title: Roles of catalase and glutathione peroxidase in the tolerance of a pulmonate gastropod to anoxia and reoxygenation.
abstract: Humans and most mammals suffer severe damage when exposed to ischemia and reperfusion episodes due to an overproduction of reactive oxygen species (ROS). In contrast, several hypoxia/anoxia-tolerant animals survive very similar situations. We evaluated herein the redox metabolism in the anoxia-tolerant land snail Helix aspersa after catalase inhibition by 3-amino-1,2,4-triazole (ATZ) injection during a cycle of wide and abrupt change in oxygen availability. The exposure to anoxia for 5 h caused a change of only one of several parameters related to free radical metabolism: a rise in selenium-dependent glutathione peroxidase (Se-GPX) activity in muscle of both saline- and ATZ-injected animals (by 1.9- and 1.8-fold, respectively). Catalase suppression had no effect in animals under normoxia or anoxia. However, during reoxygenation catalase suppression kept high levels of muscle Se-GPX activity (twofold higher than in saline-injected snails up to 30 min reoxygenation) and induced the increase in hepatopancreas SOD activity (by 22 %), indicating higher levels of ROS in both organs than in saline-injected animals. Additionally, catalase-suppressed snails showed 12 % higher levels of carbonyl protein-a sign of mild oxidative stress-in muscle during reoxygenation than those animals with intact catalase. No changes were observed in glutathione parameters (GSH, GSSG and GSSG:GSH ratio), TBARS, and GST activity in any of the experimental groups, in both organs. These results indicate that catalase inhibition inflicts changes in the free radical metabolism during reoxygenation, prompting a stress-response that is a reorganization in other enzymatic antioxidant defenses to minimize alterations in the redox homeostasis in land snails.
authors.affiliation: Departamento de Biologia Celular, Laboratório de Radicais Livres, Universidade de Brasília, Brasília, DF, 70910-900, Brazil.|Faculdade da Ceilândia, Universidade de Brasília, Ceilândia, DF, 72220-140, Brazil.
authors.forename: Alexis F
authors.initials: AF
authors.lastname: Welker
authors.affiliation: Departamento de Biologia Celular, Laboratório de Radicais Livres, Universidade de Brasília, Brasília, DF, 70910-900, Brazil.
authors.forename: Daniel C
authors.initials: DC
authors.lastname: Moreira
authors.affiliation: Departamento de Biologia Celular, Laboratório de Radicais Livres, Universidade de Brasília, Brasília, DF, 70910-900, Brazil. hermes@unb.br.
authors.forename: Marcelo
authors.identifier: 0000-0003-1732-0927
authors.initials: M
authors.lastname: Hermes-Lima
mesh_terms: D000640:Amitrole / Q000494:pharmacology; D000818:Animals; D060829:Arthropod Proteins / Q000378:metabolism; D002374:Catalase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D005979:Glutathione Peroxidase / Q000378:metabolism*; D000860:Hypoxia / Q000378:metabolism*; D009132:Muscles / Q000378:metabolism; D010100:Oxygen / Q000378:metabolism*; D012908:Snails / Q000378:metabolism*
chemical_list: D060829:Arthropod Proteins; D002374:Catalase; D005979:Glutathione Peroxidase; D010100:Oxygen; D000640:Amitrole
keywords: Free radicals; Glutathione; Hypoxia; Ischemia; Oxidative damage