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  1 / 19767 MEDLINE  
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[PMID]:28954371
[Au] Autor:Ajima MNO; Pandey PK; Kumar K; Poojary N
[Ad] Endereço:Department of Fisheries and Aquaculture Technology, Federal University of Technology, Owerri, Nigeria. Electronic address: malajimo@gmail.com.
[Ti] Título:Alteration in DNA structure, molecular responses and Na -K -ATPase activities in the gill of Nile tilapia, Oreochromis niloticus (Linnaeus, 1758) in response to sub-lethal verapamil.
[So] Source:Ecotoxicol Environ Saf;147:809-816, 2018 Jan.
[Is] ISSN:1090-2414
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The ecotoxicological consequences of residues from pharmaceutical drugs on aquatic biota have necessitated the development of sensitive and reliable techniques to assess the impact of these xenobiotics on aquatic organisms. This study investigated the alteration in DNA structure, molecular responses and the activities of Na -K -ATPase and antioxidant enzymes in the gill of Nile tilapia, Oreochromis niloticus, exposed to long-term effects at the concentrations (0.14, 0.28 and 0.57mgL ) of verapamil in static renewal system for 15, 30, 45 and 60 days. Evaluation of DNA structure, using single cell gel electrophoresis, revealed certain degree of DNA damages in the gill in a time and concentration-dependent relationship. Transcription of mRNA of superoxide dismutase (sod), catalase (cat) and heat shock protein (hsp70) genes in the gill of the fish showed the genes were up-regulated. Na -K -ATPase activity was inhibited in a concentration and time dependent manner. The indices of oxidative stress biomarkers (lipid peroxidation and carbonyl protein) as well as superoxide dismutase, glutathione peroxidase, glutathione-S-transferase were elevated in the treated fish in comparison to the control. Further, the level of reduced glutathione and catalase activity were inhibited at 0.28mgL after day 30. Long-term exposure to sub-lethal concentration of verapamil can cause DNA damages, molecular effects and oxidative stress in O. niloticus. The biomarkers analysed can be used as early warning signals in environmental biomonitoring and assessment of drug contamination in aquatic ecosystem.
[Mh] Termos MeSH primário: Ciclídeos/metabolismo
Dano ao DNA
Brânquias/efeitos dos fármacos
ATPase Trocadora de Sódio-Potássio/metabolismo
Verapamil/toxicidade
Poluentes Químicos da Água/toxicidade
[Mh] Termos MeSH secundário: Animais
Antioxidantes/metabolismo
Biomarcadores/metabolismo
Ciclídeos/genética
Relação Dose-Resposta a Droga
Monitoramento Ambiental/métodos
Brânquias/metabolismo
Estresse Oxidativo/efeitos dos fármacos
Verapamil/metabolismo
Poluentes Químicos da Água/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Biomarkers); 0 (Water Pollutants, Chemical); CJ0O37KU29 (Verapamil); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170929
[St] Status:MEDLINE


  2 / 19767 MEDLINE  
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[PMID]:29348113
[Au] Autor:Monticone S; Buffolo F; Tetti M; Veglio F; Pasini B; Mulatero P
[Ad] Endereço:Division of Internal Medicine and Hypertension UnitDepartment of Medical Sciences, University of Torino, Torino, Italy.
[Ti] Título:GENETICS IN ENDOCRINOLOGY: The expanding genetic horizon of primary aldosteronism.
[So] Source:Eur J Endocrinol;178(3):R101-R111, 2018 Mar.
[Is] ISSN:1479-683X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Aldosterone is the main mineralocorticoid hormone in humans and plays a key role in maintaining water and electrolyte homeostasis. Primary aldosteronism (PA), characterized by autonomous aldosterone overproduction by the adrenal glands, affects 6% of the general hypertensive population and can be either sporadic or familial. Aldosterone-producing adenoma (APA) and bilateral adrenal hyperplasia (BAH) are the two most frequent subtypes of sporadic PA and 4 forms of familial hyperaldosteronism (FH-I to FH-IV) have been identified. Over the last six years, the introduction of next-generation sequencing has significantly improved our understanding of the molecular mechanisms responsible for autonomous aldosterone overproduction in both sporadic and familial PA. Somatic mutations in four genes ( and ), differently implicated in intracellular ion homeostasis, have been identified in nearly 60% of the sporadic APAs. Germline mutations in and cause FH-III and FH-IV, respectively, while germline mutations in cause the rare PASNA syndrome, featuring primary aldosteronism seizures and neurological abnormalities. Further studies are warranted to identify the molecular mechanisms underlying BAH and FH-II, the most common forms of sporadic and familial PA whose molecular basis is yet to be uncovered.
[Mh] Termos MeSH primário: Canais de Cálcio Tipo L/genética
Canais de Potássio Corretores do Fluxo de Internalização Acoplados a Proteínas G/genética
Hiperaldosteronismo/genética
ATPases Transportadoras de Cálcio da Membrana Plasmática/genética
ATPase Trocadora de Sódio-Potássio/genética
[Mh] Termos MeSH secundário: Aldosterona/biossíntese
Variação Genética
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (CACNA1D protein, human); 0 (Calcium Channels, L-Type); 0 (G Protein-Coupled Inwardly-Rectifying Potassium Channels); 0 (KCNJ5 protein, human); 4964P6T9RB (Aldosterone); EC 3.6.1.- (ATP1A1 protein, human); EC 3.6.3.8 (ATP2B3 protein, human); EC 3.6.3.8 (Plasma Membrane Calcium-Transporting ATPases); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1530/EJE-17-0946


  3 / 19767 MEDLINE  
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[PMID]:29307086
[Au] Autor:Sousa L; Pessoa MTC; Costa TGF; Cortes VF; Santos HL; Barbosa LA
[Ad] Endereço:Laboratório de Bioquímica Celular, Campus Centro-Oeste Dona Lindu, Universidade Federal de São João del Rei, Av Sebastião Gonçalves Coelho, 400, Divinópolis, MG, 35501-296, Brazil.
[Ti] Título:Iron overload impact on P-ATPases.
[So] Source:Ann Hematol;97(3):377-385, 2018 Mar.
[Is] ISSN:1432-0584
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Iron is a chemical element that is active in the fundamental physiological processes for human life, but its burden can be toxic to the body, mainly because of the stimulation of membrane lipid peroxidation. For this reason, the action of iron on many ATPases has been studied, especially on P-ATPases, such as the Na ,K -ATPase and the Ca -ATPase. On the Fe -ATPase activity, the free iron acts as an activator, decreasing the intracellular Fe and playing a protection role for the cell. On the Ca -ATPase activity, the iron overload decreases the enzyme activity, raising the cytoplasmic Ca and decreasing the sarco/endoplasmic reticulum and the Golgi apparatus Ca concentrations, which could promote an enzyme oxidation, nitration, and fragmentation. However, the iron overload effect on the Na ,K -ATPase may change according to the tissue expressions. On the renal cells, as well as on the brain and the heart, iron promotes an enzyme inactivation, whereas its effect on the erythrocytes seems to be the opposite, directly stimulating the ATPase activity, or stimulating it by signaling pathways involving ROS and PKC. Modulations in the ATPase activity may impair the ionic transportation, which is essential for cell viability maintenance, inducing irreversible damage to the cell homeostasis. Here, we will discuss about the iron overload effect on the P-ATPases, such as the Na ,K -ATPase, the Ca -ATPase, and the Fe -ATPase.
[Mh] Termos MeSH primário: ATPases Transportadoras de Cálcio/metabolismo
Sobrecarga de Ferro/metabolismo
ATPase Trocadora de Sódio-Potássio/metabolismo
[Mh] Termos MeSH secundário: Animais
Transporte Biológico
Cálcio/metabolismo
Sinalização do Cálcio/fisiologia
Seres Humanos
Ferro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
E1UOL152H7 (Iron); EC 3.6.3.8 (Calcium-Transporting ATPases); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180108
[St] Status:MEDLINE
[do] DOI:10.1007/s00277-017-3222-4


  4 / 19767 MEDLINE  
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[PMID]:29339143
[Au] Autor:Komisarczuk AZ; Kongshaug H; Nilsen F
[Ad] Endereço:Sea Lice Research Centre, Department of Biology, University of Bergen, Thormøhlensgate 55, 5008, Bergen, Norway. Electronic address: Anna.Komisarczuk@uib.no.
[Ti] Título:Gene silencing reveals multiple functions of Na /K -ATPase in the salmon louse (Lepeophtheirus salmonis).
[So] Source:Exp Parasitol;185:79-91, 2018 Feb.
[Is] ISSN:1090-2449
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Na /K -ATPase has a key function in a variety of physiological processes including membrane excitability, osmoregulation, regulation of cell volume, and transport of nutrients. While knowledge about Na /K -ATPase function in osmoregulation in crustaceans is extensive, the role of this enzyme in other physiological and developmental processes is scarce. Here, we report characterization, transcriptional distribution and likely functions of the newly identified L. salmonis Na /K -ATPase (LsalNa /K -ATPase) α subunit in various developmental stages. The complete mRNA sequence was identified, with 3003 bp open reading frame encoding a putative protein of 1001 amino acids. Putative protein sequence of LsalNa /K -ATPase revealed all typical features of Na /K -ATPase and demonstrated high sequence identity to other invertebrate and vertebrate species. Quantitative RT-PCR analysis revealed higher LsalNa /K -ATPase transcript level in free-living stages in comparison to parasitic stages. In situ hybridization analysis of copepodids and adult lice revealed LsalNa /K -ATPase transcript localization in a wide variety of tissues such as nervous system, intestine, reproductive system, and subcuticular and glandular tissue. RNAi mediated knock-down of LsalNa /K -ATPase caused locomotion impairment, and affected reproduction and feeding. Morphological analysis of dsRNA treated animals revealed muscle degeneration in larval stages, severe changes in the oocyte formation and maturation in females and abnormalities in tegmental glands. Thus, the study represents an important foundation for further functional investigation and identification of physiological pathways in which Na /K -ATPase is directly or indirectly involved.
[Mh] Termos MeSH primário: Copépodes/enzimologia
Inativação Gênica
ATPase Trocadora de Sódio-Potássio/fisiologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Copépodes/genética
Copépodes/crescimento & desenvolvimento
Copépodes/fisiologia
DNA Complementar/química
Ectoparasitoses/parasitologia
Ectoparasitoses/veterinária
Feminino
Doenças dos Peixes/parasitologia
Pesqueiros
Regulação Enzimológica da Expressão Gênica
Técnicas de Silenciamento de Genes
Hibridização In Situ
Masculino
Fases de Leitura Aberta/genética
Filogenia
Interferência de RNA
RNA de Cadeia Dupla
RNA Mensageiro/química
Reação em Cadeia da Polimerase em Tempo Real
Salmo salar/parasitologia
Água do Mar
Alinhamento de Sequência
ATPase Trocadora de Sódio-Potássio/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Complementary); 0 (RNA, Double-Stranded); 0 (RNA, Messenger); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE


  5 / 19767 MEDLINE  
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[PMID]:29300475
[Au] Autor:Zou D; Zhu X; Zhang F; Du Y; Ma J; Jiang R
[Ad] Endereço:Institute of Traditional Chinese Medicine and Natural Products, College of Pharmacy, Jinan University , Guangzhou 510632, P. R. China.
[Ti] Título:An Efficient Strategy Based on Liquid-Liquid Extraction with Three-Phase Solvent System and High Speed Counter-Current Chromatography for Rapid Enrichment and Separation of Epimers of Minor Bufadienolide from Toad Meat.
[So] Source:J Agric Food Chem;66(4):1008-1014, 2018 Jan 31.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:This study presents an efficient strategy based on liquid-liquid extraction with three-phase solvent system and high speed counter-current chromatography for rapid enrichment and separation of epimers of minor bufadienolide from toad meat. The reflux extraction conditions were optimized by response surface methodology first, and a novel three-phase solvent system composed of n-hexane/methyl acetate/acetonitrile/water (3:6:5:5, v/v) was developed for liquid-liquid extraction of the crude extract. This integrative extraction process could enrich minor bufadienolide from complex matrix efficiently and minimize the loss of minor targets induced by repeated extraction with different kinds of organic solvents occurring in the classical liquid two-phase extraction. As a result, four epimers of minor bufadienolide were greatly enriched in the middle phase and total content of these epimers of minor bufadienolide was increased from 3.25% to 46.23%. Then, the enriched four epimers were separated by HSCCC with a two-phase solvent system composed of chloroform/methanol/water (4:2:2, v/v) successfully. Furthermore, we tested Na ,K -ATPase (NKA) inhibitory effect of the four epimers. 3ß-Isomers of bufadienolide showed stronger (>8-fold) inhibitory activity than 3α-isomers. The characterization of minor bufadienolide in toad meat and their significant difference of inhibitory effect on NKA would promote the further quantitative analysis and safety evaluation of toad meat as a food source.
[Mh] Termos MeSH primário: Bufanolídeos/química
Bufanolídeos/isolamento & purificação
Bufonidae
Distribuição Contracorrente/métodos
Extração Líquido-Líquido/métodos
Carne/análise
[Mh] Termos MeSH secundário: Animais
Bufanolídeos/farmacologia
Inibidores Enzimáticos
Isomerismo
ATPase Trocadora de Sódio-Potássio/antagonistas & inibidores
Solventes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bufanolides); 0 (Enzyme Inhibitors); 0 (Solvents); 29565-35-3 (bufadienolide); EC 3.6.1.- (ATP1A1 protein, human); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180105
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b05310


  6 / 19767 MEDLINE  
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[PMID]:29287866
[Au] Autor:Paquay S; Wiame E; Deggouj N; Boschi A; De Siati RD; Sznajer Y; Nassogne MC
[Ad] Endereço:Pediatric Neurology Unit, Cliniques Universitaires Saint-Luc, Université Catholique de Louvain, Brussels, Belgium. Electronic address: stephanie.paquay@uclouvain.be.
[Ti] Título:Childhood hearing loss is a key feature of CAPOS syndrome: A case report.
[So] Source:Int J Pediatr Otorhinolaryngol;104:191-194, 2018 Jan.
[Is] ISSN:1872-8464
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:CAPOS syndrome (cerebellar ataxia, areflexia, pes cavus, optic atrophy, and sensorineural hearing loss) is a rare neurological disorder, recently associated with the c.2452G > A hotspot mutation in the ATP1A3 gene, with sensorineural hearing loss as a prominent feature. We herein report on a girl who has experienced hearing loss for three years following an initial encephalitic episode when aged 15 months old. CAPOS was diagnosed only when she was six years old by targeted testing whilst she displayed optic atrophy, cerebellar signs and areflexia. CAPOS syndrome should be considered in the differential diagnosis of acquired childhood deafness, prompting clinicians to search for associated neurological features.
[Mh] Termos MeSH primário: Ataxia Cerebelar/diagnóstico
Deformidades Congênitas do Pé/diagnóstico
Perda Auditiva Neurossensorial/etiologia
Atrofia Óptica/diagnóstico
[Mh] Termos MeSH secundário: Ataxia Cerebelar/complicações
Criança
Diagnóstico Diferencial
Feminino
Deformidades Congênitas do Pé/complicações
Perda Auditiva Neurossensorial/complicações
Perda Auditiva Neurossensorial/diagnóstico
Testes Auditivos
Seres Humanos
Mutação
Atrofia Óptica/complicações
Reflexo Anormal
ATPase Trocadora de Sódio-Potássio/genética
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.3.9 (ATP1A3 protein, human); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171231
[St] Status:MEDLINE


  7 / 19767 MEDLINE  
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[PMID]:29235753
[Ti] Título:The influence of heavy metal ions, spermine and sodium nitroprusside on ATP-hydrolases of cell membranes of rat colon smooth muscle.
[So] Source:Ukr Biochem J;88(4):20-8, 2016 Jul-Aug.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:The specific features of functional lability of the rat colon smooth muscle (CSM) АТР-hydrolases were studied. Na+,K+-AТРase activity is effectively inhibited by divalent ions of both transition (≥ 0,1 µM) and nontransition (≥ 1 µM) heavy metals in succession by efficiency: Cu2+ > Fe2+ ≥ Cd2+ (10 µM). Polyamine spermine (0,5-1,0 mM) is a weak Na+,K+-AТРase inhibitor at saturation concentrations of ions and substrate. Sodium nitroprusside (1 mM) as nitric oxide-generating compound exhibits weak Na+,K+-AТРase inhibition only after prolonged preincubation with membranes. Mg2+-АТР-hydrolase activity in all cases is much more resistant to studied agents. Considering the example of the CSM Na+,K+-AТРase it is assumed that enzyme has specific biochemical features that contribute to its role as a potential target and redox-sensor, mediating the pathological mechanisms of heavy metal intoxication and cell oxidative damage.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Membrana Celular/efeitos dos fármacos
Metais Pesados/farmacologia
Nitroprussiato/farmacologia
ATPase Trocadora de Sódio-Potássio/metabolismo
Espermina/farmacologia
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/antagonistas & inibidores
Animais
Cádmio/farmacologia
Cátions Bivalentes
Fracionamento Celular
Membrana Celular/metabolismo
Colo/citologia
Colo/enzimologia
Cobre/farmacologia
Ferro/farmacologia
Cinética
Masculino
Músculo Liso/citologia
Músculo Liso/enzimologia
Miócitos de Músculo Liso/citologia
Miócitos de Músculo Liso/enzimologia
Ratos
Ratos Wistar
ATPase Trocadora de Sódio-Potássio/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cations, Divalent); 0 (Metals, Heavy); 00BH33GNGH (Cadmium); 169D1260KM (Nitroprusside); 2FZ7Y3VOQX (Spermine); 789U1901C5 (Copper); E1UOL152H7 (Iron); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (magnesium sodium ATPase); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.04.020


  8 / 19767 MEDLINE  
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[PMID]:29227611
[Au] Autor:Rushchak VV; Chashchyn MO
[Ti] Título:Cytochrome P450 2E1 participation in the pathogenesis of experimental metabolic syndrome in guinea pigs.
[So] Source:Ukr Biochem J;88(2):98-106, 2016 Mar-Apr.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:In this work the experimental metabolic syndrome on the basis of protamine sulfate modeling in guinea pigs was reproduced and pathological processes in the liver of experimental animals were studied. We determined the level of free radicals and markers of liver damage in the blood of experimental animals. We investigated the liver glycogen content and K+,Na+-ATPase activity in the liver of experimental animals as well as measured the cytochrome P450 2E1 (CY P2E1) expression ­ one of the main factors of oxidative stress. Evidence of development of hepatotoxic processes, increasing of the CY P2E1 level as well as of the free radical level in the animals with metabolic syndrome were found. Using of CY P2E1 inhibitors had shown that the free radical level in the blood of experimental animals depended on the level of the enzyme expression and activity. The obtained results suggest that the changes in the CY P2E1 expression play an important role in the development of hepatotoxic processes upon experimental metabolic syndrome. It was assumed that pharmacological correction of the enzyme expression may be an important mechanism for the influence on the metabolic syndrome clinical course.
[Mh] Termos MeSH primário: Inibidores do Citocromo P-450 CYP2E1/farmacologia
Citocromo P-450 CYP2E1/genética
Fígado/efeitos dos fármacos
Síndrome Metabólica/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Citocromo P-450 CYP2E1/metabolismo
Dissulfiram/farmacologia
Radicais Livres/antagonistas & inibidores
Radicais Livres/metabolismo
Regulação da Expressão Gênica
Glicogênio/metabolismo
Cobaias
Fígado/enzimologia
Fígado/patologia
Masculino
Síndrome Metabólica/induzido quimicamente
Síndrome Metabólica/enzimologia
Síndrome Metabólica/patologia
Estresse Oxidativo/efeitos dos fármacos
Protaminas
Pirazóis/farmacologia
Quercetina/farmacologia
ATPase Trocadora de Sódio-Potássio/genética
ATPase Trocadora de Sódio-Potássio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytochrome P-450 CYP2E1 Inhibitors); 0 (Free Radicals); 0 (Protamines); 0 (Pyrazoles); 83LCM6L2BY (fomepizole); 9005-79-2 (Glycogen); 9IKM0I5T1E (Quercetin); EC 1.14.13.- (Cytochrome P-450 CYP2E1); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase); TR3MLJ1UAI (Disulfiram)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.02.098


  9 / 19767 MEDLINE  
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[PMID]:29237574
[Au] Autor:Freire CA; Maraschi AC; Lara AF; Amado EM; Prodocimo V
[Ad] Endereço:Departamento de Fisiologia, Setor de Ciências Biológicas, Universidade Federal do Paraná, Curitiba, PR CEP 81531-990, Brazil. Electronic address: cafreire@ufpr.br.
[Ti] Título:Late rise in hemolymph osmolality in Macrobrachium acanthurus (diadromous freshwater shrimp) exposed to brackish water: Early reduction in branchial Na /K pump activity but stable muscle HSP70 expression.
[So] Source:Comp Biochem Physiol B Biochem Mol Biol;216:69-74, 2018 Feb.
[Is] ISSN:1879-1107
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Some Macrobrachium shrimps (Caridea, Palaemonidae) are diadromous; freshwater adults are truly euryhaline, while larvae need saline water for development. Branchial Na /K -ATPase (NKA) and carbonic anhydrase (CA) are involved in NaCl absorption in freshwater. This study aimed at verifying the time course of the osmoregulatory response of adult Macrobrachium acanthurus to high salinity brackish water (20‰), from the first 30min to 5days. The goal was to detect possible transition from hyper- to hyporegulation, the putative involvement of branchial NKA and CA, or the induction of muscular HSP70 expression. Hemolymph osmotic and ionic concentrations remained relatively stable and close to control levels until ~9h of exposure, but later increased consistently (~50%). A fast reduction in NKA activity (3-6h) was observed; these shrimps seem to shut off salt absorption already in the first hours. Later on, especially after 24h, hemolymph concentrations rise but HSP70 expression is not induced, possibly because constitutive levels are already sufficient to prevent protein damage. Time-dependent response mechanisms effective in high salinity brackish water, resulting in salt loading avoidance and suggestive of hyporegulation should be further investigated in decapods that evolutionary invaded freshwater.
[Mh] Termos MeSH primário: Proteínas de Artrópodes/biossíntese
Regulação da Expressão Gênica
Proteínas de Choque Térmico HSP70/biossíntese
Hemolinfa/metabolismo
Músculos/metabolismo
Palaemonidae/metabolismo
ATPase Trocadora de Sódio-Potássio/biossíntese
[Mh] Termos MeSH secundário: Animais
Concentração Osmolar
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arthropod Proteins); 0 (HSP70 Heat-Shock Proteins); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180102
[Lr] Data última revisão:
180102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171215
[St] Status:MEDLINE


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[PMID]:29115894
[Au] Autor:Pessôa MTC; Alves SLG; Taranto AG; Villar JAFP; Blanco G; Barbosa LA
[Ad] Endereço:a Laboratório de Bioquímica Celular , Universidade Federal de São João del Rei, Campus Centro-Oeste Dona Lindú , Divinópolis , Brazil.
[Ti] Título:Selectivity analyses of γ-benzylidene digoxin derivatives to different Na,K-ATPase α isoforms: a molecular docking approach.
[So] Source:J Enzyme Inhib Med Chem;33(1):85-97, 2018 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Digoxin and other cardiotonic steroids (CTS) exert their effect by inhibiting Na,K-ATPase (NKA) activity. CTS bind to the various NKA isoforms that are expressed in different cell types, which gives CTS their narrow therapeutic index. We have synthesised a series of digoxin derivatives (γ-Benzylidene digoxin derivatives) with substitutions in the lactone ring (including non-oxygen and ether groups), to obtain CTS with better NKA isoform specificity. Some of these derivatives show some NKA isoform selective effects, with BD-3, BD-8, and BD-13 increasing NKA α2 activity, BD-5 inhibiting NKA α1 and NKA α3, BD-10 reducing NKA α1, but stimulating NKA α2 and α3; and BD-14, BD-15, and BD-16 enhancing NKA α3 activity. A molecular-docking approach favoured NKA isoform specific interactions for the compounds that supported their observed activity. These results show that BD compounds are a new type of CTS with the capacity to target NKA activity in an isoform-specific manner.
[Mh] Termos MeSH primário: Compostos de Benzilideno/farmacologia
Digoxina/farmacologia
Simulação de Acoplamento Molecular
ATPase Trocadora de Sódio-Potássio/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Compostos de Benzilideno/síntese química
Compostos de Benzilideno/química
Células Cultivadas
Digoxina/síntese química
Digoxina/química
Relação Dose-Resposta a Droga
Isoenzimas/antagonistas & inibidores
Isoenzimas/metabolismo
Conformação Molecular
Células Sf9
ATPase Trocadora de Sódio-Potássio/metabolismo
Spodoptera
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzylidene Compounds); 0 (Isoenzymes); 73K4184T59 (Digoxin); EC 3.6.3.9 (Sodium-Potassium-Exchanging ATPase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171109
[St] Status:MEDLINE
[do] DOI:10.1080/14756366.2017.1380637



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