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1.
Braz. j. med. biol. res ; 37(11): 1607-1613, Nov. 2004. graf
Artigo em Inglês | LILACS | ID: lil-385871

RESUMO

Asthma is an inflammatory condition characterized by the involvement of several mediators, including reactive oxygen species. The aim of the present study was to investigate the superoxide release and cellular glutathione peroxidase (cGPx) activity in peripheral blood granulocytes and monocytes from children and adolescents with atopic asthma. Forty-four patients were selected and classified as having intermittent or persistent asthma (mild, moderate or severe). The spontaneous or phorbol myristate acetate (PMA, 30 nM)-induced superoxide release by granulocytes and monocytes was determined at 0, 5, 15, and 25 min. cGPx activity was assayed spectrophotometrically. The spontaneous superoxide release by granulocytes from patients with mild (N = 15), moderate (N = 12) or severe (N = 6) asthma was higher at 25 min compared to healthy individuals (N = 28, P < 0.05, Duncan test). The PMA-induced superoxide release by granulocytes from patients with moderate (N = 12) or severe (N = 6) asthma was higher at 15 and 25 min compared to healthy individuals (N = 28, P < 0.05 in both times of incubation, Duncan test). The spontaneous or PMA-induced superoxide release by monocytes from asthmatic patients was similar to healthy individuals (P > 0.05 in all times of incubation, Duncan test). cGPx activity of granulocytes and monocytes from patients with persistent asthma (N = 20) was also similar to healthy individuals (N = 10, P > 0.05, Kruskal-Wallis test). We conclude that, under specific circumstances, granulocytes from children with persistent asthma present a higher respiratory burst activity compared to healthy individuals. These findings indicate a risk of oxidative stress, phagocyte auto-oxidation, and the subsequent release of intracellular toxic oxidants and enzymes, leading to additional inflammation and lung damage in asthmatic children.


Assuntos
Humanos , Masculino , Feminino , Criança , Adolescente , Asma/sangue , Glutationa Peroxidase/metabolismo , Granulócitos/enzimologia , Monócitos/enzimologia , Superóxido Dismutase/biossíntese , Asma/enzimologia , Biomarcadores/sangue , Estudos de Casos e Controles , Doença Crônica , Fatores de Tempo
2.
Rev. méd. Chile ; 131(6): 613-616, jun. 2003.
Artigo em Espanhol | LILACS | ID: lil-356095

RESUMO

BACKGROUND: The presence of leukocytes, detected by peroxidase test in semen, can be a good indicator of infections in the male genital tract. Peroxidase positive cells have been positively correlated with elevated values of elastase, one of the major proteases liberated by granulocytes at the inflammation place. However, seminal granulocytes may not be adequately detected by the peroxidase test in comparison with immunological methods. AIM: To correlate the determination of peroxidase positive cells with the elastase level in the seminal plasma. MATERIAL AND METHODS: Seminal plasma from 64 patients with a high number of round cells (> 106/ml) in semen, was studied. Correlation analysis was done using the Pearson correlation coefficient. RESULTS: No correlation between the level of granulocyte elastase and the number of peroxidase positive cells (r = 0.2237, p > 0.05), or even the number of round cells (r = 0.03934, p > 0.05) was observed. CONCLUSIONS: Our results suggest that the determination of peroxidase positive cells is not a reliable indicator of leukocytes in the seminal plasma and their absence do not discard a silent genital tract infection.


Assuntos
Humanos , Masculino , Ensaios Enzimáticos Clínicos , Doenças dos Genitais Masculinos/diagnóstico , Elastase de Leucócito/análise , Infecções/diagnóstico , Peroxidase/análise , Sêmen/enzimologia , Reprodutibilidade dos Testes , Granulócitos/enzimologia , Leucócitos/enzimologia , Biomarcadores/análise , Sêmen/citologia
3.
Ciênc. cult. (Säo Paulo) ; 47(3): 151-66, May-Jun. 1995. ilus, graf
Artigo em Inglês | LILACS | ID: lil-191371

RESUMO

The cells of blood vessel walls and the external surface of all blood cells have an ecto-ATPase which hydrolyzes ATP to ADP and also ADP to AMP. This enzyme has also been called apyrase or ATP-diphosphohydrolase. The enzyme hydrolyzes a broad range of tri-and diphosphate nucleosides such as UTP and UDP, GTP and GDP in additon to the adenine nucleotides and because of that it has also been called a nucleoside triphosphate hydrolase. The possible physiological roles for this ecto-ATPase involve the control of vascular tone by modulation of the levels of ATP and ADP binding to purino-receptors of the vasculature, the modulation of thrombogenesis by controlling the extracellular level of ADP which is known to activate platelet aggregation, and the protection from cytolytic effects of extracellular ATP. An ATP-diphosphohydrolase activity has been characterized on the external surface of Schistosoma mansoni, a parasite that lives in the circulation of the human host, and on the outer surface of Entamoeba histolytica, a parasite that may enter the circulation of the host through ulceration in the intestinal mucosa. The endoparasite Toxoplasma gondii also exhibits a nucleoside triphosphate hydrolase of high activity, although in this case the ecto-localization is still not documented. We raise the possibility that the endoparasites have evolved in a way to possibly mimic some of the conditions on the surface of cells normally present in the host circulation, thus escaping hemostatic defense responses of the host which require extracellular ADP or ATP.


Assuntos
Animais , Apirase , Células Sanguíneas/enzimologia , Entamoeba histolytica/enzimologia , Schistosoma mansoni/enzimologia , Toxoplasma/enzimologia , Vasos Sanguíneos/enzimologia , Trifosfato de Adenosina , Plaquetas/enzimologia , Eritrócitos/enzimologia , Granulócitos/enzimologia , Hidrolases , Linfócitos/enzimologia , Macrófagos/enzimologia , Nucleotidases/metabolismo , Plasma/enzimologia
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