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1.
Plant Signal Behav ; 18(1): 2163349, 2023 12 31.
Artigo em Inglês | MEDLINE | ID: mdl-36645912

RESUMO

Planting Elymus nutans artificial grassland to replace degraded Artemisia baimaensis grassland on the Qinghai Tibetan plateau (QTP) can effectively alleviate local grass-livestock imbalance. However, it is unknown whether the allelopathy of natural grassland plant A. baimaensis on E. nutans affects grassland establishment. Accordingly, we examined the effects of varying concentrations of aqueous extracts of A. baimaensis litter on the seed germination and early seedling growth of E. nutans, and the effects of A. baimaensis volatile organic compounds (VOCs) on the growth parameters and physiological characteristics of E. nutans. The results indicate that the aqueous extract inhibited the force, percentage, and index of germination of E. nutans and affected early seedling growth, particularly at high concentrations. Further, the VOCs significantly reduced the aboveground and root biomass of E. nutans and increased malondialdehyde concentrations. Additionally, these VOCs altered the antioxidant enzyme activities and increased the superoxide dismutase, peroxidase, ascorbic acid peroxidase, soluble sugar, and proline content but significantly decreased glutathione reductase levels. Our results indicate that the allelopathy of A. baimaensis significantly inhibited the germination and seedling growth of E. nutans . Thus, the leaching of A. baimaensis may produce allelochemicals in the soil that inhibit the germination of E. nutans seeds. Moreover, the VOCs of A. baimaensis may disrupt the growth process, resulting in a decrease in biomass and a disruption of the physiological metabolism of seedlings under field conditions.


Assuntos
Artemisia , Elymus , Elymus/metabolismo , Pradaria , Alelopatia , Plântula , Germinação , Plantas , Sementes , Peroxidases/metabolismo , Peroxidases/farmacologia
2.
Osteoarthritis Cartilage ; 30(12): 1606-1615, 2022 12.
Artigo em Inglês | MEDLINE | ID: mdl-36096467

RESUMO

OBJECTIVE: To explore the association between oxidative stress (OS) and Kashin-Beck disease (KBD). METHODS: Terms associated with "KBD" and "OS" were searched in the six different databases up to October 2021. Stata 14.0 was used to pool the means and standard deviations using random-effect or fixed-effect model. The differentially expressed genes in the articular chondrocytes of KBD were identified, the OS related genes were identified by blasting with the GeneCards. The KEGG pathway and gene ontology enrichment analysis was conducted using STRING. RESULTS: The pooled SMD and 95% CI showed hair selenium (-4.59; -6.99, -2.19), blood selenium (-1.65; -2.86, -0.44) and glutathione peroxidases (-4.15; -6.97, -1.33) levels were decreased in KBD, whereas the malondialdehyde (1.12; 0.60, 1.64), nitric oxide (2.29; 1.31, 3.27), nitric oxide synthase (1.07; 0.81, 1.33) and inducible nitric oxide synthase (1.69; 0.62, 2.77) were increased compared with external controls. Meanwhile, hair selenium (-2.71; -5.32, -0.10) and glutathione peroxidases (-1.00; -1.78, -0.22) in KBD were decreased, whereas the malondialdehyde (1.42; 1.04, 1.80), nitric oxide (3.08; 1.93, 4.22) and inducible nitric oxide synthase (0.81; 0.00, 1.61) were elevated compared with internal controls. Enrichment analysis revealed apoptosis was significantly correlated with KBD. The significant biological processes revealed OS induced the release of cytochrome c from mitochondria. The cellular component of OS located in the mitochondrial outer membrane. CONCLUSIONS: The OS levels in KBD were significantly increased because of selenium deficiency, OS mainly occurred in mitochondrial outer membrane, released of cytochrome c from mitochondria, and induced apoptotic signaling pathway.


Assuntos
Doença de Kashin-Bek , Selênio , Humanos , Doença de Kashin-Bek/genética , Doença de Kashin-Bek/metabolismo , Óxido Nítrico Sintase Tipo II/metabolismo , Selênio/metabolismo , Biologia Computacional , Óxido Nítrico/metabolismo , Citocromos c/metabolismo , Citocromos c/farmacologia , Estresse Oxidativo , Malondialdeído/farmacologia , Glutationa/metabolismo , Glutationa/farmacologia , Peroxidases/metabolismo , Peroxidases/farmacologia
3.
Curr Protein Pept Sci ; 21(5): 497-506, 2020.
Artigo em Inglês | MEDLINE | ID: mdl-31746293

RESUMO

Latex, a milky fluid found in several plants, is widely used for many purposes, and its proteins have been investigated by researchers. Many studies have shown that latex produced by some plant species is a natural source of biologically active compounds, and many of the hydrolytic enzymes are related to health benefits. Research on the characterization and industrial and pharmaceutical utility of latex has progressed in recent years. Latex proteins are associated with plants' defense mechanisms, against attacks by fungi. In this respect, there are several biotechnological applications of antifungal proteins. Some findings reveal that antifungal proteins inhibit fungi by interrupting the synthesis of fungal cell walls or rupturing the membrane. Moreover, both phytopathogenic and clinical fungal strains are susceptible to latex proteins. The present review describes some important features of proteins isolated from plant latex which presented in vitro antifungal activities: protein classification, function, molecular weight, isoelectric point, as well as the fungal species that are inhibited by them. We also discuss their mechanisms of action.


Assuntos
Antifúngicos/farmacologia , Quitinases/farmacologia , Látex/química , Peptídeo Hidrolases/farmacologia , Peroxidases/farmacologia , Lectinas de Plantas/farmacologia , Proteínas de Plantas/farmacologia , Antifúngicos/classificação , Antifúngicos/isolamento & purificação , Botrytis/efeitos dos fármacos , Botrytis/crescimento & desenvolvimento , Candida albicans/efeitos dos fármacos , Candida albicans/crescimento & desenvolvimento , Quitinases/classificação , Quitinases/isolamento & purificação , Quitinases/fisiologia , Fusarium/efeitos dos fármacos , Fusarium/crescimento & desenvolvimento , Ponto Isoelétrico , Testes de Sensibilidade Microbiana , Peso Molecular , Peptídeo Hidrolases/classificação , Peptídeo Hidrolases/isolamento & purificação , Peptídeo Hidrolases/fisiologia , Peroxidases/classificação , Peroxidases/isolamento & purificação , Peroxidases/fisiologia , Doenças das Plantas/microbiologia , Extratos Vegetais/química , Lectinas de Plantas/classificação , Lectinas de Plantas/isolamento & purificação , Lectinas de Plantas/fisiologia , Proteínas de Plantas/classificação , Proteínas de Plantas/isolamento & purificação , Proteínas de Plantas/fisiologia , Plantas/química
4.
Curr Protein Pept Sci ; 18(8): 864-880, 2017.
Artigo em Inglês | MEDLINE | ID: mdl-28393701

RESUMO

The aim of this review is to cover most recent research on plant pathogenesis- and defenserelated proteins from latex-bearing medicinal plant Chelidonium majus (Papaveraceae) in the context of its importance for latex activity, function, pharmacological activities, and antiviral medicinal use. These results are compared with other latex-bearing plant species and recent research on proteins and chemical compounds contained in their latex. This is the first review, which clearly summarizes pathogenesisrelated (PR) protein families in latex-bearing plants pointing into their possible functions. The possible antiviral function of the latex by naming the abundant proteins present therein is also emphasized. Finally latex-borne defense system is hypothesized to constitute a novel type of preformed immediate defense response against viral, but also non-viral pathogens, and herbivores.


Assuntos
Antivirais/química , Chelidonium/química , Látex/química , Proteínas de Plantas/química , Alcaloides/química , Alcaloides/isolamento & purificação , Alcaloides/farmacologia , Antivirais/isolamento & purificação , Antivirais/farmacologia , Benzilisoquinolinas/química , Benzilisoquinolinas/isolamento & purificação , Benzilisoquinolinas/farmacologia , Catecol Oxidase/química , Catecol Oxidase/isolamento & purificação , Catecol Oxidase/farmacologia , Quitinases/química , Quitinases/isolamento & purificação , Quitinases/farmacologia , Endopeptidases/química , Endopeptidases/isolamento & purificação , Endopeptidases/farmacologia , Lipoxigenase/química , Lipoxigenase/isolamento & purificação , Lipoxigenase/farmacologia , Peroxidases/química , Peroxidases/isolamento & purificação , Peroxidases/farmacologia , Proteínas de Plantas/isolamento & purificação , Proteínas de Plantas/farmacologia , Ribonucleases/química , Ribonucleases/isolamento & purificação , Ribonucleases/farmacologia , Replicação Viral/efeitos dos fármacos
5.
Rev Med Chir Soc Med Nat Iasi ; 119(1): 257-66, 2015.
Artigo em Inglês | MEDLINE | ID: mdl-25970976

RESUMO

AIM: This study aimed to investigate the histo-anatomical features of the long shoots and leaves (young and mature) of Pinus cembra L.. The activity of antioxidant enzymatic systems and the content of heavy metals were also evaluated. MATERIAL AND METHODS: For the histo-anatomical study, the cross-sections were performed by usual techniques. The activity of antioxidant enzymatic systems (superoxide dismutase, catalase and peroxidase) was evaluated by spectrophotometric methods. The content of heavy metals was determined by atomic absorption spectroscopy. RESULTS: The cross-section through the long shoots shows many resiniferous canals and a periderm of variable thickness. The leaf has a triangular shape and only two vascular bundles in the inferior and upper levels. The highest level of superoxide dismutase activity (344.90 U/mg protein) was determined in the long shoots collected from a cembran pine in Vatra Dornei, while the highest level of peroxidase activity (7611.11 U/mg protein) was found in the leaves collected in Calimani Mountains. Cd level in all samples was under the quantification limit. Higher levels of Pb were determined in the long shoots (3 µg/g dry weight for the vegetal material collected in Vatra Dornei and 2.86 µg/g dry weight for the vegetal material collected in Calimani Mountains). CONCLUSIONS: Pinus cembra L. leaves show specific elements of subgenus Strobus (a triangular shape of the cross section, one single vascular bundle and two resiniferous canals). The results obtained for the superoxide dismutase and peroxidase activities corroborated with those obtained for the heavy metal contents indicate that antioxidant enzymes play an important role in the protection of Pinus cembra L. against exogenous stress factors.


Assuntos
Antioxidantes/farmacologia , Metais Pesados/toxicidade , Peroxidases/farmacologia , Pinus , Extratos Vegetais/farmacologia , Folhas de Planta/química , Brotos de Planta/química , Superóxido Dismutase/farmacologia , Antioxidantes/química , Catalase/farmacologia , Chumbo/toxicidade , Metais Pesados/química , Peroxidases/química , Extratos Vegetais/química , Espectrofotometria/métodos , Análise Espectral/métodos , Superóxido Dismutase/química
6.
J Appl Microbiol ; 101(1): 242-50, 2006 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-16834612

RESUMO

AIMS: To study the bactericidal properties of the lactoperoxidase (LPER)-thiocyanate and soybean peroxidase (SBP)-thiocyanate systems at low pH, their efficiency for inactivation of Escherichia coli and Shigella in acidic fruit and vegetable juices, their effect on colour stability of the juices and interaction with ascorbic acid. METHODS AND RESULTS: Three-strain cocktails of E. coli and Shigella spp. in selected juices were supplemented with the LPER or SBP system. Within 24 h at 20 degrees C, the LPER system inactivated both cocktails by > or = 5 log10 units in apple, 2-5 log10 units in orange and < or = 1 log10 unit in tomato juices. In the presence of SBP, browning was significant in apple juice and white grape juice, slight in pink grape juice and absent in orange or tomato juice. Ascorbic acid protected E. coli and Shigella against inactivation by the LPER system, and peroxidase systems significantly reduced the ascorbic acid content of juices. CONCLUSIONS: Our results suggest a different specificity of LPER and SBP for SCN-, phenolic substrates of browning and ascorbic acid in acidic juices. The LPER system appeared a more appropriate candidate than the SBP system for biopreservation of juices. SIGNIFICANCE AND IMPACT OF THE STUDY: This work may open perspectives towards the development of LPER or other peroxidases as biopreservatives in acidic foods.


Assuntos
Bebidas , Escherichia coli/efeitos dos fármacos , Conservação de Alimentos , Conservantes de Alimentos/farmacologia , Peroxidases/farmacologia , Shigella/efeitos dos fármacos , Ácido Ascórbico/análise , Cor , Disenteria Bacilar/prevenção & controle , Frutas , Testes de Sensibilidade Microbiana , Tiocianatos/análise , Verduras
7.
Plant Physiol Biochem ; 42(5): 445-50, 2004 May.
Artigo em Inglês | MEDLINE | ID: mdl-15191749

RESUMO

Tobacco (Nicotiana tabacum L. cv. Petit Havana) callus cultures were exposed to UV-C high dose pulse-treatment (254 nm, 50 kJ m(-2), 1 h-treatment). After 6, 24 and 48 h from the end of the treatment, calli were cut transversally in two layers and oxidative damage (malondialdehyde [MDA] and hydrogen peroxide), non-enzymatic (radical scavenging antioxidants [RSA] and polyamines) and enzymatic antioxidants (ascorbate peroxidase [APX, EC 1.11.1.11], glutathione reductase [GR, EC 1.6.4.2], catalase [CAT, EC 1.11.1.6] and guaiacol peroxidase [GPX, EC 1.11.1.7]) were evaluated. At each time-point data referred to UV-C treated calli were compared to data of untreated ones (control). Despite of a strong increase of H2O2 content, a slight cellular damage was observed in both upper and lower layers 24 and 48 h after UV-C treatment. An activation first of non-enzymatic antioxidants and then of enzymatic antioxidants was detected in UV-C treated calli. In particular, RSA and putrescine (PUT) accumulated 6 h after UV-C treatment while APX, GR and GPX enzyme activities increased 24 h after UV-C irradiation. Catalase activity did not change. UV-C-induced oxidative stress and antioxidative response were observed also in cell layers not directly exposed to UV irradiation, indicating that a stress signal was transmitted to the whole mass of callus.


Assuntos
Antioxidantes/farmacologia , Estresse Oxidativo , Raios Ultravioleta , Ascorbato Peroxidases , Catalase/farmacologia , Radicais Livres , Glutationa Redutase/farmacologia , Peróxido de Hidrogênio/farmacologia , Peroxidação de Lipídeos , Peróxidos Lipídicos/química , Malondialdeído/farmacologia , Peroxidase/farmacologia , Peroxidases/farmacologia , Poliaminas/química , Putrescina/farmacologia , Fatores de Tempo , Nicotiana/metabolismo
8.
Biol Pharm Bull ; 26(11): 1511-6, 2003 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-14600392

RESUMO

Plant peroxidases were found to play an important role in plant physiology such as the metabolism and transformation of small complexes. In the present research, a novel Momordica charantia peroxidase (MCP) from fruits was purified to electrophoretic homogeneity by combining consecutive treatment of ammonium sulfate fractionation, ion exchange chromatography on DEAE-Sepharose FF, affinity chromatography on concanavalin A (Con A) Sepharose and gel filtration on Sephadex G-150. The physical and chemical characters of MCP were also investigated. MCP catalyzed the oxidation of ferulic acid (FA) to dehydrodimer (FA-2) in aqueous acetone system at pH 5.0. Its structure was identified by spectral analyses including IR, 1H-, 13C-NMR and electrospray ionization mass spectroscopy (ESI-MS). The anti-inflammatory activities of FA, FA-2 and other derivatives were examined. FA-2 significantly inhibited the release of proinflammatory factors such as TNF-alpha, NO and proliferation of spleen cells induced by phytohemagglutinin (PHA) and Con A and promoted a greater DNA fragmentation of spleen cells than that of other complexes. These results suggested that MCP as a tool enzyme transformed some complexes such as FA to more active derivatives, and that FA-2 was a potential inhibitor on inflammation through interference with immune response in the process of inflammation, which maybe was associated with apoptosis of immune related cells induced by FA-2.


Assuntos
Anti-Inflamatórios não Esteroides/farmacologia , Momordica charantia , Peroxidases/farmacologia , Animais , Anti-Inflamatórios não Esteroides/química , Anti-Inflamatórios não Esteroides/isolamento & purificação , Fragmentação do DNA/efeitos dos fármacos , Fragmentação do DNA/fisiologia , Feminino , Frutas , Masculino , Camundongos , Camundongos Endogâmicos BALB C , Oxirredução/efeitos dos fármacos , Peroxidases/química , Peroxidases/isolamento & purificação , Extratos Vegetais/química , Extratos Vegetais/isolamento & purificação , Extratos Vegetais/farmacologia , Baço/efeitos dos fármacos , Baço/metabolismo
9.
Biochem Biophys Res Commun ; 290(1): 457-62, 2002 Jan 11.
Artigo em Inglês | MEDLINE | ID: mdl-11779192

RESUMO

Bax, a mammalian proapoptotic member of the Bcl-2 family, can induce cell death when expressed in yeast or plant cells. To identify plant Bax inhibitors, we cotransformed a soybean cDNA library and the Bax gene into yeast cells and screened for expressed genes that prevented Bax-induced apoptosis. From the Bax-inhibiting genes isolated, ascorbate peroxidase (sAPX) was selected for characterization. The transcription of sAPX in plants was specifically induced by oxidative stress. Moreover, overexpression of sAPX partially suppressed the H(2)O(2)-sensitive phenotype of yeast cytosolic catalase T (Deltactt)- and thermosensitive phenotype of cytochrome c peroxidase (Deltaccp)-deleted mutant cells. Examination of reactive oxygen species (ROS) production using the fluorescence method of dihydrorhodamine 123 oxidation revealed that expression of Bax in yeast cells generated ROS, which was greatly reduced by coexpression with sAPX. Our results collectively suggest that sAPX inhibits the generation of ROS by Bax, which in turn suppresses Bax-induced cell death in yeast.


Assuntos
Glycine max/enzimologia , Peroxidases/farmacologia , Proteínas Proto-Oncogênicas c-bcl-2 , Proteínas Proto-Oncogênicas/metabolismo , Espécies Reativas de Oxigênio , Apoptose , Ascorbato Peroxidases , Northern Blotting , Western Blotting , Catalase/fisiologia , Morte Celular , Clonagem Molecular , Citocromo-c Peroxidase/fisiologia , DNA Complementar/metabolismo , Citometria de Fluxo , Biblioteca Gênica , Peróxido de Hidrogênio/metabolismo , Peróxido de Hidrogênio/farmacologia , Microscopia Confocal , Microscopia Eletrônica , Estresse Oxidativo , Fenótipo , RNA Mensageiro/metabolismo , Rodaminas/farmacologia , Saccharomyces cerevisiae/enzimologia , Temperatura , Fatores de Tempo , Transcrição Gênica , Proteína X Associada a bcl-2
10.
Mol Pharmacol ; 60(5): 972-80, 2001 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-11641425

RESUMO

The antithyroid drug, methimazole (MMI) is used to treat patients with Graves' hyperthyroidism. The major action of MMI is to inhibit synthesis of thyroid hormone in the thyroid gland. However, MMI also has antioxidant and immunomodulatory effects on thyrocytes and/or immune cells. This study identifies novel antioxidant and immunomodulatory effects of MMI involving the interferon-gamma (IFN-gamma) signaling pathway in thyroid cells. MMI inhibits transcription of the intercellular adhesion molecule-1 (ICAM-1) gene by modulating the function of transcription factor STAT1 (signal transducer and activator of transcription 1), which binds to the IFN-gamma activated site of the ICAM-1 promoter. Furthermore, MMI rapidly eliminates H(2)O(2) produced by IFN-gamma treatment in thyroid cells and thus inhibits the H(2)O(2)-mediated phosphorylation of tyrosine 701 in STAT1. MMI also eliminates H(2)O(2) in vitro. MMI facilitates electron transfer from NADPH to H(2)O(2) using thioredoxin or glutathione, fulfilling a role similar to peroxiredoxin or glutathione peroxidase, respectively. MMI prevents the IFN-gamma and H(2)O(2)-mediated reversible inactivation of phosphatases. These effects inhibit full activation of the IFN-gamma-induced Janus kinase(JAK)/STAT signaling pathway in FRTL-5 thyroid cells. These results may in part explain the antioxidant and immunomodulatory effects of MMI in thyroid cells of Graves' disease patients.


Assuntos
Antioxidantes/farmacologia , Expressão Gênica/efeitos dos fármacos , Peróxido de Hidrogênio/metabolismo , Interferon gama/farmacologia , Metimazol/farmacologia , Proteínas , Proteínas Proto-Oncogênicas , Proteínas Repressoras , Glândula Tireoide/efeitos dos fármacos , Fatores de Transcrição , Adjuvantes Imunológicos/farmacologia , Animais , Proteínas de Transporte/biossíntese , Células Cultivadas , Proteínas de Ligação a DNA/metabolismo , Interações Medicamentosas , Transporte de Elétrons/efeitos dos fármacos , Peróxido de Hidrogênio/farmacologia , Molécula 1 de Adesão Intercelular/biossíntese , Molécula 1 de Adesão Intercelular/genética , Interferon gama/antagonistas & inibidores , Janus Quinase 1 , Janus Quinase 2 , Cinética , Peroxidases/farmacologia , Peroxirredoxinas , Fosforilação/efeitos dos fármacos , Biossíntese de Proteínas , Proteínas Inibidoras de STAT Ativados , Proteínas Tirosina Quinases/metabolismo , Ratos , Fator de Transcrição STAT1 , Fator de Transcrição STAT3 , Transdução de Sinais/fisiologia , Proteína 1 Supressora da Sinalização de Citocina , Proteína 3 Supressora da Sinalização de Citocinas , Proteínas Supressoras da Sinalização de Citocina , Glândula Tireoide/citologia , Glândula Tireoide/metabolismo , Transativadores/metabolismo , Tirosina/metabolismo
11.
Immunopharmacology ; 46(1): 71-7, 2000 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-10665781

RESUMO

Adjuvant arthritis, induced by Mycobacterium butyricum, is an experimental immunopathy that shares many features of human rheumatoid arthritis and, as such, is one of the most widely used models for studying the anti-inflammatory activity of compounds. In rats with adjuvant induced arthritis, IgG antibodies to M. butyricum have been detected and autoantigens that cross react with mycobacteria may be involved in the pathogenesis of adjuvant arthritis. In this study, the anti-inflammatory and immunosuppressive activities of two cyclooxygenase-2 selective inhibitors, flosulide and L-745,337, at doses of 0.1, 1 and 5 mg/kg/day, were examined in adjuvant arthritic rats. After 14 days of treatment, a clear dose-dependent inhibition of plantar edema was seen for both flosulide (ID50 lower than 0.1 mg/kg) and L-745,337 (ID50 = 0.4 mg/kg). Plasma levels of IgG anti-M. butyricum antibodies were also decreased by both drugs. In each case the maximal immunosuppressive effect was observed at doses lower than 5 mg/kg. The non-selective COX-2 inhibitor, indomethacin (1 mg/kg) decreased paw edema by 65% and the levels of IgG anti-M. butyricum by 45%. Neither cyclooxygenase selective inhibitors nor indomethacin decreased the delayed hypersensitivity reaction induced by M. butyricum. Thus, in vivo inhibition of COX-2 inhibited articular swelling and also the humoral immune response to Mycobacterium.


Assuntos
Anticorpos Antibacterianos/efeitos dos fármacos , Artrite Experimental/tratamento farmacológico , Artrite Experimental/imunologia , Isoenzimas/farmacologia , Mycobacterium/imunologia , Prostaglandina-Endoperóxido Sintases/farmacologia , Animais , Anti-Inflamatórios não Esteroides/uso terapêutico , Peso Corporal , Ciclo-Oxigenase 2 , Inibidores de Ciclo-Oxigenase 2 , Inibidores de Ciclo-Oxigenase/uso terapêutico , Modelos Animais de Doenças , Relação Dose-Resposta a Droga , Edema/terapia , Feminino , Pé/patologia , Imunoglobulina G/sangue , Imunoglobulina G/efeitos dos fármacos , Terapia de Imunossupressão , Indanos/uso terapêutico , Indometacina/uso terapêutico , Peroxidases/antagonistas & inibidores , Peroxidases/farmacologia , Ratos , Ratos Wistar
12.
Planta Med ; 66(8): 724-7, 2000 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-11199129

RESUMO

A basic peroxidase (EC 1.11.1.7) (pl around 9.0) has been identified in commercial gel of Aloe barbadensis. In vivo, the activity is localised in the vascular system of inner aqueous leaf parenchyma. Some relevant properties of this basic peroxidase of Aloe have been investigated in leaf extract and in commercial gel where it is notably stable. The acid optimum pH (5.0) for activity and the low KM for H2O2 (0.14 mM) suggest that, when topically applied, Aloe peroxidase may scavenge H2O2 in skin surface.


Assuntos
Aloe/enzimologia , Peroxidases/isolamento & purificação , Plantas Medicinais , Pele/efeitos dos fármacos , Géis , Peroxidases/farmacologia
14.
Oral Microbiol Immunol ; 7(5): 315-20, 1992 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-1494457

RESUMO

Effects of the salivary peroxidase (SPO) system on the growth, glucose uptake and metabolic activities of oral bacteria are well documented but the effects on oral fungi are virtually unknown. Therefore, the viability of Candida albicans (ATCC 28366) exposed to the peroxidase/SCN-/H2O2 system was studied in sterilized saliva, in phosphate-buffered saline (PBS) and in potassium chloride. The growth of C. albicans in glucose-supplemented saliva was faster at pH 5.5 than at pH 7. The addition of the complete SPO (or lactoperoxidase) system to either sterilized saliva, KCl (50 microM) or PBS at pH 5.5 inhibited dose-dependently the viability of C. albicans in KCl, but no inhibition was found in PBS or saliva. Maximal inhibition was achieved in 2 h and with > 320 microM of peroxidase-generated HOSCN/OSCN-. However, physiological salivary concentrations of phosphate (> or = 1.0 mM) and PBS blocked the antifungal effect of HOSCN/OSCN-. The relative proportions of SCN- and H2O2 were critical to the antifungal effects. With 0.2 mM KSCN, a complete loss of viability was achieved, though the HOSCN/OSCN- concentrations did not exceed 100 microM. It is concluded that C. albicans is sensitive to HOSCN/OSCN- but salivary concentrations of phosphate block the antifungal effect of the peroxidase systems.


Assuntos
Candida albicans/efeitos dos fármacos , Peroxidases/farmacologia , Saliva/enzimologia , Tiocianatos/farmacologia , Antifúngicos/farmacologia , Peróxido de Hidrogênio/farmacologia , Concentração de Íons de Hidrogênio , Lactoperoxidase/farmacologia , Fosfatos/farmacologia , Saliva/microbiologia , Proteínas e Peptídeos Salivares/farmacologia
15.
Farmakol Toksikol ; 50(6): 47-51, 1987.
Artigo em Russo | MEDLINE | ID: mdl-3436424

RESUMO

Experiments were carried out on rats after coronary arterial ligation. In the myocardial infarction region there is the border zone or reversibly damaged zone which may be partially saved from necrosis by using beta-blocking agents. Atenolol, dibunol, Astragalus dasyanthus pall. moderately decrease the myocardial damage area at permanent and transient ischemia.


Assuntos
Atenolol/farmacologia , Infarto do Miocárdio/tratamento farmacológico , Peroxidases/farmacologia , Extratos Vegetais/farmacologia , Animais , Hidroxitolueno Butilado/farmacologia , Infarto do Miocárdio/patologia , Necrose , Ratos
16.
J Dent Res ; 64(6): 870-6, 1985 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-3858312

RESUMO

Microperoxidase (small m.wt tracer) and horseradish peroxidase (large m.wt tracer) were used to investigate the existence of extracellular (between blood vessels and bone cells) and intracellular transport pathways in the alveolar bone cells of five-day-old rats. HRP directly penetrated the cytoplasm and nucleus of the osteocytes and osteoblasts, but MP did not. These findings suggest that HRP at high dosages is more toxic to bone cells than is MP, since the direct penetration of HRP probably results from alteration of plasma membrane permeability. If so, MP seems to be a more suitable tracer than HRP. The findings from MP tracing suggest that a main transport pathway of bone fluid exists between the external part of the unmineralized zone, which is located in the lacunar and canalicular spaces around bone cells, and the innermost edge of the mineralized matrix, which constitutes the lacunar and canalicular walls; in addition, minor pathways as accessory routes might diverge from the main pathway to go around the bone cells.


Assuntos
Processo Alveolar/metabolismo , Permeabilidade da Membrana Celular/efeitos dos fármacos , Peroxidase do Rábano Silvestre/metabolismo , Peroxidases/metabolismo , Processo Alveolar/citologia , Processo Alveolar/crescimento & desenvolvimento , Animais , Transporte Biológico , Núcleo Celular/metabolismo , Citoplasma/metabolismo , Peroxidase do Rábano Silvestre/farmacologia , Membranas Intracelulares/metabolismo , Osteoblastos/metabolismo , Osteoclastos/metabolismo , Peroxidases/farmacologia , Ratos , Ratos Endogâmicos
17.
Arch Oral Biol ; 29(6): 445-51, 1984.
Artigo em Inglês | MEDLINE | ID: mdl-6589987

RESUMO

The hypothiocyanite ion (OSCN-) is the principal oxidation product of the salivary peroxidase-thiocyanate (SCN-)-hydrogen peroxide antimicrobial system. Supplementation of human saliva in vitro and in vivo with low amounts (less than 1.0 mM) of hydrogen peroxide increase the concentration of salivary OSCN- (in vivo up to 0.3 mM). Elevated concentrations of OSCN- are strongly antimicrobial and may therefore be protective against dental caries. However, as OSCN- is a highly-reactive oxidizing agent, its possible toxic effect on human cells was studied using gingival fibroblasts as target cells. Concentrations of OSCN- (up to 300 microM) had no effect on [3H]-thymidine incorporation into the cells. However, fibroblasts were sensitive to peroxide so that 100 microM of H2O2 caused over 80 per cent reduction in [3H]-thymidine incorporation. The toxicity of H2O2 could be entirely prevented by adding lactoperoxidase and SCN- to the cell culture before the addition of peroxide. Thus, conversion of toxic H2O2 to non-toxic OSCN- in fibroblast culture by lactoperoxidase and SCN- suggests a dual role for the salivary peroxidase system: protection of human cells from H2O2 toxicity and antimicrobial action against oral pathogens. Furthermore, the elevated concentrations of OSCN- which produce inhibition of bacterial metabolism did not damage human cells.


Assuntos
Gengiva/efeitos dos fármacos , Peróxido de Hidrogênio/antagonistas & inibidores , Lactoperoxidase/farmacologia , Peroxidases/farmacologia , Tiocianatos/farmacologia , Adulto , Células Cultivadas , Fibroblastos/efeitos dos fármacos , Fibroblastos/metabolismo , Gengiva/citologia , Humanos , Peróxido de Hidrogênio/farmacologia , Masculino , Tiocianatos/metabolismo , Timidina/metabolismo
18.
J Immunol ; 128(2): 726-31, 1982 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-7054295

RESUMO

The antimicrobial effect of the lactoperoxidase (LPO) system (enzyme with the thiocyanate ion and hydrogen peroxide) on Streptococcus mutans NCTC 10449 (serotype c) was significantly enhanced when the system was combined with secretory IgA. Similar enhancement was observed with LPO-myeloma IgA1 or IgA2 combinations. This enhancement of the antimicrobial efficiency was not dependent on the presence of specific antibodies to S. mutans in the IgA preparation, but seemed to require binding between LPO and immunoglobulin. However, neither human polyclonal nor myeloma IgG or IgM nor rabbit IgG enhanced the antibacterial activity of the LPO system. None of the immunoglobulins, when added alone, produced antimicrobial effects. LPO was shown to bind to colostral secretory IgA, myeloma IgA1, IgA2, and to a lesser degree to monoclonal and polyclonal IgG and monoclonal IgM. This binding had a stabilizing effect on the enzyme activity. Our results suggest that IgA significantly enhances the antibacterial efficiency of one of the innate immune factors--the LPO system.


Assuntos
Imunoglobulina A Secretora/imunologia , Imunoglobulina A/imunologia , Lactoperoxidase/farmacologia , Peroxidases/farmacologia , Streptococcus mutans/efeitos dos fármacos , Animais , Formação de Anticorpos , Bovinos , Colostro/imunologia , Humanos , Peróxido de Hidrogênio/farmacologia , Imunoglobulina A Secretora/metabolismo , Imunoglobulina G/imunologia , Imunoglobulina G/metabolismo , Imunoglobulina M/metabolismo , Lactalbumina/farmacologia , Lactoferrina/farmacologia , Lactoperoxidase/metabolismo , Coelhos , Receptores Imunológicos , Albumina Sérica/farmacologia , Tiocianatos/metabolismo
19.
Biochim Biophys Acta ; 611(2): 227-40, 1980 Feb 14.
Artigo em Inglês | MEDLINE | ID: mdl-6766743

RESUMO

An L-amino acid oxidase (L-amino-acid oxygen oxidoreductase (deaminating), EC 1.4.3.2) from the blue-green alga Anacystis nidulans has been purified to homogeneity with an overall yield of about 10%. Purification included ammonium sulfate fractionation and CM-Sephadex, DEAE-Sephadex, and hydroxyapatite chromatography. The purified enzyme has an absorption spectrum which is characteristic of a flavoprotein, and contains 1 mol FAD per mol enzyme. The native enzyme has a molecular weight of 98 000 as determined by gel exclusion chromatography. Electrophoresis in SDS-polyacrylamide gels gives a single protein band corresponding to a molecular weight of 49 000, which suggests that the native enzyme is composed of 2 subunits of equal molecular weight. As previously demonstrated, the enzyme catalyzes the oxidative deamination of the basic amino acids: L-arginine, L-lysine, L-ornithine and L-histidine. In the presence of catalase and of any of these amino acids, 0.5 mol O2 is consumed, and 1 mol ammonia is formed for each mol amino acid oxidized. HCN is formed from L-histidine when the L-amino acid oxidase is supplemented with peroxidase. In addition to the unusual substrate specificity of this L-amino acid ozidase, it also has an unusual set of inhibitors including o-phenanthroline as well as divalent cations of which Cu2+, Zn2+, and Cd2+ are the most effective ones, but Mg2+ and Ca2+ also inhibit. This inhibition can be reversed by chelating agents such as EDTA. ATP and ADP, but not AMP, can also overcome the inhibition caused by Mg2+, for example. The inhibitory effect of cations can be demonstrated in vivo.


Assuntos
Aminoácido Oxirredutases/metabolismo , Cianobactérias/enzimologia , Aminoácido Oxirredutases/antagonistas & inibidores , Aminoácido Oxirredutases/isolamento & purificação , Cátions Bivalentes , Ácido Edético , Eletroforese em Gel de Poliacrilamida , Peso Molecular , Consumo de Oxigênio , Peroxidases/farmacologia , Compostos de Amônio Quaternário/metabolismo , Especificidade por Substrato
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