Base de dados : MEDLINE
Pesquisa : D12.776.157.530.400.500.040.437 [Categoria DeCS]
Referências encontradas : 1248 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 125 ir para página                         

  1 / 1248 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29373579
[Au] Autor:Schrade K; Tröger J; Eldahshan A; Zühlke K; Abdul Azeez KR; Elkins JM; Neuenschwander M; Oder A; Elkewedi M; Jaksch S; Andrae K; Li J; Fernandes J; Müller PM; Grunwald S; Marino SF; Vukicevic T; Eichhorst J; Wiesner B; Weber M; Kapiloff M; Rocks O; Daumke O; Wieland T; Knapp S; von Kries JP; Klussmann E
[Ad] Endereço:Max Delbrück Center for Molecular Medicine Berlin (MDC), Berlin, Germany.
[Ti] Título:An AKAP-Lbc-RhoA interaction inhibitor promotes the translocation of aquaporin-2 to the plasma membrane of renal collecting duct principal cells.
[So] Source:PLoS One;13(1):e0191423, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Stimulation of renal collecting duct principal cells with antidiuretic hormone (arginine-vasopressin, AVP) results in inhibition of the small GTPase RhoA and the enrichment of the water channel aquaporin-2 (AQP2) in the plasma membrane. The membrane insertion facilitates water reabsorption from primary urine and fine-tuning of body water homeostasis. Rho guanine nucleotide exchange factors (GEFs) interact with RhoA, catalyze the exchange of GDP for GTP and thereby activate the GTPase. However, GEFs involved in the control of AQP2 in renal principal cells are unknown. The A-kinase anchoring protein, AKAP-Lbc, possesses GEF activity, specifically activates RhoA, and is expressed in primary renal inner medullary collecting duct principal (IMCD) cells. Through screening of 18,431 small molecules and synthesis of a focused library around one of the hits, we identified an inhibitor of the interaction of AKAP-Lbc and RhoA. This molecule, Scaff10-8, bound to RhoA, inhibited the AKAP-Lbc-mediated RhoA activation but did not interfere with RhoA activation through other GEFs or activities of other members of the Rho family of small GTPases, Rac1 and Cdc42. Scaff10-8 promoted the redistribution of AQP2 from intracellular vesicles to the periphery of IMCD cells. Thus, our data demonstrate an involvement of AKAP-Lbc-mediated RhoA activation in the control of AQP2 trafficking.
[Mh] Termos MeSH primário: Proteínas de Ancoragem à Quinase A/metabolismo
Aquaporina 2/metabolismo
Membrana Celular/metabolismo
Túbulos Renais Coletores/citologia
Antígenos de Histocompatibilidade Menor/metabolismo
Proteínas Proto-Oncogênicas/metabolismo
Bibliotecas de Moléculas Pequenas/farmacologia
Proteína rhoA de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Membrana Celular/efeitos dos fármacos
Células HEK293
Seres Humanos
Ligação Proteica/efeitos dos fármacos
Transporte Proteico/efeitos dos fármacos
Bibliotecas de Moléculas Pequenas/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (A Kinase Anchor Proteins); 0 (AKAP13 protein, human); 0 (Aquaporin 2); 0 (Minor Histocompatibility Antigens); 0 (Proto-Oncogene Proteins); 0 (Small Molecule Libraries); EC 3.6.5.2 (rhoA GTP-Binding Protein)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180127
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191423


  2 / 1248 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28943376
[Au] Autor:Kishida T; Suzuki M; Takayama A
[Ad] Endereço:Wildlife Research Center, Kyoto University, 2-24 Tanaka Sekiden-cho, Sakyo, Kyoto 606-8203, Japan. Electronic address: taku.kishida@gmail.com.
[Ti] Título:Evolution of the alternative AQP2 gene: Acquisition of a novel protein-coding sequence in dolphins.
[So] Source:Mol Phylogenet Evol;118:54-57, 2018 Jan.
[Is] ISSN:1095-9513
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Taxon-specific de novo protein-coding sequences are thought to be important for taxon-specific environmental adaptation. A recent study revealed that bottlenose dolphins acquired a novel isoform of aquaporin 2 generated by alternative splicing (alternative AQP2), which helps dolphins to live in hyperosmotic seawater. The AQP2 gene consists of four exons, but the alternative AQP2 gene lacks the fourth exon and instead has a longer third exon that includes the original third exon and a part of the original third intron. Here, we show that the latter half of the third exon of the alternative AQP2 arose from a non-protein-coding sequence. Intact ORF of this de novo sequence is shared not by all cetaceans, but only by delphinoids. However, this sequence is conservative in all modern cetaceans, implying that this de novo sequence potentially plays important roles for marine adaptation in cetaceans.
[Mh] Termos MeSH primário: Aquaporina 2/química
Golfinhos/classificação
Evolução Molecular
[Mh] Termos MeSH secundário: Processamento Alternativo
Animais
Aquaporina 2/genética
Aquaporina 2/metabolismo
Sequência de Bases
Golfinhos/metabolismo
Éxons
Íntrons
Rim/metabolismo
Filogenia
Isoformas de Proteínas/química
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
RNA/química
RNA/isolamento & purificação
RNA/metabolismo
Alinhamento de Sequência
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aquaporin 2); 0 (Protein Isoforms); 63231-63-0 (RNA)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170926
[St] Status:MEDLINE


  3 / 1248 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28931009
[Au] Autor:Trimpert C; Wesche D; de Groot T; Pimentel Rodriguez MM; Wong V; van den Berg DTM; Cheval L; Ariza CA; Doucet A; Stagljar I; Deen PMT
[Ad] Endereço:Department of Physiology, Radboud University Medical Center, Nijmegen, The Netherlands.
[Ti] Título:NDFIP allows NEDD4/NEDD4L-induced AQP2 ubiquitination and degradation.
[So] Source:PLoS One;12(9):e0183774, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Regulation of our water homeostasis is fine-tuned by dynamic translocation of Aquaporin-2 (AQP2)-bearing vesicles to and from the plasma membrane of renal principal cells. Whereas binding of vasopressin to its type-2 receptor initiates a cAMP-protein kinase A cascade and AQP2 translocation to the apical membrane, this is counteracted by protein kinase C-activating hormones, resulting in ubiquitination-dependent internalization of AQP2. The proteins targeting AQP2 for ubiquitin-mediated degradation are unknown. In collecting duct mpkCCD cells, siRNA knockdown of NEDD4 and NEDD4L E3 ligases yielded increased AQP2 abundance, but they did not bind AQP2. Membrane Yeast Two-Hybrid assays using full-length AQP2 as bait, identified NEDD4 family interacting protein 2 (NDFIP2) to bind AQP2. NDFIP2 and its homologue NDFIP1 have PY motifs by which they bind NEDD4 family members and bring them close to target proteins. In HEK293 cells, NDFIP1 and NDFIP2 bound AQP2 and were essential for NEDD4/NEDD4L-mediated ubiquitination and degradation of AQP2, an effect not observed with PY-lacking NDFIP1/2 proteins. In mpkCCD cells, downregulation of NDFIP1, NEDD4 and NEDD4L, but not NDFIP2, increased AQP2 abundance. In mouse kidney, Ndfip1 and Ndfip2 mRNA distribution was similar and high in proximal tubules and collecting ducts, which was also found for NDFIP1 proteins. Our results reveal that NEDD4/NEDD4L mediate ubiquitination and degradation of AQP2, but that NDFIP proteins are needed to connect NEDD4/NEDD4L to AQP2. As NDFIP1/2 bind many NEDD4 family E3 ligases, which are implicated in several cellular processes, NDFIP1/2 may be the missing link for AQP2 ubiquitination and degradation from different subcellular locations.
[Mh] Termos MeSH primário: Aquaporina 2/metabolismo
Proteínas de Transporte/metabolismo
Complexos Endossomais de Distribuição Requeridos para Transporte/metabolismo
Proteínas de Membrana/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte/genética
Linhagem Celular
Regulação para Baixo
Complexos Endossomais de Distribuição Requeridos para Transporte/antagonistas & inibidores
Complexos Endossomais de Distribuição Requeridos para Transporte/genética
Células HEK293
Seres Humanos
Imunoprecipitação
Masculino
Proteínas de Membrana/genética
Camundongos
Camundongos Endogâmicos C57BL
Ubiquitina-Proteína Ligases Nedd4
Néfrons/metabolismo
Ligação Proteica
Interferência de RNA
RNA Mensageiro/metabolismo
RNA Interferente Pequeno/metabolismo
Técnicas do Sistema de Duplo-Híbrido
Ubiquitina-Proteína Ligases/antagonistas & inibidores
Ubiquitina-Proteína Ligases/genética
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aquaporin 2); 0 (Carrier Proteins); 0 (Endosomal Sorting Complexes Required for Transport); 0 (Membrane Proteins); 0 (NDFIP1 protein, human); 0 (NDFIP2 protein, human); 0 (RNA, Messenger); 0 (RNA, Small Interfering); EC 2.3.2.26 (Nedd4 Ubiquitin Protein Ligases); EC 2.3.2.26 (Nedd4 protein, human); EC 2.3.2.26 (Nedd4L protein, human); EC 2.3.2.26 (Nedd4l protein, mouse); EC 2.3.2.27 (Ubiquitin-Protein Ligases)
[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:170921
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183774


  4 / 1248 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28783044
[Au] Autor:Ware JS; Wain LV; Channavajjhala SK; Jackson VE; Edwards E; Lu R; Siew K; Jia W; Shrine N; Kinnear S; Jalland M; Henry AP; Clayton J; O'Shaughnessy KM; Tobin MD; Schuster VL; Cook S; Hall IP; Glover M
[Ad] Endereço:NIHR Biomedical Research Unit in Cardiovascular Disease at Royal Brompton & Harefield, NHS Foundation Trust and Imperial College London, London, United Kingdom.
[Ti] Título:Phenotypic and pharmacogenetic evaluation of patients with thiazide-induced hyponatremia.
[So] Source:J Clin Invest;127(9):3367-3374, 2017 Sep 01.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Thiazide diuretics are among the most widely used treatments for hypertension, but thiazide-induced hyponatremia (TIH), a clinically significant adverse effect, is poorly understood. Here, we have studied the phenotypic and genetic characteristics of patients hospitalized with TIH. In a cohort of 109 TIH patients, those with severe TIH displayed an extended phenotype of intravascular volume expansion, increased free water reabsorption, urinary prostaglandin E2 excretion, and reduced excretion of serum chloride, magnesium, zinc, and antidiuretic hormone. GWAS in a separate cohort of 48 TIH patients and 2,922 controls from the 1958 British birth cohort identified an additional 14 regions associated with TIH. We identified a suggestive association with a variant in SLCO2A1, which encodes a prostaglandin transporter in the distal nephron. Resequencing of SLCO2A1 revealed a nonsynonymous variant, rs34550074 (p.A396T), and association with this SNP was replicated in a second cohort of TIH cases. TIH patients with the p.A396T variant demonstrated increased urinary excretion of prostaglandin E2 and metabolites. Moreover, the SLCO2A1 phospho-mimic p.A396E showed loss of transporter function in vitro. These findings indicate that the phenotype of TIH involves a more extensive metabolic derangement than previously recognized. We propose one mechanism underlying TIH development in a subgroup of patients in which SLCO2A1 regulation is altered.
[Mh] Termos MeSH primário: Hiponatremia/induzido quimicamente
Inibidores de Simportadores de Cloreto de Sódio/efeitos adversos
Tiazidas/efeitos adversos
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Aquaporina 1/genética
Aquaporina 2/genética
Estudos de Coortes
Dinoprostona/metabolismo
Feminino
Estudo de Associação Genômica Ampla
Seres Humanos
Hiponatremia/genética
Masculino
Meia-Idade
Néfrons/metabolismo
Transportadores de Ânions Orgânicos/genética
Farmacogenética
Fenótipo
Polimorfismo de Nucleotídeo Único
Prostaglandinas/metabolismo
Reino Unido
Água/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AQP1 protein, human); 0 (AQP2 protein, human); 0 (Aquaporin 2); 0 (Organic Anion Transporters); 0 (Prostaglandins); 0 (SLCO2A1 protein, human); 0 (Sodium Chloride Symporter Inhibitors); 0 (Thiazides); 059QF0KO0R (Water); 146410-94-8 (Aquaporin 1); K7Q1JQR04M (Dinoprostone)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170808
[St] Status:MEDLINE


  5 / 1248 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28736155
[Au] Autor:Hatem-Vaquero M; Griera M; Giermakowska W; Luengo A; Calleros L; Gonzalez Bosc LV; Rodríguez-Puyol D; Rodríguez-Puyol M; De Frutos S
[Ad] Endereço:Department of Systems Biology, Physiology Unit, Faculty of Medicine, University of Alcalá, 28805 Alcalá de Henares, Madrid, Spain; Instituto Reina Sofia de Investigación Renal and REDinREN from Instituto de Salud Carlos III, Madrid, Spain. Electronic address: marco.hatem@edu.uah.es.
[Ti] Título:Integrin linked kinase regulates the transcription of AQP2 by NFATC3.
[So] Source:Biochim Biophys Acta;1860(9):922-935, 2017 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Two processes are associated with progressive loss of renal function: 1) decreased aquaporin-2 (AQP2) expression and urinary concentrating capacity (Nephrogenic Diabetes Insipidus, NDI); and 2) changes in extracellular matrix (ECM) composition, e.g. increased collagen I (Col I) deposition, characteristic of tubule-interstitial fibrosis. AQP2 expression is regulated by both the ECM-to-intracellular scaffold protein integrin-linked kinase (ILK) by NFATc/AP1 and other transcription factors. In the present work, we used in vivo and in vitro approaches to examine ILK participation in NFATc3/AP-1-mediated increases in AQP2 gene expression. Both NFATc3 knock-out mice and ILK conditional-knockdown mice (cKD-ILK) display symptoms of NDI (polyuria and reduced AQP2 expression). NFATc3 is upregulated in the renal medulla tubular cells of cKD-ILK mice but with reduced nuclear localization. Inner medullary collecting duct mIMCD3 cells were subjected to ILK depletion and transfected with reporter plasmids. Pharmacological activators or inhibitors determined the effect of ILK activity on NFATc/AP-1-dependent increases in transcription of AQP2. Finally, mIMCD3 cultured on Col I showed reduced activity of the ILK/GSK3ß/NFATc/AQP2 axis, suggesting this pathway is a potential target for therapeutic treatment of NDI.
[Mh] Termos MeSH primário: Aquaporina 2/genética
Fatores de Transcrição NFATC/genética
Proteínas Serina-Treonina Quinases/metabolismo
Transcrição Genética/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Diabetes Insípido Nefrogênico/genética
Diabetes Insípido Nefrogênico/metabolismo
Integrinas/metabolismo
Medula Renal/metabolismo
Túbulos Renais Coletores/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Camundongos Endogâmicos C57BL
Camundongos Knockout
Poliúria/genética
Poliúria/metabolismo
Fator de Transcrição AP-1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aqp2 protein, mouse); 0 (Aquaporin 2); 0 (Integrins); 0 (NFATC Transcription Factors); 0 (Nfatc3 protein, mouse); 0 (Transcription Factor AP-1); EC 2.7.1.- (integrin-linked kinase); EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE


  6 / 1248 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28710278
[Au] Autor:Roche JV; Survery S; Kreida S; Nesverova V; Ampah-Korsah H; Gourdon M; Deen PMT; Törnroth-Horsefield S
[Ad] Endereço:From the Department of Biochemistry and Structural Biology, Lund University, 221 00 Lund, Sweden and.
[Ti] Título:Phosphorylation of human aquaporin 2 (AQP2) allosterically controls its interaction with the lysosomal trafficking protein LIP5.
[So] Source:J Biol Chem;292(35):14636-14648, 2017 Sep 01.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The interaction between the renal water channel aquaporin-2 (AQP2) and the lysosomal trafficking regulator-interacting protein LIP5 targets AQP2 to multivesicular bodies and facilitates lysosomal degradation. This interaction is part of a process that controls AQP2 apical membrane abundance in a vasopressin-dependent manner, allowing for urine volume adjustment. Vasopressin regulates phosphorylation at four sites within the AQP2 C terminus (Ser , Ser , Ser , and Thr ), of which Ser is crucial and sufficient for AQP2 translocation from storage vesicles to the apical membrane. However, whether AQP2 phosphorylation modulates AQP2-LIP5 complex affinity is unknown. Here we used far-Western blot analysis and microscale thermophoresis to show that the AQP2 binds LIP5 in a phosphorylation-dependent manner. We constructed five phospho-mimicking mutants (S256E, S261E, S264E, T269E, and S256E/T269E) and a C-terminal truncation mutant (ΔP242) that lacked all phosphorylation sites but retained a previously suggested LIP5-binding site. CD spectroscopy indicated that wild-type AQP2 and the phospho-mimicking mutants had similar overall structure but displayed differences in melting temperatures possibly arising from C-terminal conformational changes. Non-phosphorylated AQP2 bound LIP5 with the highest affinity, whereas AQP2-ΔP242 had 20-fold lower affinity as determined by microscale thermophoresis. AQP2-S256E, S261E, T269E, and S256E/T269E all had reduced affinity. This effect was most prominent for AQP2-S256E, which fits well with its role in apical membrane targeting. AQP2-S264E had affinity similar to non-phosphorylated AQP2, possibly indicating a role in exosome excretion. Our data suggest that AQP2 phosphorylation allosterically controls its interaction with LIP5, illustrating how altered affinities to interacting proteins form the basis for regulation of AQP2 trafficking by post-translational modifications.
[Mh] Termos MeSH primário: Aquaporina 2/metabolismo
Complexos Endossomais de Distribuição Requeridos para Transporte/metabolismo
Modelos Moleculares
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Regulação Alostérica
Substituição de Aminoácidos
Aquaporina 2/química
Sítios de Ligação
Complexos Endossomais de Distribuição Requeridos para Transporte/química
Deleção de Genes
Seres Humanos
Mutação
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Fosforilação
Pichia/enzimologia
Pichia/metabolismo
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Estabilidade Proteica
Transporte Proteico
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Temperatura de Transição
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AQP2 protein, human); 0 (Aquaporin 2); 0 (Endosomal Sorting Complexes Required for Transport); 0 (Peptide Fragments); 0 (Recombinant Fusion Proteins); 0 (VTA1 protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170716
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.788364


  7 / 1248 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28701310
[Au] Autor:Mamuya FA; Xie D; Lei L; Huang M; Tsuji K; Capen DE; Yang B; Weissleder R; Paunescu TG; Lu HAJ
[Ad] Endereço:Program in Membrane Biology and Division of Nephrology, Department of Medicine, Massachusetts General Hospital, Boston, Massachusetts.
[Ti] Título:Deletion of ß1-integrin in collecting duct principal cells leads to tubular injury and renal medullary fibrosis.
[So] Source:Am J Physiol Renal Physiol;313(4):F1026-F1037, 2017 Oct 01.
[Is] ISSN:1522-1466
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The renal collecting duct (CD) contains two major cell types, intercalated (ICs) and principal cells (PCs). A previous report showed that deletion of ß1-integrin in the entire renal CD causes defective CD morphogenesis resulting in kidney dysfunction. However, subsequent deletion of ß1-integrin specifically in ICs and PCs, respectively, did not cause any morphological defects in the CDs. The discrepancy between these studies prompts us to reinvestigate the role of ß1-integrin in CD cells, specifically in the PCs. We conditionally deleted ß1-integrin in mouse CD PCs using a specific aquaporin-2 (AQP2) promoter Cre-LoxP system. The resulting mutant mice, ß-1 AQP2-Cre+, had lower body weight, failed to thrive, and died around 8-12 wk. Their CD tubules were dilated, and some of them contained cellular debris. Increased apoptosis and proliferation of PCs were observed in the dilated CDs. Trichrome staining and electron microscopy revealed the presence of peritubular and interstitial fibrosis that is associated with increased production of extracellular matrix proteins including collagen type IV and fibronectin, as detected by immunoblotting. Further analysis revealed a significantly increased expression of transforming growth factor-ß (TGF-ß)-induced protein, fibronectin, and TGF-ß receptor-1 mRNAs and concomitantly increased phosphorylation of SMAD-2 that indicates the activation of the TGF-ß signaling pathway. Therefore, our data reveal that normal expression of ß1-integrin in PCs is a critical determinant of CD structural and functional integrity and further support the previously reported critical role of ß1-integrin in the development and/or maintenance of the CD structure and function.
[Mh] Termos MeSH primário: Matriz Extracelular/metabolismo
Deleção de Genes
Integrina beta1/metabolismo
Medula Renal/metabolismo
Túbulos Renais Coletores/metabolismo
Poliúria/metabolismo
Insuficiência Renal/metabolismo
[Mh] Termos MeSH secundário: Fatores Etários
Animais
Apoptose
Aquaporina 2/genética
Proliferação Celular
Matriz Extracelular/ultraestrutura
Insuficiência de Crescimento/genética
Insuficiência de Crescimento/metabolismo
Insuficiência de Crescimento/patologia
Fibrose
Predisposição Genética para Doença
Integrases/genética
Integrina beta1/genética
Medula Renal/ultraestrutura
Túbulos Renais Coletores/ultraestrutura
Camundongos Knockout
Fenótipo
Fosforilação
Poliúria/genética
Poliúria/patologia
Regiões Promotoras Genéticas
Proteínas Serina-Treonina Quinases/genética
Proteínas Serina-Treonina Quinases/metabolismo
Receptores de Fatores de Crescimento Transformadores beta/genética
Receptores de Fatores de Crescimento Transformadores beta/metabolismo
Insuficiência Renal/genética
Insuficiência Renal/patologia
Transdução de Sinais
Proteína Smad2/metabolismo
Fator de Crescimento Transformador beta/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aqp2 protein, mouse); 0 (Aquaporin 2); 0 (Integrin beta1); 0 (Receptors, Transforming Growth Factor beta); 0 (Smad2 Protein); 0 (Smad2 protein, mouse); 0 (Transforming Growth Factor beta); EC 2.7.1.11 (TGF-beta type I receptor); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.7.- (Cre recombinase); EC 2.7.7.- (Integrases)
[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:10.1152/ajprenal.00038.2017


  8 / 1248 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[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


  9 / 1248 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28668390
[Au] Autor:Yui N; Ando F; Sasaki S; Uchida S
[Ad] Endereço:Department of Nephrology, Graduate School of Medical and Dental Science, Tokyo Medical and Dental University, Tokyo, Japan. Electronic address: nyui.kid@tmd.ac.jp.
[Ti] Título:Ser-261 phospho-regulation is involved in pS256 and pS269-mediated aquaporin-2 apical translocation.
[So] Source:Biochem Biophys Res Commun;490(3):1039-1044, 2017 Aug 26.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Vasopressin catalyzes aquaporin-2 phosphorylation at several serine sites in the C-terminal region. Compared with Ser-256 and Ser-269 phosphorylation, the role of Ser-261 phospho-regulation on vasopressin-regulated AQP2 apical translocation is largely unknown. In addition, recent discovery of transcytotic apical delivery of AQP2 made the concept of its intracellular trafficking even more complicated. In this study, we evaluated how intact phospho-AQP2 signals fit with the transcytosis trafficking model in Madin-Darby canine kidney cells. PS256 and pS269 signals were intracellularly detectable in wild-type AQP2 at the beginning of forskolin stimulation (1 min). These phospho-signals were detectable in basolateral membranes even after 10 min of stimulation. AQP2 stably inserted in the apical membrane increased pS269 and decreased pS261 signals. In an NDI-causing mutant P262L-AQP2, in which Ser-261 phospho-regulation is impaired, the pS256 and pS269 signals were detectable in the basolateral membranes with increased pS261 signals after forskolin stimulation. These results suggest that Ser-261 phospho-regulation is involved in pS256- and pS269-mediated AQP2 apical translocation.
[Mh] Termos MeSH primário: Aquaporina 2/metabolismo
[Mh] Termos MeSH secundário: Animais
Aquaporina 2/análise
Membrana Celular/metabolismo
Membrana Celular/ultraestrutura
Colforsina/farmacologia
Cães
Endocitose/efeitos dos fármacos
Células Madin Darby de Rim Canino
Fosforilação/efeitos dos fármacos
Transporte Proteico/efeitos dos fármacos
Ratos
Serina/análise
Serina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aquaporin 2); 1F7A44V6OU (Colforsin); 452VLY9402 (Serine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170703
[St] Status:MEDLINE


  10 / 1248 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28615247
[Au] Autor:de Groot T; Doornebal J; Christensen BM; Cockx S; Sinke AP; Baumgarten R; Bedford JJ; Walker RJ; Wetzels JFM; Deen PMT
[Ad] Endereço:Department of Physiology, Radboud University Medical Center, Nijmegen, The Netherlands.
[Ti] Título:Lithium-induced NDI: acetazolamide reduces polyuria but does not improve urine concentrating ability.
[So] Source:Am J Physiol Renal Physiol;313(3):F669-F676, 2017 Sep 01.
[Is] ISSN:1522-1466
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lithium is the mainstay treatment for patients with bipolar disorder, but it generally causes nephrogenic diabetes insipidus (NDI), a disorder in which the renal urine concentrating ability has become vasopressin insensitive. Li-NDI is caused by lithium uptake by collecting duct principal cells and downregulation of aquaporin-2 (AQP2) water channels, which are essential for water uptake from tubular urine. Recently, we found that the prophylactic administration of acetazolamide to mice effectively attenuated Li-NDI. To evaluate whether acetazolamide might benefit lithium-treated patients, we administered acetazolamide to mice with established Li-NDI and six patients with a lithium-induced urinary concentrating defect. In mice, acetazolamide partially reversed lithium-induced polyuria and increased urine osmolality, which, however, did not coincide with increased AQP2 abundances. In patients, acetazolamide led to the withdrawal of two patients from the study due to side effects. In the four remaining patients acetazolamide did not lead to clinically relevant changes in maximal urine osmolality. Urine output was also not affected, although none of these patients demonstrated overt lithium-induced polyuria. In three out of four patients, acetazolamide treatment increased serum creatinine levels, indicating a decreased glomerular filtration rate (GFR). Strikingly, these three patients also showed a decrease in systemic blood pressure. All together, our data reveal that acetazolamide does not improve the urinary concentrating defect caused by lithium, but it lowers the GFR, likely explaining the reduced urine output in our mice and in a recently reported patient with lithium-induced polyuria. The reduced GFR in patients prone to chronic kidney disease development, however, warrants against application of acetazolamide in Li-NDI patients without long-term (pre)clinical studies.
[Mh] Termos MeSH primário: Acetazolamida/uso terapêutico
Diabetes Insípido Nefrogênico/tratamento farmacológico
Diuréticos/uso terapêutico
Capacidade de Concentração Renal/efeitos dos fármacos
Rim/efeitos dos fármacos
Cloreto de Lítio
Poliúria/tratamento farmacológico
[Mh] Termos MeSH secundário: Acetazolamida/efeitos adversos
Idoso
Animais
Aquaporina 2/metabolismo
Pressão Sanguínea/efeitos dos fármacos
Diabetes Insípido Nefrogênico/induzido quimicamente
Diabetes Insípido Nefrogênico/fisiopatologia
Modelos Animais de Doenças
Diuréticos/efeitos adversos
Feminino
Taxa de Filtração Glomerular/efeitos dos fármacos
Seres Humanos
Rim/metabolismo
Rim/fisiopatologia
Masculino
Camundongos Endogâmicos C57BL
Meia-Idade
Países Baixos
Nova Zelândia
Concentração Osmolar
Projetos Piloto
Poliúria/induzido quimicamente
Poliúria/fisiopatologia
Estudos Prospectivos
Fatores de Tempo
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE; MULTICENTER STUDY
[Nm] Nome de substância:
0 (Aqp2 protein, mouse); 0 (Aquaporin 2); 0 (Diuretics); G4962QA067 (Lithium Chloride); O3FX965V0I (Acetazolamide)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1152/ajprenal.00147.2017



página 1 de 125 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde