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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


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[PMID]:28247940
[Au] Autor:Olli KE; Li K; Galileo DS; Martin-DeLeon PA
[Ad] Endereço:Department of Biological Sciences, University of Delaware, Newark, Delaware.
[Ti] Título:Plasma membrane calcium ATPase 4 (PMCA4) co-ordinates calcium and nitric oxide signaling in regulating murine sperm functional activity.
[So] Source:J Cell Physiol;233(1):11-22, 2018 Jan.
[Is] ISSN:1097-4652
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Reduced sperm motility (asthenospermia) and resulting infertility arise from deletion of the Plasma Membrane Ca -ATPase 4 (Pmca4) gene which encodes the highly conserved Ca efflux pump, PMCA4. This is the major Ca clearance protein in murine sperm. Since the mechanism underlying asthenospermia in PMCA4's absence or reduced activity is unknown, we investigated if sperm PMCA4 negatively regulates nitric oxide synthases (NOSs) and when absent NO, peroxynitrite, and oxidative stress levels are increased. Using co-immunoprecipitation (Co-IP) and Fluorescence Resonance Energy Transfer (FRET), we show an association of PMCA4 with the NOSs in elevated cytosolic [Ca ] in capacitated and Ca ionophore-treated sperm and with neuronal (nNOS) at basal [Ca ] (ucapacitated sperm). FRET efficiencies for PMCA4-eNOS were 35% and 23% in capacitated and uncapacitated sperm, significantly (p < 0.01) different, with the molecules being <10 nm apart. For PMCA4-nNOS, this interaction was seen only for capacitated sperm where FRET efficiency was 24%, significantly (p < 0.05) higher than in uncapacitated sperm (6%). PMCA4 and the NOSs were identified as interacting partners in a quaternary complex that includes Caveolin1, which co-immunoprecipitated with eNOS in a Ca -dependent manner. In Pmca4 sperm NOS activity was elevated twofold in capacitated/uncapacitated sperm (vs. wild-type), accompanied by a twofold increase in peroxynitrite levels and significantly (p < 0.001) increased numbers of apoptotic germ cells. The data support a quaternary complex model in which PMCA4 co-ordinates Ca and NO signaling to maintain motility, with increased NO levels resulting in asthenospermia in Pmca4 males. They suggest the involvement of PMCA4 mutations in human asthenospermia, with diagnostic relevance.
[Mh] Termos MeSH primário: Astenozoospermia/enzimologia
Sinalização do Cálcio
ATPases Transportadoras de Cálcio/metabolismo
Membrana Celular/enzimologia
Óxido Nítrico/metabolismo
Motilidade Espermática
Espermatozoides/enzimologia
[Mh] Termos MeSH secundário: Animais
Apoptose
Astenozoospermia/genética
Astenozoospermia/patologia
Astenozoospermia/fisiopatologia
ATPases Transportadoras de Cálcio/deficiência
ATPases Transportadoras de Cálcio/genética
Caveolina 1/metabolismo
Fertilidade
Transferência Ressonante de Energia de Fluorescência
Predisposição Genética para Doença
Masculino
Camundongos Endogâmicos C57BL
Camundongos Endogâmicos ICR
Camundongos Knockout
Complexos Multienzimáticos
Óxido Nítrico Sintase Tipo I/metabolismo
Óxido Nítrico Sintase Tipo III/metabolismo
Estresse Oxidativo
Ácido Peroxinitroso/metabolismo
Fenótipo
Espermatozoides/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cav1 protein, mouse); 0 (Caveolin 1); 0 (Multienzyme Complexes); 14691-52-2 (Peroxynitrous Acid); 31C4KY9ESH (Nitric Oxide); EC 1.14.13.39 (Nitric Oxide Synthase Type I); EC 1.14.13.39 (Nitric Oxide Synthase Type III); EC 1.14.13.39 (Nos1 protein, mouse); EC 1.14.13.39 (Nos3 protein, mouse); EC 3.6.3.8 (Calcium-Transporting ATPases); EC 3.6.3.8 (PMCA4 protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180124
[Lr] Data última revisão:
180124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170302
[St] Status:MEDLINE
[do] DOI:10.1002/jcp.25882


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[PMID]:29236392
[Au] Autor:Rudnytska MV; Palladina TA
[Ti] Título:Effect of preparations Methyure and Ivine on Са(2+)-ATPases activity in plasma and vacuolar membrane of corn seedling roots under salt stress conditions.
[So] Source:Ukr Biochem J;89(1):76-81, 2017 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:Ca2+-ATPases regulate the functioning of Ca2+-dependent signaling pathway SOS which provides removal of Na+ from the cytoplasm of cells via Na+/H+-antiporters in saline conditions. The influence of synthetic preparations Methyure and Ivine on the Ca2+-ATPase activity was investigated. It was shown that exposition of corn seedlings in the presence of 0.1 M NaCl rather enhanced hydrolytic than transport activity of Ca2+-ATPases in plasma and vacuolar membrane of root cells. It was found that seed treatment with such preparations, especially Methyure, caused intensification of the both activities of Ca2+-ATPases, mainly in vacuolar membrane. The results indicate than salt protective activity of preparations, especially Methyure, is associated with increased Ca2+-ATPase activity, which regulates the functioning of Na+/H+-antiporters.
[Mh] Termos MeSH primário: ATPases Transportadoras de Cálcio/metabolismo
Membrana Celular/efeitos dos fármacos
Substâncias Protetoras/farmacologia
Pirimidinas/farmacologia
Trocadores de Sódio-Hidrogênio/metabolismo
Vacúolos/efeitos dos fármacos
Zea mays/efeitos dos fármacos
[Mh] Termos MeSH secundário: Adaptação Fisiológica
Membrana Celular/metabolismo
Membranas Intracelulares/efeitos dos fármacos
Membranas Intracelulares/metabolismo
Transporte de Íons
Células Vegetais/efeitos dos fármacos
Células Vegetais/metabolismo
Raízes de Plantas/efeitos dos fármacos
Raízes de Plantas/metabolismo
Salinidade
Plântulas/efeitos dos fármacos
Plântulas/metabolismo
Cloreto de Sódio/farmacologia
Trocadores de Sódio-Hidrogênio/agonistas
Estresse Fisiológico
Vacúolos/metabolismo
Zea mays/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protective Agents); 0 (Pyrimidines); 0 (Sodium-Hydrogen Exchangers); 451W47IQ8X (Sodium Chloride); EC 3.6.3.8 (Calcium-Transporting ATPases)
[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/ubj89.01.076


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[PMID]:28726644
[Au] Autor:Astegno A; Bonza MC; Vallone R; La Verde V; D'Onofrio M; Luoni L; Molesini B; Dominici P
[Ad] Endereço:From the Department of Biotechnology, University of Verona, Strada Le Grazie 15, 37134 Verona, Italy and alessandra.astegno@univr.it.
[Ti] Título: calmodulin-like protein CML36 is a calcium (Ca ) sensor that interacts with the plasma membrane Ca -ATPase isoform ACA8 and stimulates its activity.
[So] Source:J Biol Chem;292(36):15049-15061, 2017 Sep 08.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Calmodulin-like (CML) proteins are major EF-hand-containing, calcium (Ca )-binding proteins with crucial roles in plant development and in coordinating plant stress tolerance. Given their abundance in plants, the properties of Ca sensors and identification of novel target proteins of CMLs deserve special attention. To this end, we recombinantly produced and biochemically characterized CML36 from We analyzed Ca and Mg binding to the individual EF-hands, observed metal-induced conformational changes, and identified a physiologically relevant target. CML36 possesses two high-affinity Ca /Mg mixed binding sites and two low-affinity Ca -specific sites. Binding of Ca induced an increase in the α-helical content and a conformational change that lead to the exposure of hydrophobic regions responsible for target protein recognition. Cation binding, either Ca or Mg , stabilized the secondary and tertiary structures of CML36, guiding a large structural transition from a molten globule apo-state to a compact holoconformation. Importantly, through binding and activity assays, we showed that CML36 interacts directly with the regulative N terminus of the plasma membrane Ca -ATPase isoform 8 (ACA8) and that this interaction stimulates ACA8 activity. Gene expression analysis revealed that and are co-expressed mainly in inflorescences. Collectively, our results support a role for CML36 as a Ca sensor that binds to and modulates ACA8, uncovering a possible involvement of the CML protein family in the modulation of plant-autoinhibited Ca pumps.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/química
ATPases Transportadoras de Cálcio/metabolismo
Cálcio/metabolismo
Calmodulina/metabolismo
Membrana Celular/enzimologia
[Mh] Termos MeSH secundário: Arabidopsis/enzimologia
Proteínas de Arabidopsis/genética
Calmodulina/genética
Ativação Enzimática
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (CML36 protein, Arabidopsis); 0 (Calmodulin); EC 3.6.3.8 (Aca8 protein, Arabidopsis); EC 3.6.3.8 (Calcium-Transporting ATPases); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170721
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.787796


  5 / 10940 MEDLINE  
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[PMID]:28714864
[Au] Autor:Lessard S; Gatof ES; Beaudoin M; Schupp PG; Sher F; Ali A; Prehar S; Kurita R; Nakamura Y; Baena E; Ledoux J; Oceandy D; Bauer DE; Lettre G
[Ad] Endereço:Montreal Heart Institute and Université de Montréal, Montréal, Québec, Canada.
[Ti] Título:An erythroid-specific ATP2B4 enhancer mediates red blood cell hydration and malaria susceptibility.
[So] Source:J Clin Invest;127(8):3065-3074, 2017 Aug 01.
[Is] ISSN:1558-8238
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The lack of mechanistic explanations for many genotype-phenotype associations identified by GWAS precludes thorough assessment of their impact on human health. Here, we conducted an expression quantitative trait locus (eQTL) mapping analysis in erythroblasts and found erythroid-specific eQTLs for ATP2B4, the main calcium ATPase of red blood cells (rbc). The same SNPs were previously associated with mean corpuscular hemoglobin concentration (MCHC) and susceptibility to severe malaria infection. We showed that Atp2b4-/- mice demonstrate increased MCHC, confirming ATP2B4 as the causal gene at this GWAS locus. Using CRISPR-Cas9, we fine mapped the genetic signal to an erythroid-specific enhancer of ATP2B4. Erythroid cells with a deletion of the ATP2B4 enhancer had abnormally high intracellular calcium levels. These results illustrate the power of combined transcriptomic, epigenomic, and genome-editing approaches in characterizing noncoding regulatory elements in phenotype-relevant cells. Our study supports ATP2B4 as a potential target for modulating rbc hydration in erythroid disorders and malaria infection.
[Mh] Termos MeSH primário: ATPases Transportadoras de Cálcio/genética
Eritrócitos/citologia
Predisposição Genética para Doença
Malária/genética
ATPases Transportadoras de Cálcio da Membrana Plasmática/genética
[Mh] Termos MeSH secundário: Animais
Sistemas CRISPR-Cas
Cálcio/metabolismo
ATPases Transportadoras de Cálcio/metabolismo
Mapeamento Cromossômico
Elementos Facilitadores Genéticos
Epigenômica
Eritroblastos/metabolismo
Perfilação da Expressão Gênica
Redes Reguladoras de Genes
Estudo de Associação Genômica Ampla
Células HEK293
Seres Humanos
Malária/metabolismo
Masculino
Camundongos
Camundongos Transgênicos
Fenótipo
ATPases Transportadoras de Cálcio da Membrana Plasmática/metabolismo
Polimorfismo de Nucleotídeo Único
Locos de Características Quantitativas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.1.8 (ATP2B4 protein, human); EC 3.6.3.8 (Calcium-Transporting ATPases); EC 3.6.3.8 (PMCA4 protein, mouse); EC 3.6.3.8 (Plasma Membrane Calcium-Transporting ATPases); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE


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[PMID]:28692648
[Au] Autor:Xia Z; Wei J; Li Y; Wang J; Li W; Wang K; Hong X; Zhao L; Chen C; Min J; Wang F
[Ad] Endereço:Nutrition Discovery Innovation Center, Institute of Nutrition and Food Safety, School of Public Health, The First Affiliated Hospital, Institute of Translational Medicine, The Children's Hospital, Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, School of Medicine,
[Ti] Título:Zebrafish slc30a10 deficiency revealed a novel compensatory mechanism of Atp2c1 in maintaining manganese homeostasis.
[So] Source:PLoS Genet;13(7):e1006892, 2017 Jul.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent studies found that mutations in the human SLC30A10 gene, which encodes a manganese (Mn) efflux transporter, are associated with hypermanganesemia with dystonia, polycythemia, and cirrhosis (HMDPC). However, the relationship between Mn metabolism and HMDPC is poorly understood, and no specific treatments are available for this disorder. Here, we generated two zebrafish slc30a10 mutant lines using the CRISPR/Cas9 system. Compared to wild-type animals, mutant adult animals developed significantly higher systemic Mn levels, and Mn accumulated in the brain and liver of mutant embryos in response to exogenous Mn. Interestingly, slc30a10 mutants developed neurological deficits in adulthood, as well as environmental Mn-induced manganism in the embryonic stage; moreover, mutant animals had impaired dopaminergic and GABAergic signaling. Finally, mutant animals developed steatosis, liver fibrosis, and polycythemia accompanied by increased epo expression. This phenotype was rescued partially by EDTA- CaNa2 chelation therapy and iron supplementation. Interestingly, prior to the onset of slc30a10 expression, expressing ATP2C1 (ATPase secretory pathway Ca2+ transporting 1) protected mutant embryos from Mn exposure, suggesting a compensatory role for Atp2c1 in the absence of Slc30a10. Notably, expressing either wild-type or mutant forms of SLC30A10 was sufficient to inhibit the effect of ATP2C1 in response to Mn challenge in both zebrafish embryos and HeLa cells. These findings suggest that either activating ATP2C1 or restoring the Mn-induced trafficking of ATP2C1 can reduce Mn accumulation, providing a possible target for treating HMDPC.
[Mh] Termos MeSH primário: ATPases Transportadoras de Cálcio/genética
Proteínas de Transporte de Cátions/genética
Homeostase/genética
Manganês/metabolismo
Doenças Metabólicas/genética
[Mh] Termos MeSH secundário: Animais
Encéfalo/metabolismo
Encéfalo/patologia
Sistemas CRISPR-Cas
Proteínas de Transporte de Cátions/deficiência
Genótipo
Células HeLa
Seres Humanos
Doenças Metabólicas/metabolismo
Doenças Metabólicas/patologia
Mutação
Peixe-Zebra/genética
Transportador 8 de Zinco
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cation Transport Proteins); 0 (SLC30A8 protein, human); 0 (Zinc Transporter 8); 42Z2K6ZL8P (Manganese); EC 3.6.3.8 (ATP2C1 protein, human); EC 3.6.3.8 (Calcium-Transporting ATPases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170711
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006892


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[PMID]:28648117
[Au] Autor:Fodor J; Gomba-Tóth A; Oláh T; Zádor E; Tóth ZC; Ioannis I; Molnár B; Kovács I; Csernoch L
[Ad] Endereço:1 Department of Physiology, Faculty of Medicine, University of Debrecen , Debrecen, Hungary.
[Ti] Título:Alteration of sarcoplasmic reticulum Ca ATPase expression in lower limb ischemia caused by atherosclerosis obliterans.
[So] Source:Physiol Int;104(2):183-192, 2017 Jun 01.
[Is] ISSN:2498-602X
[Cp] País de publicação:Hungary
[La] Idioma:eng
[Ab] Resumo:Atherosclerosis is a disease caused by a build-up of fatty plaques and cholesterol in the arteries. The lumen of the vessels is obliterated resulting in restricted blood supply to tissues. In ischemic conditions, the cytosolic Ca level of skeletal muscle may increase, indicating the alteration of Ca removal mechanisms. Ca is transported from cytosol into the sarcoplasmic reticulum by Ca ATPase (SERCA), with its 1a isoform expressed in adult, while its 1b isoform in neonatal and regenerating fast-twitch skeletal muscle. To investigate the role of these isoforms in ischemic skeletal muscle, biopsies from musculus biceps femoris of patients who underwent amputation due to atherosclerosis were examined. Samples were removed from the visibly healthy and hypoxia-affected tissue. Significantly increased SERCA1a expression was detected under the ischemic conditions (246 ± 69%; p < 0.05) compared with the healthy tissue. Furthermore, the ratio of SERCA1a-positive fibers was slightly increased (46 ± 4% in healthy tissue and 60 ± 5% in ischemic tissue; p > 0.05), whereas SERCA2a did not change. In addition, in primary cultures derived from hypoxia-affected tissue, the diameter and fusion index of myotubes were significantly increased (30 ± 1.6 µm vs. 41 ± 2.4 µm and 31 ± 4% vs. 45 ± 3%; p < 0.05). We propose that the increased SERCA1a expression indicates the existence and location of compensating mechanisms in ischemic muscle.
[Mh] Termos MeSH primário: Aterosclerose/enzimologia
Isquemia/enzimologia
Fibras Musculares Esqueléticas/enzimologia
Fibras Musculares Esqueléticas/patologia
Músculo Esquelético/enzimologia
ATPases Transportadoras de Cálcio do Retículo Sarcoplasmático/metabolismo
Retículo Sarcoplasmático/enzimologia
[Mh] Termos MeSH secundário: Idoso
Aterosclerose/patologia
Cálcio/metabolismo
Sinalização do Cálcio
ATPases Transportadoras de Cálcio/metabolismo
Feminino
Seres Humanos
Extremidade Inferior/irrigação sanguínea
Masculino
Retículo Sarcoplasmático/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.3.8 (Calcium-Transporting ATPases); EC 3.6.3.8 (Sarcoplasmic Reticulum Calcium-Transporting ATPases); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170914
[Lr] Data última revisão:
170914
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170627
[St] Status:MEDLINE
[do] DOI:10.1556/2060.104.2017.2.1


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[PMID]:28641207
[Au] Autor:Zhang X; Tang X; Wang M; Zhang W; Zhou B; Wang Y
[Ad] Endereço:Department of Marine Ecology, College of Marine Life Sciences, Ocean University of China, Qingdao, China.
[Ti] Título:ROS and calcium signaling mediated pathways involved in stress responses of the marine microalgae Dunaliella salina to enhanced UV-B radiation.
[So] Source:J Photochem Photobiol B;173:360-367, 2017 Aug.
[Is] ISSN:1873-2682
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:UV-B ray has been addressed to trigger common metabolic responses on marine microalgae, however, the upstream events responsible for these changes in marine microalgae are poorly understood. In the present study, a species of marine green microalgae Dunaliella salina was exposed to a series of enhanced UV-B radiation ranging from 0.25 to 1.00 KJ·m per day. The role of ROS and calcium signaling in the D. salina responses to UV-B was discussed. Results showed that enhanced UV-B radiation markedly decreased the cell density in a dose-dependent manner, but the contents of protein and glycerol that were essential for cell growth increased. It suggested that it was cell division instead of cell growth that UV-B exerted negative effects on. The subcellular damages on nuclei and plasmalemma further evidenced the hypothesis. The nutrient absorption was affected with UV-B exposure, and the inhibition on PO uptake was more serious compared to NO uptake. UV-B radiation promoted reactive oxygen species (ROS) formation and thiobarbituric acid reactive substances (TBARS) contents, decreased the redox status and altered the antioxidant enzyme activities. The addition of the ROS scavenger and the glutathione biosynthesis precursor N-acetyl-l-cysteine (NAC) alleviated the stress degree, implying ROS-mediated pathway was involved in the stress response to UV-B radiation. Transient increase in Ca -ATPase was triggered simultaneously with UV-B exposure. Meanwhile, the addition of an intracellular free calcium chelator aggravated the damage of cell division, but exogenous calcium and ion channel blocker applications did not, inferring that endogenously initiated calcium signaling played roles in response to UV-B. Cross-talk analysis showed a relatively clear relationship between ROS inhibition and Ca -ATPase suppression, and a relation between Ca inhibition and GPx activity change was also observed. It was thus presumed that ROS-coupled calcium signaling via the glutathione cycle was involved in the response of marine microalgae to UV-B stimuli.
[Mh] Termos MeSH primário: Sinalização do Cálcio/efeitos da radiação
Microalgas/efeitos da radiação
Estresse Oxidativo/efeitos da radiação
Espécies Reativas de Oxigênio/metabolismo
Raios Ultravioleta/efeitos adversos
Volvocida/efeitos da radiação
[Mh] Termos MeSH secundário: Acetilcisteína/metabolismo
Antioxidantes/metabolismo
Transporte Biológico/efeitos da radiação
ATPases Transportadoras de Cálcio/metabolismo
Glutationa/biossíntese
Microalgas/citologia
Microalgas/metabolismo
Volvocida/citologia
Volvocida/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Reactive Oxygen Species); EC 3.6.3.8 (Calcium-Transporting ATPases); GAN16C9B8O (Glutathione); WYQ7N0BPYC (Acetylcysteine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE


  9 / 10940 MEDLINE  
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[PMID]:28631341
[Au] Autor:Nareshkumar B; Akbar SM; Sharma HC; Jayalakshmi SK; Sreeramulu K
[Ad] Endereço:Department of Biochemistry, Gulbarga University, Gulbarga, Karnataka, India.
[Ti] Título:Evaluation of flubendiamide-induced mitochondrial dysfunction and metabolic changes in Helicoverpa armigera (Hubner).
[So] Source:Arch Insect Biochem Physiol;96(1), 2017 Sep.
[Is] ISSN:1520-6327
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phthalic acid diamide insecticides are the most effective insecticides used against most of the lepidopteran pests including Helicoverpa armigera, a polyphagous pest posing threat to several crops worldwide. The present studies were undertaken to understand different target sites and their interaction with insect ryanodine receptors (RyR). Bioassays indicated that flubendiamide inhibited the larval growth in dose-dependent manner with LD value of 0.72 µM, and at 0.8 µM larval growth decreased by about 88%. Flubendiamide accelerated the Ca -ATPase activity in dose-dependent trend, and at 0.8 µM, the activity was increased by 77.47%. Flubendiamide impedes mitochondrial function by interfering with complex I and F F -ATPase activity, and at 0.8 µM the inhibition was found to be about 92% and 50%, respectively. In vitro incubation of larval mitochondria with flubendiamide induced the efflux of cytochrome c, indicating the mitochondrial toxicity of the insecticide. Flubendiamide inhibited lactate dehydrogenase and the accumulation of H O , thereby preventing the cells from lipid peroxidation compared to control larvae. At 0.8 µM the LDH, H O content and lipid peroxidation was inhibited by 98.44, 70.81, and 70.81%, respectively. Cytochrome P450, general esterases, AChE, and antioxidant enzymes (catalase and superoxide dismutase) exhibited a dose-dependent increasing trend, whereas alkaline phosphatase and the midgut proteases, except amino peptidase, exhibited dose-dependent inhibition in insecticide-fed larvae. The results suggest that flubendiamide induced the harmful effects on the growth and development of H. armigera larvae by inducing mitochondrial dysfunction and inhibition of midgut proteases, along with its interaction with RyR.
[Mh] Termos MeSH primário: Benzamidas/toxicidade
Mitocôndrias/efeitos dos fármacos
Mariposas/efeitos dos fármacos
Sulfonas/toxicidade
[Mh] Termos MeSH secundário: Animais
Antioxidantes/metabolismo
ATPases Transportadoras de Cálcio/metabolismo
Citocromos c/secreção
Mitocôndrias/enzimologia
Mariposas/enzimologia
Estresse Oxidativo/efeitos dos fármacos
Peptídeo Hidrolases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Benzamides); 0 (Sulfones); 9007-43-6 (Cytochromes c); EC 3.4.- (Peptide Hydrolases); EC 3.6.3.8 (Calcium-Transporting ATPases); GEV84ZI4K6 (flubendiamide)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170621
[St] Status:MEDLINE
[do] DOI:10.1002/arch.21401


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[PMID]:28618103
[Au] Autor:Dang D; Prasad H; Rao R
[Ad] Endereço:Department of Physiology, The Johns Hopkins University School of Medicine, Baltimore, Maryland.
[Ti] Título:Secretory pathway Ca -ATPases promote in vitro microcalcifications in breast cancer cells.
[So] Source:Mol Carcinog;56(11):2474-2485, 2017 Nov.
[Is] ISSN:1098-2744
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Calcification of the breast is often an outward manifestation of underlying molecular changes that drive carcinogenesis. Up to 50% of all non-palpable breast tumors and 90% of ductal carcinoma in situ present with radiographically dense mineralization in mammographic scans. However, surprisingly little is known about the molecular pathways that lead to microcalcifications in the breast. Here, we report on a rapid and quantitative in vitro assay to monitor microcalcifications in breast cancer cell lines, including MCF7, MDA-MB-231, and Hs578T. We show that the Secretory Pathway Ca -ATPases SPCA1 and SPCA2 are strongly induced under osteogenic conditions that elicit microcalcifications. SPCA gene expression is significantly elevated in breast cancer subtypes that are associated with microcalcifications. Ectopic expression of SPCA genes drives microcalcifications and is dependent on pumping activity. Conversely, knockdown of SPCA expression significantly attenuates formation of microcalcifications. We propose that high levels of SPCA pumps may initiate mineralization in the secretory pathway by elevating luminal Ca . Our new findings offer mechanistic insight and functional implications on a widely observed, yet poorly understood radiographic signature of breast cancer.
[Mh] Termos MeSH primário: Neoplasias da Mama/metabolismo
Mama/metabolismo
Calcinose/metabolismo
ATPases Transportadoras de Cálcio/metabolismo
Cálcio/metabolismo
[Mh] Termos MeSH secundário: Mama/patologia
Neoplasias da Mama/genética
Neoplasias da Mama/patologia
Calcinose/genética
Calcinose/patologia
ATPases Transportadoras de Cálcio/genética
Linhagem Celular Tumoral
Feminino
Seres Humanos
Via Secretória
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.6.3.8 (ATP2C1 protein, human); EC 3.6.3.8 (ATP2C2 protein, human); EC 3.6.3.8 (Calcium-Transporting ATPases); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1002/mc.22695



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