Your browser doesn't support javascript.

Portal de Pesquisa da BVS Veterinária

Informação e Conhecimento para a Saúde

Home > Pesquisa > ()
Imprimir Exportar

Formato de exportação:

Exportar

Exportar:

Email
Adicionar mais destinatários

Enviar resultado
| |

Catalase and glutathione peroxidase in dogs naturally infected by Leishmania infantum

Lopes-Neto, Belarmino Eugênio; Santos, Glauco Jonas Lemos; Lima, Adam Leal; Barbosa, Maritza Cavalcante; Santos, Talya Ellen Jesus dos; Uchoa, Daniel Couto; Pinheiro, Ana Débora Nunes; Pinheiro, Romélia Gonçalves; Nunes-Pinheiro, Diana Célia Sousa.
Acta sci. vet. (Online); 44: 01-06, 2016. tab
Artigo em Inglês | VETINDEX | ID: vti-722682

Resumo

Background: Canine leishmaniasis (CanL) is caused by an obligatory intracellular parasite of Leishmania genus that affects organs and tissues. Several studies evaluate the role of reactive oxygen species (ROS) in the pathogenesis of many diseases. The overproduction of ROS on infectious diseases can induce an imbalance between oxidants and antioxidants at cellular or systemic level. Thus, the aim of this study was to evaluate the activity of antioxidant enzymes in CanL. Materials, Methods & Results: Females (n = 17) and males (n = 10), at different ages and with different weight, were selected for this study. Dogs were divided into two groups according classical clinical signs and sorological test to CanL. Animals were considered infected based on indirect immunofluorescent assay and ELISA titration 1:40. Group B (n = 15) composed by positive dogs to CanL from Zoonosis Control Center of Fortaleza (Ceará, Brazil) and group A (n = 12) was composed by dogs from private kennel that were serologically negative to L. infantum and had absence of clinical signs to CanL. Blood sample were collected for evaluation of hematological and biochemical parameters and glutathione peroxidase (GPx) and catalase (CAT) enzymatic activity. Data were analyzed by Students t-test and Pearson correlation coefficient (P 0.05). Total proteins (TP, mg/dL) and alkaline phosphatase (ALP, U/L) [...](AU)
Biblioteca responsável: BR68.1
Localização: BR68.1