alucinógenos/toxicidade
Rim/metabolismo
Túbulos Renais Coletores/efeitos dos fármacos
Túbulos Renais Coletores/metabolismo
Masculino
Fibras Musculares Esqueléticas/metabolismo
Fibras Musculares Esqueléticas/patologia
Ratos Wistar
Rabdomiólise/prevenção & controle
Membro 1 da Família 12 de Carreador de Soluto/metabolismo
Substâncias Reativas com Ácido Tiobarbitúrico/metabolismo
Água/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aquaporin 2); 0 (Epithelial Sodium Channels); 0 (Free Radical Scavengers); 0 (Hallucinogens); 0 (Reactive Oxygen Species); 0 (Solute Carrier Family 12, Member 1); 0 (Thiobarbituric Acid Reactive Substances); 059QF0KO0R (Water); 63CZ7GJN5I (Allopurinol); GAN16C9B8O (Glutathione); KE1SEN21RM (N-Methyl-3,4-methylenedioxyamphetamine); WYQ7N0BPYC (Acetylcysteine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170706
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179199


  7 / 2306 MEDLINE  
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[PMID]:28667160
[Au] Autor:Lewis BW; Sultana R; Sharma R; Noël A; Langohr I; Patial S; Penn AL; Saini Y
[Ad] Endereço:Department of Comparative Biomedical Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803.
[Ti] Título:Early Postnatal Secondhand Smoke Exposure Disrupts Bacterial Clearance and Abolishes Immune Responses in Muco-Obstructive Lung Disease.
[So] Source:J Immunol;199(3):1170-1183, 2017 Aug 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Secondhand smoke (SHS) exposure has been linked to the worsening of ongoing lung diseases. However, whether SHS exposure affects the manifestation and natural history of imminent pediatric muco-obstructive airway diseases such as cystic fibrosis remains unclear. To address these questions, we exposed transgenic ( -Tg ) mice to SHS from postnatal day (PND) 3-21 and lung phenotypes were examined at PND22. Although a majority of filtered air (FA)-exposed -Tg (FA-Tg ) mice successfully cleared spontaneous bacterial infections by PND22, the SHS-exposed -Tg (SHS-Tg ) mice failed to resolve these infections. This defect was associated with suppressed antibacterial defenses, i.e., phagocyte recruitment, IgA secretion, and Muc5b expression. Whereas the FA-Tg mice exhibited marked mucus obstruction and responses, SHS-Tg mice displayed a dramatic suppression of these responses. Mechanistically, downregulated expression of IL-33, a stimulator of type II innate lymphoid cells, in lung epithelial cells was associated with suppression of neutrophil recruitment, IgA secretions, responses, and delayed bacterial clearance in SHS-Tg mice. Cessation of SHS exposure for 21 d restored previously suppressed responses, including phagocyte recruitment, IgA secretion, and mucous cell metaplasia. However, in contrast with FA-Tg mice, the SHS-Tg mice had pronounced epithelial necrosis, alveolar space consolidation, and lymphoid hyperplasia; indicating lagged unfavorable effects of early postnatal SHS exposure in later life. Collectively, our data show that early postnatal SHS exposure reversibly suppresses IL-33 levels in airspaces which, in turn, results in reduced neutrophil recruitment and diminished response. Our data indicate that household smoking may predispose neonates with muco-obstructive lung disease to bacterial exacerbations.
[Mh] Termos MeSH primário: Infecções Bacterianas/imunologia
Pneumopatias Obstrutivas/imunologia
Poluição por Fumaça de Tabaco/efeitos adversos
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Infecções Bacterianas/fisiopatologia
Carga Bacteriana
Movimento Celular
Fibrose Cística/imunologia
Fibrose Cística/microbiologia
Fibrose Cística/fisiopatologia
Modelos Animais de Doenças
Regulação para Baixo
Células Epiteliais/imunologia
Células Epiteliais/patologia
Canais Epiteliais de Sódio/deficiência
Canais Epiteliais de Sódio/genética
Canais Epiteliais de Sódio/metabolismo
Feminino
Células Caliciformes/patologia
Seres Humanos
Imunoglobulina A/imunologia
Interleucina-33/genética
Interleucina-33/imunologia
Interleucina-33/metabolismo
Pulmão/citologia
Pulmão/imunologia
Pulmão/patologia
Pneumopatias Obstrutivas/fisiopatologia
Camundongos
Camundongos Transgênicos
Mucina-5B
Muco/metabolismo
Neutrófilos/imunologia
Neutrófilos/patologia
Neutrófilos/fisiologia
Transdução de Sinais
Células Th2/imunologia
Células Th2/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Epithelial Sodium Channels); 0 (Il33 protein, mouse); 0 (Immunoglobulin A); 0 (Interleukin-33); 0 (Muc5b protein, mouse); 0 (Mucin-5B); 0 (SCNN1B protein, human); 0 (Tobacco Smoke Pollution)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170702
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700144


  8 / 2306 MEDLINE  
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[PMID]:28559392
[Au] Autor:Ueda K; Nishimoto M; Hirohama D; Ayuzawa N; Kawarazaki W; Watanabe A; Shimosawa T; Loffing J; Zhang MZ; Marumo T; Fujita T
[Ad] Endereço:From the Division of Clinical Epigenetics, Research Center of Advanced Science and Technology, The University of Tokyo, Japan (K.U., M.N., D.H., N.A., W.K., A.W., T.M., T.F.); Department of Clinical Laboratory, International University of Health and Welfare, School of Medicine, Tokyo, Japan (T.S.);
[Ti] Título:Renal Dysfunction Induced by Kidney-Specific Gene Deletion of as a Primary Cause of Salt-Dependent Hypertension.
[So] Source:Hypertension;70(1):111-118, 2017 Jul.
[Is] ISSN:1524-4563
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Genome-wide analysis of renal sodium-transporting system has identified specific variations of Mendelian hypertensive disorders, including gene variants in apparent mineralocorticoid excess. However, these genetic variations in extrarenal tissue can be involved in developing hypertension, as demonstrated in former studies using global and brain-specific knockout rodents. To re-examine the importance of renal dysfunction on developing hypertension, we generated kidney-specific knockout mice. The knockout mice exhibited systemic hypertension, which was abolished by reducing salt intake, suggesting its salt-dependency. In addition, we detected an increase in renal membrane expressions of cleaved epithelial sodium channel-α and T53-phosphorylated Na -Cl cotransporter in the knockout mice. Acute intraperitoneal administration of amiloride-induced natriuresis and increased urinary sodium/potassium ratio more in the knockout mice compared with those in the wild-type control mice. Chronic administration of amiloride and high-KCl diet significantly decreased mean blood pressure in the knockout mice, which was accompanied with the correction of hypokalemia and the resultant decrease in Na -Cl cotransporter phosphorylation. Accordingly, a Na -Cl cotransporter blocker hydrochlorothiazide significantly decreased mean blood pressure in the knockout mice. Chronic administration of mineralocorticoid receptor antagonist spironolactone significantly decreased mean blood pressure of the knockout mice along with downregulation of cleaved epithelial sodium channel-α and phosphorylated Na -Cl cotransporter expression in the knockout kidney. Our data suggest that kidney-specific deficiency of 11ß-HSD2 leads to salt-dependent hypertension, which is attributed to mineralocorticoid receptor-epithelial sodium channel-Na -Cl cotransporter activation in the kidney, and provides evidence that renal dysfunction is essential for developing the phenotype of apparent mineralocorticoid excess.
[Mh] Termos MeSH primário: 11-beta-Hidroxiesteroide Desidrogenase Tipo 2/genética
Pressão Sanguínea/genética
Hipertensão
Receptores de Mineralocorticoides/metabolismo
Insuficiência Renal
Cloreto de Sódio na Dieta
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Canais Epiteliais de Sódio/efeitos dos fármacos
Canais Epiteliais de Sódio/metabolismo
Deleção de Genes
Hipertensão/genética
Hipertensão/metabolismo
Hipertensão/fisiopatologia
Hipertensão/terapia
Transporte de Íons/efeitos dos fármacos
Camundongos
Camundongos Knockout
Antagonistas de Receptores de Mineralocorticoides/farmacologia
Insuficiência Renal/metabolismo
Insuficiência Renal/fisiopatologia
Cloreto de Sódio na Dieta/efeitos adversos
Cloreto de Sódio na Dieta/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Epithelial Sodium Channels); 0 (Mineralocorticoid Receptor Antagonists); 0 (Receptors, Mineralocorticoid); 0 (Sodium Chloride, Dietary); EC 1.1.1.146 (11-beta-Hydroxysteroid Dehydrogenase Type 2); EC 1.1.1.146 (HSD11B2 protein, mouse)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170824
[Lr] Data última revisão:
170824
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170601
[St] Status:MEDLINE
[do] DOI:10.1161/HYPERTENSIONAHA.116.08966


  9 / 2306 MEDLINE  
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[PMID]:28542249
[Au] Autor:Belviso S; Iuliano R; Amato R; Perrotti N; Menniti M
[Ad] Endereço:Department of Experimental and Clinical Medicine, University Magna Graecia of Catanzaro, Catanzaro, Italy.
[Ti] Título:The human asparaginase enzyme (ASPG) inhibits growth in leukemic cells.
[So] Source:PLoS One;12(5):e0178174, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The human protein ASPG is an enzyme with a putative antitumor activity. We generated in bacteria and then purified a recombinant GST-ASPG protein that we used to characterize the biochemical and cytotoxic properties of the human ASPG. We demonstrated that ASPG possesses asparaginase and PAF acetylhydrolase activities that depend on a critical threonine residue at position 19. Consistently, ASPG but not its T19A mutant showed cytotoxic activity in K562, NALM-6 and MOLT-4 leukemic cell lines but not in normal cells. Regarding the mechanism of action of ASPG, it was able to induce a significant apoptotic death in K562 cells. Taken together our data suggest that ASPG, combining different enzymatic activities, should be considered a promising anti-cancer agent for inhibiting the growth of leukemia cells.
[Mh] Termos MeSH primário: Antineoplásicos/uso terapêutico
Asparaginase/uso terapêutico
Leucemia/tratamento farmacológico
[Mh] Termos MeSH secundário: 1-Alquil-2-acetilglicerofosfocolina Esterase/genética
1-Alquil-2-acetilglicerofosfocolina Esterase/uso terapêutico
Substituição de Aminoácidos
Apoptose/efeitos dos fármacos
Asparaginase/genética
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Canais Epiteliais de Sódio/metabolismo
Seres Humanos
Células K562
Leucemia/metabolismo
Leucemia/patologia
Mutagênese Sítio-Dirigida
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/uso terapêutico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Epithelial Sodium Channels); 0 (Recombinant Fusion Proteins); EC 3.1.1.47 (1-Alkyl-2-acetylglycerophosphocholine Esterase); EC 3.5.1.1 (Asparaginase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178174


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[PMID]:28515172
[Au] Autor:Wang L; Song J; Wang S; Buggs J; Chen R; Zhang J; Wang L; Rong S; Li W; Wei J; Liu R
[Ad] Endereço:Department of Molecular Pharmacology and Physiology, University of South Florida College of Medicine, Tampa, Florida; leiwang@health.usf.edu.
[Ti] Título:Cross-sex transplantation alters gene expression and enhances inflammatory response in the transplanted kidneys.
[So] Source:Am J Physiol Renal Physiol;313(2):F326-F338, 2017 Aug 01.
[Is] ISSN:1522-1466
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Kidney transplantation (KTX) is a life-saving procedure for patients with end-stage renal disease. Expression levels of many genes in the kidney vary between males and females, which may play an essential role in the sex differences in graft function. However, whether these differences are affected after cross-sex-KTX is unknown. In the present study, we assessed postoperative changes in genotype, function, and inflammatory responses of the grafts in same-sex- and cross-sex-KTX. Single kidney transplants were performed between same and different sex C57BL/6 mice paired into four combination groups: female donor/female recipient (F/F); male donor/male recipient (M/M); female donor/male recipient (F/M); and male donor/female recipient (M/F). The remnant native kidney was removed 4 days posttransplant. Expression levels of genes related to the contractility of the afferent arteriole and tubular sodium reabsorption were assessed. Same-sex-KTX did not significantly alter the magnitude or sex difference pattern of gene expression in male or female grafts. Cross-sex-KTX showed an attenuated sex difference in gene expressions. The measurements of endothelin 1, endothelin ET receptor, Na -K -2Cl cotransporter 2 (NKCC2), and epithelial Na channels (ENaC) subunits exhibited decreases in M/F compared with M/M and increases in F/M compared with F/F. There were no significant differences in hemodynamics or sodium excretion in response to acute volume expansion for any sex combinations. Cross-sex-KTX stimulated more robust inflammatory responses than same-sex-KTX. IL-6 and KC mRNA levels elevated 5- to 20-fold in cross-sex-KTX compared with same-sex-KTX. In conclusion, cross-sex-KTX alters gene expression levels and induces inflammatory responses, which might play an important role in long-term graft function.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica
Transplante de Rim/efeitos adversos
Rim/metabolismo
Rim/cirurgia
Nefrite/genética
[Mh] Termos MeSH secundário: Animais
Endotelina-1/genética
Endotelina-1/metabolismo
Canais Epiteliais de Sódio/genética
Canais Epiteliais de Sódio/metabolismo
Feminino
Interação Gene-Ambiente
Genótipo
Hemodinâmica
Mediadores da Inflamação/metabolismo
Rim/irrigação sanguínea
Rim/patologia
Masculino
Camundongos Endogâmicos C57BL
Modelos Animais
Nefrite/metabolismo
Nefrite/patologia
Nefrite/fisiopatologia
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Receptores de Angiotensina/genética
Receptores de Angiotensina/metabolismo
Receptores de Endotelina/genética
Receptores de Endotelina/metabolismo
Circulação Renal
Eliminação Renal
Fatores Sexuais
Sódio/metabolismo
Trocador 3 de Sódio-Hidrogênio
Trocadores de Sódio-Hidrogênio/genética
Trocadores de Sódio-Hidrogênio/metabolismo
Membro 1 da Família 12 de Carreador de Soluto/genética
Membro 1 da Família 12 de Carreador de Soluto/metabolismo
Membro 3 da Família 12 de Carreador de Soluto/genética
Membro 3 da Família 12 de Carreador de Soluto/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Endothelin-1); 0 (Epithelial Sodium Channels); 0 (Inflammation Mediators); 0 (RNA, Messenger); 0 (Receptors, Angiotensin); 0 (Receptors, Endothelin); 0 (Slc12a1 protein, mouse); 0 (Slc12a3 protein, mouse); 0 (Sodium-Hydrogen Exchanger 3); 0 (Sodium-Hydrogen Exchangers); 0 (Solute Carrier Family 12, Member 1); 0 (Solute Carrier Family 12, Member 3); 9NEZ333N27 (Sodium)
[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:170519
[St] Status:MEDLINE
[do] DOI:10.1152/ajprenal.00039.2017



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