Extracellular glutathione peroxidase from the blood-sucking bug, rhodnius prolixus
Glutathione peroxidase (GPX) activity was measured in several tissues of the blood-sucking bug, Rhodnius prolixus. In contrast to the pattern found in vertebrates, where GPX is predominantly intracellular, the highest levels of this enzyme in Rhodnius were found in the hemolymph. The hemolymph glutathione-dependent peroxidase accepted both H(2)O(2) and t-butyl hydroperoxide as substrates. This fact, together with the absolute glutathione dependence, inhibition by mercaptosuccinate, insensitivity to cyanide, and a molecular mass (100.7 kDa) similar to vertebrate GPXs, led us to attribute this peroxidatic activity to a Se-dependent enzyme. Hemolymph GPX specific activity increases during development and a twofold stimulation was observed after an oxidative challenge with hemin, suggesting that enzyme synthesis is under regulatory control. A role for extracellular GPX as an antioxidant protection against oxidative damage produced by heme derived from digestion of blood hemoglobin is discussed. Arch. Copyright 1999 Wiley-Liss, Inc.
Paes
MC
Departamento de Bioquimica Medica, Instituto de Ciencias Biomedicas, Centro de Ciencias da Saude, Universidade Federal do Rio de Janeiro, Ilha do Fundao, Rio de Janeiro, RJ, Brasil.
Oliveira
PL