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[PMID]:29204997
[Au] Autor:Zhao B; Yao SQ; Hao XH
[Ad] Endereço:Forensic Science Brigade of Tangshan Public Security Bureau, Tangshan 063000, China.
[Ti] Título:[Expression of AQP-1 and AQP-4 in the Lungs of Drown Rats].
[So] Source:Fa Yi Xue Za Zhi;32(5):321-325, 2016 Oct.
[Is] ISSN:1004-5619
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVES: To observe the changes of expression of aquaporin-1(AQP-1) and AQP-4 in drowned and postmortem immersed rats' lungs. METHODS: Thirty healthy male Wistar rats were randomly divided into drowning group, postmortem immersion group and cervical dislocation group. The morphological changes of rats' lungs were observed using HE staining. The mRNA and protein expressions of AQP-1 and AQP-4 in rats' lungs were detected by real-time PCR, immunohistochemistry and Western blotting, respectively. RESULTS: The results of immunohistochemistry and the Western blotting showed that the protein expression of AQP-1 of the drowning group was higher than the postmortem immersion group and the cervical dislocation group ( <0.05). The result of immunohistochemistry showed that the protein expression of AQP-4 of the drowning group was higher than the postmortem immersion group and the cervical dislocation group ( <0.05) while no difference were detected among the three of them by Western blotting ( >0.05). The mRNA expressions of AQP-1 and AQP-4 in rats' lungs of the drowning group was significantly higher than the postmortem immersion group ( <0.05). CONCLUSIONS: The increase of mRNA and protein expressions of AQP-1 and AQP-4 in lungs of rats with cute lung injury of the drowning group would be useful for differentiating vital drowning from postmortem immersion.
[Mh] Termos MeSH primário: Aquaporina 1/metabolismo
Aquaporina 4/metabolismo
Afogamento
Pulmão/metabolismo
[Mh] Termos MeSH secundário: Animais
Autopsia
Western Blotting
Imuno-Histoquímica
Masculino
RNA Mensageiro
Ratos
Ratos Sprague-Dawley
Ratos Wistar
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aqp1 protein, rat); 0 (Aqp4 protein, rat); 0 (Aquaporin 4); 0 (RNA, Messenger); 146410-94-8 (Aquaporin 1)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE
[do] DOI:10.3969/j.issn.1004-5619.2016.05.001


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[PMID]:28470555
[Au] Autor:Hong-Min F; Chun-Rong H; Rui Z; Li-Na S; Ya-Jun W; Li L
[Ad] Endereço:Comprehensive Pediatric Internal Department, Children's Hospital, Kunming Medical University, Kunming, 6500032, People's Republic of China.
[Ti] Título:CGRP 8-37 enhances lipopolysaccharide-induced acute lung injury and regulating aquaporin 1 and 5 expressions in rats.
[So] Source:J Physiol Biochem;73(3):381-386, 2016 Aug.
[Is] ISSN:1877-8755
[Cp] País de publicação:Spain
[La] Idioma:eng
[Ab] Resumo:Calcitonin gene-related peptide (CGRP) has been shown to play important roles in biological functions. However, there is very little evidence on the value of CGRP in lipopolysaccharide (LPS)-induced acute lung injury/acute respiratory distress syndrome (ALI/ARDS). Therefore, this study aimed to investigate the role of CGRP in LPS-induced ALI in rats. In the experiment, Sprague-Dawley (SD) rats were randomized into control, an antagonist of α-calcitonin gene-related peptide receptor (CGRP8-37), LPS groups, and CGRP8-37 + LPS groups. ALI model was prepared through retrograde injection of LPS (10 mg/kg). At 6 and 12 h, bronchoalveolar lavage was performed and used to assess total cell count and levels of tumor necrosis factor-α, interleukin-1ß, -6, and -10 by enzyme-linked immunosorbent assay (ELISA). Lung tissue was collected for assessing wet-to-dry (W/D) ratio, hematoxylin and eosin staining. Aquaporin (AQP)-1 and -5 expressions in lung tissues were detected by quantitative PCR and Western blot. The results showed that histological injury, total cell count, and W/D ratio significantly reduced in LPS group after 6 h. The levels of inflammatory cytokines in CGRP8-37 + LPS-treated rats were higher than that in LPS-treated rats (all, P < 0.001). Real-time RT-PCR analysis showed that levels of AQP-1 in rats from CGRP8-37 + LPS group was lower than that in LPS-treated rats (P = 0.005 and P < 0.001). Western blotting analysis showed that AQP-1 protein levels at 6 h significantly decreased in CGRP8-37 + LPS rats. Together, our data suggest that CGRP antagonists, CGRP8-37 could enhance ALI induced by LPS in the rat model, and regulate the expression levels of AQP-1 and AQP-5 by affecting inflammatory cytokines. Thereby, regulating endogenous CGRP may be a potential treatment for ALI/ARDS.
[Mh] Termos MeSH primário: Lesão Pulmonar Aguda/imunologia
Aquaporina 1/genética
Aquaporina 5/genética
Peptídeo Relacionado com Gene de Calcitonina/farmacologia
Fragmentos de Peptídeos/farmacologia
[Mh] Termos MeSH secundário: Lesão Pulmonar Aguda/metabolismo
Animais
Aquaporina 1/metabolismo
Aquaporina 5/metabolismo
Expressão Gênica/efeitos dos fármacos
Lipopolissacarídeos/farmacologia
Pulmão/imunologia
Pulmão/metabolismo
Pulmão/patologia
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aqp1 protein, rat); 0 (Aqp5 protein, rat); 0 (Aquaporin 5); 0 (Lipopolysaccharides); 0 (Peptide Fragments); 119911-68-1 (calcitonin gene-related peptide (8-37)); 146410-94-8 (Aquaporin 1); 83652-28-2 (Calcitonin Gene-Related Peptide)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/s13105-017-0563-3


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[PMID]:29196765
[Au] Autor:Kumari S; Gao J; Mathias RT; Sun X; Eswaramoorthy A; Browne N; Zhang N; Varadaraj K
[Ad] Endereço:Department of Physiology and Biophysics, Stony Brook University, Stony Brook, New York, United States.
[Ti] Título:Aquaporin 0 Modulates Lens Gap Junctions in the Presence of Lens-Specific Beaded Filament Proteins.
[So] Source:Invest Ophthalmol Vis Sci;58(14):6006-6019, 2017 Dec 01.
[Is] ISSN:1552-5783
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose: The objective of this study was to understand the molecular and physiologic mechanisms behind the lens cataract differences in Aquaporin 0-knockout-Heterozygous (AQP0-Htz) mice developed in C57 and FVB (lacks beaded filaments [BFs]) strains. Methods: Lens transparency was studied using dark field light microscopy. Water permeability (Pf) was measured in fiber cell membrane vesicles. Western blotting/immunostaining was performed to verify expression of BF proteins and connexins. Microelectrode-based intact lens intracellular impedance was measured to determine gap junction (GJ) coupling resistance. Lens intracellular hydrostatic pressure (HP) was determined using a microelectrode/manometer system. Results: Lens opacity and spherical aberration were more distinct in AQP0-Htz lenses from FVB than C57 strains. In either background, compared to wild type (WT), AQP0-Htz lenses showed decreased Pf (approximately 50%), which was restored by transgenic expression of AQP1 (TgAQP1/AQP0-Htz), but the opacities and differences between FVB and C57 persisted. Western blotting revealed no change in connexin expression levels. However, in C57 AQP0-Htz and TgAQP1/AQP0-Htz lenses, GJ coupling resistance decreased approximately 2.8-fold and the HP gradient decreased approximately 1.9-fold. Increased Pf in TgAQP1/AQP0-Htz did not alter GJ coupling resistance or HP. Conclusions: In C57 AQP0-Htz lenses, GJ coupling resistance decreased. HP reduction was smaller than the coupling resistance reduction, a reflection of an increase in fluid circulation, which is one reason for the less severe cataract in C57 than FVB. Overall, our results suggest that AQP0 modulates GJs in the presence of BF proteins to maintain lens transparency and homeostasis.
[Mh] Termos MeSH primário: Aquaporina 1/genética
Catarata/genética
Proteínas do Olho/genética
Regulação da Expressão Gênica
Proteínas de Filamentos Intermediários/genética
Cristalino/metabolismo
RNA/genética
[Mh] Termos MeSH secundário: Animais
Aquaporina 1/biossíntese
Western Blotting
Catarata/metabolismo
Catarata/patologia
Modelos Animais de Doenças
Impedância Elétrica
Proteínas do Olho/biossíntese
Junções Comunicantes/genética
Junções Comunicantes/metabolismo
Genótipo
Heterozigoto
Proteínas de Filamentos Intermediários/biossíntese
Cristalino/patologia
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Microeletrodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aqp1 protein, mouse); 0 (Eye Proteins); 0 (Intermediate Filament Proteins); 0 (filensin); 146410-94-8 (Aquaporin 1); 63231-63-0 (RNA)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171220
[Lr] Data última revisão:
171220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171203
[St] Status:MEDLINE
[do] DOI:10.1167/iovs.17-22153


  4 / 1459 MEDLINE  
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[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


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[PMID]:28762291
[Au] Autor:Pini N; Pfeifle VA; Kym U; Keck S; Galati V; Holland-Cunz S; Gros SJ
[Ad] Endereço:a Department of Pediatric Surgery , University Childrens' Hospital of Basel (UKBB) , Basel , Switzerland.
[Ti] Título:Water permeability is a measure of severity in acute appendicitis.
[So] Source:J Enzyme Inhib Med Chem;32(1):1036-1041, 2017 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Acute appendicitis is the most common indication for pediatric abdominal emergency surgery. Determination of the severity of appendicitis on clinical grounds is challenging. Complicated appendicitis presenting with perforation, abscess or diffuse peritonitis is not uncommon. The question remains why and when acute appendicitis progresses to perforation. The aim of this study was to assess the impact of water permeability on the severity of appendicitis. We show that AQP1 expression and water permeability in appendicitis correlate with the stage of inflammation and systemic infection parameters, leading eventually to perforation of the appendix. AQP1 is also expressed within the ganglia of the enteric nervous system and ganglia count increases with inflammation. Severity of appendicitis can be correlated with water permeability measured by AQP1 protein expression and increase of ganglia count in a progressive manner. This introduces the question if regulation of water permeability can present novel curative or ameliorating therapeutic options.
[Mh] Termos MeSH primário: Apendicite/diagnóstico
Água/química
[Mh] Termos MeSH secundário: Doença Aguda
Adolescente
Aquaporina 1/biossíntese
Criança
Pré-Escolar
Feminino
Seres Humanos
Masculino
Permeabilidade
Índice de Gravidade de Doença
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AQP1 protein, human); 059QF0KO0R (Water); 146410-94-8 (Aquaporin 1)
[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:170802
[St] Status:MEDLINE
[do] DOI:10.1080/14756366.2017.1347167


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[PMID]:28733452
[Au] Autor:Toussaint J; Raval CB; Nguyen T; Fadaifard H; Joshi S; Wolberg G; Quarfordt S; Jan KM; Rumschitzki DS
[Ad] Endereço:Department of Chemical Engineering, City College of the City University of New York, New York, New York.
[Ti] Título:Chronic hypertension increases aortic endothelial hydraulic conductivity by upregulating endothelial aquaporin-1 expression.
[So] Source:Am J Physiol Heart Circ Physiol;313(5):H1063-H1073, 2017 Nov 01.
[Is] ISSN:1522-1539
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Numerous studies have examined the role of aquaporins in osmotic water transport in various systems, but virtually none have focused on the role of aquaporin in hydrostatically driven water transport involving mammalian cells save for our laboratory's recent study of aortic endothelial cells. Here, we investigated aquaporin-1 expression and function in the aortic endothelium in two high-renin rat models of hypertension, the spontaneously hypertensive genetically altered Wistar-Kyoto rat variant and Sprague-Dawley rats made hypertensive by two-kidney, one-clip Goldblatt surgery. We measured aquaporin-1 expression in aortic endothelial cells from whole rat aortas by quantitative immunohistochemistry and function by measuring the pressure-driven hydraulic conductivities of excised rat aortas with both intact and denuded endothelia on the same vessel. We used them to calculate the effective intimal hydraulic conductivity, which is a combination of endothelial and subendothelial components. We observed well-correlated enhancements in aquaporin-1 expression and function in both hypertensive rat models as well as in aortas from normotensive rats whose expression was upregulated by 2 h of forskolin treatment. Upregulated aquaporin-1 expression and function may be a response to hypertension that critically determines conduit artery vessel wall viability and long-term susceptibility to atherosclerosis. The aortic endothelia of two high-renin hypertensive rat models express greater than two times the aquaporin-1 and, at low pressures, have greater than two times the endothelial hydraulic conductivity of normotensive rats. Data are consistent with theory predicting that higher endothelial aquaporin-1 expression raises the critical pressure for subendothelial intima compression and for artery wall hydraulic conductivity to drop.
[Mh] Termos MeSH primário: Aorta/metabolismo
Aquaporina 1/metabolismo
Pressão Arterial
Endotélio Vascular/metabolismo
Hipertensão/metabolismo
Mecanotransdução Celular
[Mh] Termos MeSH secundário: Animais
Aorta/fisiopatologia
Doença Crônica
AMP Cíclico/metabolismo
Modelos Animais de Doenças
Endotélio Vascular/fisiopatologia
Hipertensão/genética
Hipertensão/fisiopatologia
Masculino
Modelos Cardiovasculares
Nefrectomia
Ratos Endogâmicos SHR
Ratos Endogâmicos WKY
Ratos Sprague-Dawley
Fatores de Tempo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aqp1 protein, rat); 146410-94-8 (Aquaporin 1); E0399OZS9N (Cyclic AMP)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170723
[St] Status:MEDLINE
[do] DOI:10.1152/ajpheart.00651.2016


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[PMID]:28596233
[Au] Autor:Hsu K; Lee TY; Periasamy A; Kao FJ; Li LT; Lin CY; Lin HJ; Lin M
[Ad] Endereço:Transfusion Medicine Laboratory, Mackay Memorial Hospital, Tamsui, Taiwan; khsu1@mmh.org.tw.
[Ti] Título:Adaptable interaction between aquaporin-1 and band 3 reveals a potential role of water channel in blood CO transport.
[So] Source:FASEB J;31(10):4256-4264, 2017 Oct.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human CO respiration requires rapid conversion between CO and HCO Carbonic anhydrase II facilitates this reversible reaction inside red blood cells, and band 3 [anion exchanger 1 (AE1)] provides a passage for HCO flux across the cell membrane. These 2 proteins are core components of the CO transport metabolon. Intracellular H O is necessary for CO /HCO conversion. However, abundantly expressed aquaporin 1 (AQP1) in erythrocytes is thought not to be part of band 3 complexes or the CO transport metabolon. To solve this conundrum, we used Förster resonance energy transfer (FRET) measured by fluorescence lifetime imaging (FLIM-FRET) and identified interaction between aquaporin-1 and band 3 at a distance of 8 nm, within the range of dipole-dipole interaction. Notably, their interaction was adaptable to membrane tonicity changes. This suggests that the function of AQP1 in tonicity response could be coupled or correlated to its function in band 3-mediated CO /HCO exchange. By demonstrating AQP1 as a mobile component of the CO transport metabolon, our results uncover a potential role of water channel in blood CO transport and respiration.-Hsu, K., Lee, T.-Y., Periasamy, A., Kao, F.-J., Li, L.-T., Lin, C.-Y., Lin, H.-J., Lin, M. Adaptable interaction between aquaporin-1 and band 3 reveals a potential role of water channel in blood CO transport.
[Mh] Termos MeSH primário: Proteína 1 de Troca de Ânion do Eritrócito/metabolismo
Aquaporina 1/metabolismo
Transporte Biológico/fisiologia
Dióxido de Carbono/sangue
Permeabilidade da Membrana Celular/fisiologia
Eritrócitos/metabolismo
[Mh] Termos MeSH secundário: Membrana Eritrocítica/metabolismo
Seres Humanos
Concentração de Íons de Hidrogênio
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anion Exchange Protein 1, Erythrocyte); 142M471B3J (Carbon Dioxide); 146410-94-8 (Aquaporin 1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170610
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201601282R


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[PMID]:28409279
[Au] Autor:Schuoler C; Haider TJ; Leuenberger C; Vogel J; Ostergaard L; Kwapiszewska G; Kohler M; Gassmann M; Huber LC; Brock M
[Ad] Endereço:Institute of Veterinary Physiology, Vetsuisse Faculty, University of Zurich, Zurich, Switzerland.
[Ti] Título:Aquaporin 1 controls the functional phenotype of pulmonary smooth muscle cells in hypoxia-induced pulmonary hypertension.
[So] Source:Basic Res Cardiol;112(3):30, 2017 May.
[Is] ISSN:1435-1803
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Vascular remodelling in hypoxia-induced pulmonary hypertension (PH) is driven by excessive proliferation and migration of endothelial and smooth muscle cells. The expression of aquaporin 1 (AQP1), an integral membrane water channel protein involved in the control of these processes, is tightly regulated by oxygen levels. The role of AQP1 in the pathogenesis of PH, however, has not been directly addressed so far. This study was designed to characterize expression and function of AQP1 in pulmonary vascular cells from human arteries and in the mouse model of hypoxia-induced PH. Exposure of human pulmonary vascular cells to hypoxia significantly induced the expression of AQP1. Similarly, levels of AQP1 were found to be upregulated in lungs of mice with hypoxia-induced PH. The functional role of AQP1 was further tested in human pulmonary artery smooth muscle cells demonstrating that depletion of AQP1 reduced proliferation, the migratory potential, and, conversely, increased apoptosis of these cells. This effect was associated with higher expression of the tumour suppressor gene p53. Using the mouse model of hypoxia-induced PH, application of GapmeR inhibitors targeting AQP1 abated the hypoxia-induced upregulation of AQP1 and, of note, reversed PH by decreasing both right ventricular pressure and hypertrophy back to the levels of control mice. Our data suggest an important functional role of AQP1 in the pathobiology of hypoxia-induced PH. These results offer novel insights in our pathogenetic understanding of the disease and propose AQP1 as potential therapeutic in vivo target.
[Mh] Termos MeSH primário: Aquaporina 1/metabolismo
Hipertensão Pulmonar/metabolismo
Miócitos de Músculo Liso/metabolismo
Remodelação Vascular/fisiologia
[Mh] Termos MeSH secundário: Animais
Western Blotting
Células Cultivadas
Modelos Animais de Doenças
Seres Humanos
Hipóxia
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Músculo Liso Vascular/metabolismo
Fenótipo
Artéria Pulmonar/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AQP1 protein, human); 0 (Aqp1 protein, mouse); 146410-94-8 (Aquaporin 1)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170425
[Lr] Data última revisão:
170425
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170415
[St] Status:MEDLINE
[do] DOI:10.1007/s00395-017-0620-7


  9 / 1459 MEDLINE  
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[PMID]:28380032
[Au] Autor:Guo H; Wei M; Liu Y; Zhu Y; Xu W; Meng L; Wang N; Shao C; Lu S; Gao F; Cui Z; Wei Z; Zhao F; Chen S
[Ad] Endereço:Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences (CAFS), Key Laboratory for Sustainable Development of Marine Fisheries, Ministry of Agriculture, Qingdao, PR China.
[Ti] Título:Molecular cloning and expression analysis of the aqp1aa gene in half-smooth tongue sole (Cynoglossus semilaevis).
[So] Source:PLoS One;12(4):e0175033, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Aquaporin 1 (AQP1) is a member of the transmembrane water channel family of proteins with special structural features, and two AQP1 paralogous genes (aqp1aa and aqp1ab) are reported in teleosts. In the present study, the aqp1aa gene of half-smooth tongue sole (Cynoglossus semilaevis) was cloned and characterized. The full-length cDNA of aqp1aa is 1411 bp with a 786 bp open reading frame encoding a 261-amino acid putative protein with a characteristic structure consisting of 6 membrane-spanning α-helical domains and two highly conserved asparagine-proline-alanine motifs. Real-time quantitative PCR revealed that aqp1aa mRNA is expressed predominantly in the testis of males and pseudo-males, while its expression is low in the ovary and lowest in doublesex and mab-3-related transcription factor 1(DMRT1) knock out fish and triploid males. In situ hybridization indicated that aqp1aa mRNA is expressed mainly in the germ cells of males and pseudo-males, especially in spermatozoa and spermatids. These results suggest that the aqp1aa may play a role in spermatogenesis of C. semilaevis.
[Mh] Termos MeSH primário: Aquaporina 1/genética
Linguados/genética
[Mh] Termos MeSH secundário: Animais
Aquaporina 1/metabolismo
Clonagem Molecular
Feminino
Linguados/metabolismo
Perfilação da Expressão Gênica
Hibridização In Situ
Masculino
Ovário/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Espermatogênese/genética
Testículo/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
146410-94-8 (Aquaporin 1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170406
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175033


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[PMID]:28279185
[Au] Autor:Cartwright SP; Darby RA; Sarkar D; Bonander N; Gross SR; Ashe MP; Bill RM
[Ad] Endereço:School of Life and Health Sciences, Aston University, Aston Triangle, Birmingham, B4 7ET, UK.
[Ti] Título:Constitutively-stressed yeast strains are high-yielding for recombinant Fps1: implications for the translational regulation of an aquaporin.
[So] Source:Microb Cell Fact;16(1):41, 2017 Mar 09.
[Is] ISSN:1475-2859
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: We previously selected four strains of Saccharomyces cerevisiae for their ability to produce the aquaporin Fps1 in sufficient yield for further study. Yields from the yeast strains spt3Δ, srb5Δ, gcn5Δ and yTHCBMS1 (supplemented with 0.5 µg/mL doxycycline) that had been transformed with an expression plasmid containing 249 base pairs of 5' untranslated region (UTR) in addition to the primary FPS1 open reading frame (ORF) were 10-80 times higher than yields from wild-type cells expressing the same plasmid. One of the strains increased recombinant yields of the G protein-coupled receptor adenosine receptor 2a (A R) and soluble green fluorescent protein (GFP). The specific molecular mechanisms underpinning a high-yielding Fps1 phenotype remained incompletely described. RESULTS: Polysome profiling experiments were used to analyze the translational state of spt3Δ, srb5Δ, gcn5Δ and yTHCBMS1 (supplemented with 0.5 µg/mL doxycycline); all but gcn5Δ were found to exhibit a clear block in translation initiation. Four additional strains with known initiation blocks (rpl31aΔ, rpl22aΔ, ssf1Δ and nop1Δ) also improved the yield of recombinant Fps1 compared to wild-type. Expression of the eukaryotic transcriptional activator GCN4 was increased in spt3Δ, srb5Δ, gcn5Δ and yTHCBMS1 (supplemented with 0.5 µg/mL doxycycline); these four strains also exhibited constitutive phosphorylation of the eukaryotic initiation factor, eIF2α. Both responses are indicative of a constitutively-stressed phenotype. Investigation of the 5'UTR of FPS1 in the expression construct revealed two untranslated ORFs (uORF1 and uORF2) upstream of the primary ORF. Deletion of either uORF1 or uORF1 and uORF2 further improved recombinant yields in our four strains; the highest yields of the uORF deletions were obtained from wild-type cells. Frame-shifting the stop codon of the native uORF (uORF2) so that it extended into the FPS1 ORF did not substantially alter Fps1 yields in spt3Δ or wild-type cells, suggesting that high-yielding strains are able to bypass 5'uORFs in the FPS1 gene via leaky scanning, which is a known stress-response mechanism. Yields of recombinant A R, GFP and horseradish peroxidase could be improved in one or more of the yeast strains suggesting that a stressed phenotype may also be important in high-yielding cell factories. CONCLUSIONS: Regulation of Fps1 levels in yeast by translational control may be functionally important; the presence of a native uORF (uORF2) may be required to maintain low levels of Fps1 under normal conditions, but higher levels as part of a stress response. Constitutively-stressed yeast strains may be useful high-yielding microbial cell factories for recombinant protein production.
[Mh] Termos MeSH primário: Aquaporina 1/biossíntese
Aquaporina 1/genética
Regulação Fúngica da Expressão Gênica
Iniciação Traducional da Cadeia Peptídica/genética
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Regiões 5' não Traduzidas
Códon de Terminação
Doxiciclina/farmacologia
Genes Fúngicos
Proteínas de Fluorescência Verde/genética
Fases de Leitura Aberta
Plasmídeos/genética
Polirribossomos
Receptor A2A de Adenosina/biossíntese
Receptor A2A de Adenosina/genética
Proteínas Recombinantes/biossíntese
Saccharomyces cerevisiae/efeitos dos fármacos
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (Codon, Terminator); 0 (Receptor, Adenosine A2A); 0 (Recombinant Proteins); 0 (Saccharomyces cerevisiae Proteins); 146410-94-8 (Aquaporin 1); 147336-22-9 (Green Fluorescent Proteins); N12000U13O (Doxycycline)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170420
[Lr] Data última revisão:
170420
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170311
[St] Status:MEDLINE
[do] DOI:10.1186/s12934-017-0656-2



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