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Pesquisa : D08.811.682.690.708.125 [Categoria DeCS]
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Id: biblio-1010394
Autor: Xie, Jian-Hui; Chai, Ting-Ting; Xu, Ran; Liu, Dan; Yang, Yu-Xiu; Deng, Zhi-Cheng; Jin, Hua; He, Hong.
Título: Induction of defense-related enzymes in patchouli inoculated with virulent Ralstonia solanacearum
Fonte: Electron. j. biotechnol;27:63-69, May. 2017. graf.
Idioma: en.
Projeto: National Natural Science Foundation of China; . Programs Foundation of Ministry of Education of China.
Resumo: Background: Defense-related anti-oxidative response is a vital defense mechanism of plants against pathogen invasion. Ralstonia solanacearum is an important phytopathogen. Bacterial wilt caused by R. solanacearum is the most destructive disease and causes severe losses in patchouli, an important aromatic and medicinal plant in Southeast Asia. The present study evaluated the defense response of patchouli inoculated with virulent R. solanacearum. Results: Results showed that the basic enzymatic activities differed not only between the leaves and stems but also between the upper and lower parts of the same organ of patchouli. POD, SOD, PPO, and PAL enzymatic activities were significantly elevated in leaves and stems from patchouli inoculated with R. solanacearum compared to those in control. The variation magnitude and rate of POD, PPO, and PAL activities were more obvious than those of SOD in patchouli inoculated with R. solanacearum. PAGE isoenzymatic analysis showed that there were one new POD band and two new SOD bands elicited, and at least two isoformic POD bands and two SOD bands were observably intensified compared to the corresponding control. Conclusion: Our results suggest that not only defense-related enzymatic activities were elevated but also the new isoenzymatic isoforms were induced in patchouli inoculated with R. solanacearum.
Descritores: Ralstonia solanacearum/patogenicidade
-Fenilalanina Amônia-Liase/metabolismo
Superóxido Dismutase/metabolismo
Catecol Oxidase/metabolismo
Ralstonia solanacearum/fisiologia
Eletroforese em Gel de Poliacrilamida
Eletroforese em Gel de Poliacrilamida Nativa
Responsável: CL1.1 - Biblioteca Central

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Id: biblio-889397
Autor: Faheem, Mehwish; Lone, Khalid Parvez.
Título: Oxidative stress and histopathologic biomarkers of exposure to bisphenol-A in the freshwater fish, Ctenopharyngodon idella
Fonte: Braz. J. Pharm. Sci. (Online);53(3):e17003, 2017. graf, ilus.
Idioma: en.
Resumo: ABSTRACT Bisphenol-A (BPA) belongs to the family of endocrine disrupting chemicals (EDCs) and it is used in the production of polycarbonate plastic and epoxy resins. The reproductive toxicity of BPA is well documented but it also exerts its toxic effects through multiple pathways especially by inducing a state of oxidative stress and causing damage to the vital organs. In the present study, histopathologic and oxidative damage caused by BPA in liver and kidneys of fresh water cyprinid, Ctenopharyngodon idella was evaluated. LC50 of BPA for Ctenopharyngodon idella was determined by probit regression analysis. Fish were exposed to a sublethal concentration of BPA i.e. 3.2 ppm (1/2 LC50) for 14 days. Histologic studies revealed that BPA caused degenerative changes in liver and kidneys and exposure of sublethal concentration of BPA caused oxidative damage in both organs. Lipid peroxidation significantly increased in liver and kidneys of treated group. Catalase activity and reduced glutathione content significantly decreased in the group exposed to BPA compared to control and glutathione-S-transferase activity increased significantly in both organs exposed to the sublethal concentration of BPA. From this study it is concluded that BPA caused toxic effects in fish species by changing oxidative balance and damaging the vital organs.
Descritores: Carpas
Estresse Oxidativo/imunologia
-Técnicas Histológicas
Catecol Oxidase/classificação
Limites: Animais
Responsável: BR40.1 - DBD - Divisão de Biblioteca e Documentacão do Conjunto das Químicas

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Texto completo SciELO Brasil
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Id: lil-755833
Autor: Itako, Adriana Terumi; Tolentino Júnior, João Batista; Silva Júnior, Tadeu Antônio Fernandes da; Soman, José Marcelo; Maringoni, Antonio Carlos.
Título: Chemical products induce resistance to Xanthomonas perforans in tomato
Fonte: Braz. j. microbiol;46(3):701-706, July-Sept. 2015. tab.
Idioma: en.
Projeto: FAPESP (The State of Sao Paulo Research Foundation); . National Council for the Improvement of Higher Education (CAPES).

The bacterial spot of tomato, caused by Xanthomonas spp., is a very important disease, especially in the hot and humid periods of the year. The chemical control of the disease has not been very effective for a number of reasons. This study aimed to evaluate, under greenhouse conditions, the efficacy of leaf-spraying chemicals (acibenzolar-S-methyl (ASM) (0.025 g.L−1), fluazinam (0.25 g.L−1), pyraclostrobin (0.08 g.L−1), pyraclostrobin + methiran (0.02 g.L−1 + 2.2 g.L−1), copper oxychloride (1.50 g.L−1), mancozeb + copper oxychloride (0.88 g.L−1 + 0.60 g.L−1), and oxytetracycline (0.40 g.L−1)) on control of bacterial spot. Tomatoes Santa Clara and Gisele cultivars were pulverized 3 days before inoculation with Xanthomonas perforans. The production of enzymes associated with resistance induction (peroxidase, polyphenol oxidase, phenylalanine ammonia-lyase, β-1,3-glucanase, and protease) was quantified from leaf samples collected 24 hours before and 24 hours after chemical spraying and at 1, 2, 4, 6, and 8 days after bacterial inoculation. All products tested controlled bacterial spot, but only ASM, pyraclostrobin, and pyraclostrobin + metiram increased the production of peroxidase in the leaves of the two tomato cultivars, and increased the production of polyphenol oxidase and β-1,3-glucanase in the Santa Clara cultivar.

Descritores: Resistência à Doença/efeitos dos fármacos
Fungicidas Industriais/farmacologia
Lycopersicon esculentum/microbiologia
Doenças das Plantas/microbiologia
Xanthomonas/crescimento & desenvolvimento
-Catecol Oxidase/metabolismo
Lycopersicon esculentum/enzimologia
Lycopersicon esculentum/imunologia
Peptídeo Hidrolases/metabolismo
Fenilalanina Amônia-Liase/metabolismo
Doenças das Plantas/imunologia
Xanthomonas/efeitos dos fármacos
Tipo de Publ: Research Support, Non-U.S. Gov't
Responsável: BR1.1 - BIREME

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Id: lil-161615
Autor: Gutierrez Correa, Jose; Biscardi, Ana Maria; Stoppani, Andres O. M.
Título: Inactivación de la lipoamida deshidrogenasa de miocardio por catecolaminas: protección por captopril y otros tioles / Inactivation of the myocardial lipoamide dehydrogenase by catecholamines: prevention by captopril and other thiol compounds
Fonte: Medicina (B.Aires);55(5/1):397-407, 1995. ilus, tab, graf.
Idioma: es.
Conferência: Apresentado em: Congresso Latinoamericano de Farmacología, 14, Santiago de Chile, 1994.
Resumo: Inactivation of lipoamide dehydrogenase (LipDH) by the Cu(II)/H2O2 Fenton system (SF-Cu(II): (5.0 microM Cu(II), 3.0 mM H2O2) was enhanced by catecholamines (CAs), namely, epinephrine, levoDOPA (DOPA), DOPAMINE, 6-hydroxyDOPAMINE (OH-DOPAMINE) and related compounds (DOPAC, CATECHOL, etc.). After 5 min incubation with the Cu(II)/H2O2/CA system (0,4 mM CA), the enzyme activity decayed as indicated by the following percentage values (mean +/- S.D.; in parenthesis, number of determinations): SF-Cu(II) alone, 43 +/- 10 (18); SF-Cu(II) + epinephrine, 80 +/- 9 (5); SF-Cu(II)'+ DOPA, 78 +/- 2 (4); SF + Cu(II) + DOPAMINE, 88 +/- 7 (5); SF-Cu(II) + OH-DOPAMINE 87 +/- 6 (7); SF-Cu(II) + DOPAC, 88 +/- 3 (6); SF-Cu(II) + catechol, 85 +/- 6 (5). In all cases P < 0,05, with respect to the SF-Cu(II) control sample. CAs effect was concentration-dependent and at the 0-100 microM concentration range, it varied with the CA structure. Above the 100 MicroM concentration, CAs were equally effective and produced 90-100 percent enzyme, inactivation (Figure 2). In the absence of oxy-radical generation, the enzyme specific activity (mean + S.D.) was 149 +/- 10 (24) micromol NADH/min/mg protein. Assay of HO. production by the Cu(II)/H2O2/CA system in the presence of deoxyribose (TBA assay) yielded values much greater than those obtained omitting CA. Hydroxyl radical production depended on the presence of Cu(II) and H2O2, and significant HO. values were obtained with OH-DOPAMINE, DOPAC, epinephrine, DOPAMINE, DOPA and catecol supplemented systems (Table 2). LipDH (1.0 microM) inhibited 50-80 percent deoxyribose oxidation, the inhibition depending on the CA structure (Table 2). Native catalase (20 microg/ml) and bovine serum albumin (40 microg/ml) effectively prevented LipDH inactivation by the Cu(II)/H2O2/CA system, denaturated catalase, SOD, 0,3 M mannitol, 6,0 mM ethanol and 0,2 M benzoate were less effective or did not protect LipDH (Table 3). Incubation of CAs with the Cu(II)H2O2 system produced a time and Cu(II)-dependent destruction of CAs, the corresponding o-quinone, production as illustrated with epinephrine (figures 6 and 7), as illustrated with epinephrine and DOPAMINE (Table 4). These results support LipDH inactivation by (a) reduction of Cu(II) to Cu(I) by CAs followed by Cu-catalyzed production of HO. from H2O2; (b) CA oxidation followed by the corresponding o-quinone interaction with LipDH. CAPTOPRIL, N-acetylcysteine, mercaptopropionylglycine and penicillamine prevented to various degree LipDH inactivation by the Cu(II)/H2O2/CA systems (Table 1). The former was the most effective and 0,4 mM CAPTOPRIL prevented about 95-100 percent the effect of Cu(II)/H2O2/CA systems supplemented with epinephrine, DOPAMINE and OH-DOPAMINE (Figures 3 and Table 1). LipDH increased and CAPTOPRIL inhibited epinephrine oxidation by Cu(II)/H2O2 (Figures 4 and 5). Since un-physiological concentrations of CAs and Cu(II) may be released in the myocardium after ischemia-reperfusion, the summarized observations may contribute to explain myocardial damage in that condition.
Descritores: Catecol Oxidase/química
Di-Hidrolipoamida Desidrogenase/antagonistas & inibidores
Cromatografia Líquida de Alta Pressão
Di-Hidrolipoamida Desidrogenase/metabolismo
Interações Medicamentosas
Compostos de Sulfidrila/farmacologia
Tipo de Publ: Estudo Comparativo
Responsável: BR1.1 - BIREME

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