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  1 / 40588 MEDLINE  
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[PMID]:29442032
[Au] Autor:Jiang JF; Zhai J; Liu ZR; Chao L; Zhao YF; Wu YJ; Cui MX
[Ti] Título:Ampelopsin sodium induces mitochondrial-mediated apoptosis in human lung adenocarcinoma SPC-A-1 cell line.
[So] Source:Pharmazie;71(8):455-459, 2016 08 01.
[Is] ISSN:0031-7144
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Ampelopsin is a well-known flavonoid which has variety of biological and pharmacological actions including anticancer effects and induction of apoptosis on the several cancer cell lines. The present study aimed to evaluate the role of ampelopsin sodium (Amp-Na) in the mitochondrial-mediated apoptosis of human lung adenocarcionma SPC-A-1 cells. The analysis of cell proliferation and ultrastructure were performed. Furthermore, to clarify its action mechanism by determining the mitochondrial membrane potential (Δψm), intracellular calcium (Ca2+) concentration, mitochondrial nitric oxide (NO) level and total ATPase activity. The results showed that Amp-Na markedly inhibited the SPC-A-1 cell proliferation and caused ultrastructural apoptosis feature in SPC-A-1 cells in a dose-dependent manner. Amp-Na led to a rapid and sustained Ca2+ elevation and Δψm reduction, and induced the mitochondrial NO production and decreased the total ATPase activity in SPC-A-1 cells. The results enhance the potential of Amp-Na as a therapeutic drug for treating lung cancer, and provide new information for mechanism of Amp-Na which induces mitochondrial-mediated apoptosis in tumor cells.
[Mh] Termos MeSH primário: Adenocarcinoma/tratamento farmacológico
Antineoplásicos Fitogênicos/farmacologia
Apoptose/efeitos dos fármacos
Flavonoides/farmacologia
Neoplasias Pulmonares/tratamento farmacológico
Mitocôndrias/efeitos dos fármacos
[Mh] Termos MeSH secundário: Adenocarcinoma/patologia
Adenocarcinoma/ultraestrutura
Adenosina Trifosfatases/metabolismo
Cálcio/metabolismo
Linhagem Celular Tumoral
Proliferação Celular
Relação Dose-Resposta a Droga
Seres Humanos
Neoplasias Pulmonares/patologia
Neoplasias Pulmonares/ultraestrutura
Potencial da Membrana Mitocondrial/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents, Phytogenic); 0 (Flavonoids); 27200-12-0 (ampelopsin); EC 3.6.1.- (Adenosine Triphosphatases); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180215
[St] Status:MEDLINE
[do] DOI:10.1691/ph.2016.6571


  2 / 40588 MEDLINE  
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[PMID]:29295984
[Au] Autor:Goyal N; Rossi MJ; Mazina OM; Chi Y; Moritz RL; Clurman BE; Mazin AV
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA, 19102, USA.
[Ti] Título:RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions.
[So] Source:Nat Commun;9(1):34, 2018 01 02.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In eukaryotes, RAD54 catalyzes branch migration (BM) of Holliday junctions, a basic process during DNA repair, replication, and recombination. RAD54 also stimulates RAD51 recombinase and has other activities. Here, we investigate the structural determinants for different RAD54 activities. We find that the RAD54 N-terminal domain (NTD) is responsible for initiation of BM through two coupled, but distinct steps; specific binding to Holliday junctions and RAD54 oligomerization. Furthermore, we find that the RAD54 oligomeric state can be controlled by NTD phosphorylation at S49, a CDK2 consensus site, which inhibits RAD54 oligomerization and, consequently, BM. Importantly, the effect of phosphorylation on RAD54 oligomerization is specific for BM, as it does not affect stimulation of RAD51 recombinase by RAD54. Thus, the transition of the oligomeric states provides an important control of the biological functions of RAD54 and, likely, other multifunctional proteins.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
DNA Helicases/metabolismo
DNA Cruciforme/metabolismo
Proteínas Nucleares/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sítios de Ligação/genética
Linhagem Celular
DNA Helicases/química
DNA Helicases/genética
Reparo do DNA
DNA Cruciforme/química
DNA Cruciforme/genética
Seres Humanos
Hidrólise
Proteínas Nucleares/química
Proteínas Nucleares/genética
Conformação de Ácido Nucleico
Fosforilação
Multimerização Proteica
Recombinação Genética
Homologia de Sequência de Aminoácidos
Células Sf9
Spodoptera
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (DNA, Cruciform); 0 (Nuclear Proteins); 0 (RAD54L protein, human); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.- (DNA Helicases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180104
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02497-x


  3 / 40588 MEDLINE  
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[PMID]:29371594
[Au] Autor:Rhee S; Chung JI; King DA; D'amato G; Paik DT; Duan A; Chang A; Nagelberg D; Sharma B; Jeong Y; Diehn M; Wu JC; Morrison AJ; Red-Horse K
[Ad] Endereço:Department of Biology, Stanford University, 371 Serra Mall, Stanford, CA, 94305, USA.
[Ti] Título:Endothelial deletion of Ino80 disrupts coronary angiogenesis and causes congenital heart disease.
[So] Source:Nat Commun;9(1):368, 2018 01 25.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:During development, the formation of a mature, well-functioning heart requires transformation of the ventricular wall from a loose trabecular network into a dense compact myocardium at mid-gestation. Failure to compact is associated in humans with congenital diseases such as left ventricular non-compaction (LVNC). The mechanisms regulating myocardial compaction are however still poorly understood. Here, we show that deletion of the Ino80 chromatin remodeler in vascular endothelial cells prevents ventricular compaction in the developing mouse heart. This correlates with defective coronary vascularization, and specific deletion of Ino80 in the two major coronary progenitor tissues-sinus venosus and endocardium-causes intermediate phenotypes. In vitro, endothelial cells promote myocardial expansion independently of blood flow in an Ino80-dependent manner. Ino80 deletion increases the expression of E2F-activated genes and endothelial cell S-phase occupancy. Thus, Ino80 is essential for coronary angiogenesis and allows coronary vessels to support proper compaction of the heart wall.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Endotélio Vascular/metabolismo
Cardiopatias Congênitas/metabolismo
Neovascularização Patológica/metabolismo
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Animais
Vasos Coronários/metabolismo
DNA Helicases/genética
DNA Helicases/metabolismo
Endocárdio/metabolismo
Endocárdio/patologia
Células Endoteliais/enzimologia
Células Endoteliais/metabolismo
Endotélio Vascular/patologia
Cardiopatias Congênitas/genética
Ventrículos do Coração/metabolismo
Ventrículos do Coração/patologia
Seres Humanos
Camundongos Knockout
Camundongos Transgênicos
Miocárdio/metabolismo
Miocárdio/patologia
Neovascularização Patológica/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (INO80 protein, mouse); EC 3.6.4.- (DNA Helicases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180127
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02796-3


  4 / 40588 MEDLINE  
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[PMID]:29281637
[Au] Autor:Boot M; van Winden VJC; Sparrius M; van de Weerd R; Speer A; Ummels R; Rustad T; Sherman DR; Bitter W
[Ad] Endereço:Department of Medical Microbiology and Infection Control, VU University Medical Center, Amsterdam, the Netherlands.
[Ti] Título:Cell envelope stress in mycobacteria is regulated by the novel signal transduction ATPase IniR in response to trehalose.
[So] Source:PLoS Genet;13(12):e1007131, 2017 12.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cell envelope of mycobacteria is a highly unique and complex structure that is functionally equivalent to that of Gram-negative bacteria to protect the bacterial cell. Defects in the integrity or assembly of this cell envelope must be sensed to allow the induction of stress response systems. The promoter that is specifically and most strongly induced upon exposure to ethambutol and isoniazid, first line drugs that affect cell envelope biogenesis, is the iniBAC promoter. In this study, we set out to identify the regulator of the iniBAC operon in Mycobacterium marinum using an unbiased transposon mutagenesis screen in a constitutively iniBAC-expressing mutant background. We obtained multiple mutants in the mce1 locus as well as mutants in an uncharacterized putative transcriptional regulator (MMAR_0612). This latter gene was shown to function as the iniBAC regulator, as overexpression resulted in constitutive iniBAC induction, whereas a knockout mutant was unable to respond to the presence of ethambutol and isoniazid. Experiments with the M. tuberculosis homologue (Rv0339c) showed identical results. RNAseq experiments showed that this regulatory gene was exclusively involved in the regulation of the iniBAC operon. We therefore propose to name this dedicated regulator iniBAC Regulator (IniR). IniR belongs to the family of signal transduction ATPases with numerous domains, including a putative sugar-binding domain. Upon testing different sugars, we identified trehalose as an activator and metabolic cue for iniBAC activation, which could also explain the effect of the mce1 mutations. In conclusion, cell envelope stress in mycobacteria is regulated by IniR in a cascade that includes trehalose.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/genética
Mycobacterium marinum/genética
Mycobacterium marinum/metabolismo
Trealose/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Membrana Celular/metabolismo
Parede Celular/genética
Parede Celular/metabolismo
Elementos de DNA Transponíveis
Regulação Bacteriana da Expressão Gênica
Genes Bacterianos
Mutagênese Insercional
Óperon
Regiões Promotoras Genéticas
Transdução de Sinais
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA Transposable Elements); B8WCK70T7I (Trehalose); EC 3.6.1.- (Adenosine Triphosphatases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171228
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007131


  5 / 40588 MEDLINE  
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[PMID]:29372964
[Au] Autor:Evstiukhina TA; Alekseeva EA; Fedorov DV; Peshekhonov VT; Korolev VG
[Ti] Título:[The role of remodeling complexes CHD1 and ISWI in spontaneous and UV-induced mutagenesis control in yeast Saccharomyces cerevisiae].
[So] Source:Genetika;53(2):173-80, 2017 Feb.
[Is] ISSN:0016-6758
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:Chromatin remodulators are special multiprotein machines capable of transforming the structure, constitution, and positioning of nucleosomes on DNA. Biochemical activities of remodeling complexes CHD1 and ISWI from the SWI2/SNF2 family are well established. They ensure correct positioning of nucleosomes along the genome, which is probably critical for genome stability, in particular, after action of polymerases, repair enzymes, and transcription. In this paper, we show that single mutations in genes ISW1, ISW2, and CHD1 weakly affect repair and mutagenic processes in yeast cells. At the same time, there are differences in the effect of these mutations on spontaneous mutation levels, which indicates certain specificity of action of protein complexes ISW1, ISW2, and CHD1 on expression of different genes that control repair and mutation processes in yeast.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Proteínas de Ligação a DNA/metabolismo
Mutagênese/efeitos da radiação
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
Fatores de Transcrição/metabolismo
Raios Ultravioleta
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Proteínas de Ligação a DNA/genética
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CHD1 protein, S cerevisiae); 0 (DNA-Binding Proteins); 0 (ISWI protein); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factors); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (ISW1 protein, S cerevisiae)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180127
[St] Status:MEDLINE


  6 / 40588 MEDLINE  
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[PMID]:29321502
[Au] Autor:Gardner BM; Castanzo DT; Chowdhury S; Stjepanovic G; Stefely MS; Hurley JH; Lander GC; Martin A
[Ad] Endereço:Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA, 94720, USA.
[Ti] Título:The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading.
[So] Source:Nat Commun;9(1):135, 2018 01 10.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Pex1 and Pex6 form a heterohexameric motor essential for peroxisome biogenesis and function, and mutations in these AAA-ATPases cause most peroxisome-biogenesis disorders in humans. The tail-anchored protein Pex15 recruits Pex1/Pex6 to the peroxisomal membrane, where it performs an unknown function required for matrix-protein import. Here we determine that Pex1/Pex6 from S. cerevisiae is a protein translocase that unfolds Pex15 in a pore-loop-dependent and ATP-hydrolysis-dependent manner. Our structural studies of Pex15 in isolation and in complex with Pex1/Pex6 illustrate that Pex15 binds the N-terminal domains of Pex6, before its C-terminal disordered region engages with the pore loops of the motor, which then processively threads Pex15 through the central pore. Furthermore, Pex15 directly binds the cargo receptor Pex5, linking Pex1/Pex6 to other components of the peroxisomal import machinery. Our results thus support a role of Pex1/Pex6 in mechanical unfolding of peroxins or their extraction from the peroxisomal membrane during matrix-protein import.
[Mh] Termos MeSH primário: ATPases Associadas a Diversas Atividades Celulares/metabolismo
Proteínas de Membrana/metabolismo
Peroxissomos/enzimologia
Fosfoproteínas/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/antagonistas & inibidores
Conformação Proteica
Saccharomyces cerevisiae
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (PEX15 protein, S cerevisiae); 0 (Phosphoproteins); 0 (Saccharomyces cerevisiae Proteins); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities); EC 3.6.4.- (PEX1 protein, S cerevisiae); EC 3.6.4.- (PEX6 protein, S cerevisiae)
[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:180112
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02474-4


  7 / 40588 MEDLINE  
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[PMID]:29282978
[Au] Autor:Li L; Fu Q; Xia M; Xin L; Shen H; Li G; Ji G; Meng Q; Xie Y
[Ad] Endereço:Research Center for Health and Nutrition, Shanghai University of Traditional Chinese Medicine , Shanghai 201203, China.
[Ti] Título:Inhibition of P-Glycoprotein Mediated Efflux in Caco-2 Cells by Phytic Acid.
[So] Source:J Agric Food Chem;66(4):988-998, 2018 Jan 31.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phytic acid (IP6) is a natural phosphorylated inositol, which is abundantly present in most cereal grains and seeds. This study investigated the effects of IP6 regulation on P-glycoprotein (P-gp) and its potential mechanisms using in situ and in vitro models. The effective permeability of the typical P-gp substrate rhodamine 123 (R123) in colon was significantly increased from (1.69 ± 0.22) × 10 cm/s in the control group to (3.39 ± 0.417) × 10 cm/s (p < 0.01) in the 3.5 mM IP6 group. Additionally, IP6 can concentration-dependently decrease the R123 efflux ratio in both Caco-2 and MDCK II-MDR1 cell monolayers and increase intracellular R123 accumulation in Caco-2 cells. Furthermore, IP6 noncompetitively inhibited P-gp by impacting R123 efflux kinetics. The noncompetitive inhibition of P-gp by IP6 was likely due to decreases in P-gp ATPase activity and P-gp molecular conformational changes induced by IP6. In summary, IP6 is a promising P-gp inhibitor candidate.
[Mh] Termos MeSH primário: Membro 1 da Subfamília B de Cassetes de Ligação de ATP/antagonistas & inibidores
Ácido Fítico/farmacologia
[Mh] Termos MeSH secundário: Membro 1 da Subfamília B de Cassetes de Ligação de ATP/química
Membro 1 da Subfamília B de Cassetes de Ligação de ATP/genética
Adenosina Trifosfatases/metabolismo
Regulação Alostérica
Animais
Transporte Biológico/efeitos dos fármacos
Células CACO-2
Permeabilidade da Membrana Celular/efeitos dos fármacos
Colo/metabolismo
Cães
Seres Humanos
Rim/metabolismo
Células Madin Darby de Rim Canino
Conformação Molecular/efeitos dos fármacos
RNA Mensageiro/análise
Ratos
Ratos Sprague-Dawley
Rodamina 123/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ATP-Binding Cassette, Sub-Family B, Member 1); 0 (RNA, Messenger); 1N3CZ14C5O (Rhodamine 123); 7IGF0S7R8I (Phytic Acid); EC 3.6.1.- (Adenosine Triphosphatases)
[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:171229
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b04307


  8 / 40588 MEDLINE  
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[PMID]:29240795
[Au] Autor:Ferreira MJ; Mendes AL; de Sá-Nogueira I
[Ad] Endereço:UCIBIO, REQUIMTE, Departamento de Ciências da Vida, Faculdade de Ciências e Tecnologia, Universidade NOVA de Lisboa, Caparica, Portugal.
[Ti] Título:The MsmX ATPase plays a crucial role in pectin mobilization by Bacillus subtilis.
[So] Source:PLoS One;12(12):e0189483, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Carbohydrates from plant cell walls are often found as heteropolysaccharides intertwined with each other. For competitive advantage against other microorganisms, and ability to fully exploit available carbon and energy sources, Bacillus subtilis possesses a high number of proteins dedicated to the uptake of mono- and oligosaccharides. Here, we characterize transporter complexes, belonging to the ATP-binding cassette (ABC) superfamily, involved in the uptake of oligosaccharides commonly found in pectin. The uptake of these carbohydrates is shown to be MsmX-dependent, assigning a key role in pectin mobilization for MsmX, a multipurpose ATPase serving several distinct ABC-type I sugar importers. Mutagenesis analysis of the transmembrane domains of the AraNPQ MsmX-dependent importer revealed putative residues for MsmX interaction. Interestingly however, although MsmX is shown to be essential for energizing various ABC transporters we found that a second B. subtilis ATPase, YurJ, is able to complement its function when placed in trans at a different locus of the chromosome.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Bacillus subtilis/metabolismo
Pectinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pectins); 89NA02M4RX (pectin); EC 3.6.1.- (Adenosine Triphosphatases)
[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:171215
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189483


  9 / 40588 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


  10 / 40588 MEDLINE  
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[PMID]:29206865
[Au] Autor:Dani P; Ujaoney AK; Apte SK; Basu B
[Ad] Endereço:Molecular Biology Division, Bhabha Atomic Research Centre, Mumbai, India.
[Ti] Título:Regulation of potassium dependent ATPase (kdp) operon of Deinococcus radiodurans.
[So] Source:PLoS One;12(12):e0188998, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The genome of D. radiodurans harbors genes for structural and regulatory proteins of Kdp ATPase, in an operon pattern, on Mega plasmid 1. Organization of its two-component regulatory genes is unique. Here we demonstrate that both, the structural as well as regulatory components of the kdp operon of D. radiodurans are expressed quickly as the cells experience potassium limitation but are not expressed upon increase in osmolarity. The cognate DNA binding response regulator (RR) effects the expression of kdp operon during potassium deficiency through specific interaction with the kdp promoter. Deletion of the gene encoding RR protein renders the mutant D. radiodurans (ΔRR) unable to express kdp operon under potassium limitation. The ΔRR D. radiodurans displays no growth defect when grown on rich media or when exposed to oxidative or heat stress but shows reduced growth following gamma irradiation. The study elucidates the functional and regulatory aspects of the novel kdp operon of this extremophile, for the first time.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Deinococcus/genética
Óperon
Potássio/metabolismo
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Deinococcus/crescimento & desenvolvimento
Ensaio de Desvio de Mobilidade Eletroforética
Genes Bacterianos
Pressão Osmótica
Estresse Fisiológico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.1.- (Adenosine Triphosphatases); RWP5GA015D (Potassium)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188998



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