title: Oxidative DNA damage and antioxidant defenses in the European common lizard (Lacerta vivipara) in supercooled and frozen states.
abstract: The European common lizard (Lacerta vivipara) tolerates long periods at sub-zero temperatures, either in the supercooled or the frozen state. Both physiological conditions limit oxygen availability to tissues, compelling lizards to cope with potential oxidative stress during the transition from ischemic/anoxic conditions to reperfusion with aerated blood during recovery. To determine whether antioxidant defenses are implicated in the survival of lizards when facing sub-zero temperatures, we monitored the activities of antioxidant enzymes and oxidative stress either during supercooling or during freezing exposures (20 h at -2.5 degrees C) and 24 h after thawing in two organs of lizards--muscle and liver. Supercooling induced a significant increase in the total SOD and GPx activity in muscle (by 67 and 157%, respectively), but freezing had almost no effect on enzyme activity, either in muscle or in liver. By contrast, thawed lizards exhibited higher GPx activity in both organs (a 133% increase in muscle and 59% increase in liver) and a significant decrease in liver catalase activity (a 47% difference between control and thawed lizards). These data show that supercooling (but not freezing) triggers activation of the antioxidant system and this may be in anticipation of the overgeneration of oxyradicals when the temperature increases (while thawing or at the end of supercooling). Oxidative stress was assessed from the content of 8-oxodGuo and the different DNA adducts resulting from lipid peroxidation, but it was unaltered whatever the physiological state of the lizards, thus demonstrating the efficiency of the antioxidant system that has been developed by this species. Overall, antioxidant defenses appear to be part of the adaptive machinery for reptilian tolerance to sub-zero temperatures.
authors.affiliation: Physiologie Intégrative Cellulaire et Moléculaires (UMR 5123), Campus La Doua, Bât 404, 4th Etage, 43 bd du 11 novembre 1918, F-69622 Villeurbanne Cedex, France. yann.voituron@univ-lyon1.fr
authors.forename: Yann
authors.initials: Y
authors.lastname: Voituron
authors.forename: Stéphane
authors.initials: S
authors.lastname: Servais
authors.forename: Caroline
authors.initials: C
authors.lastname: Romestaing
authors.forename: Thierry
authors.initials: T
authors.lastname: Douki
authors.forename: Hervé
authors.initials: H
authors.lastname: Barré
mesh_terms: D000222:Adaptation, Physiological; D000225:Adenine / Q000378:metabolism; D000447:Aldehydes / Q000378:metabolism; D000818:Animals; D000975:Antioxidants / Q000378:metabolism / Q000494:pharmacology*; D002374:Catalase / Q000378:metabolism; D004249:DNA Damage / Q000187:drug effects* / Q000502:physiology; D005615:Freezing; D005979:Glutathione Peroxidase / Q000378:metabolism; D006147:Guanine / Q000378:metabolism; D015227:Lipid Peroxidation; D008099:Liver / Q000378:metabolism; D008116:Lizards / Q000378:metabolism*; D008315:Malondialdehyde / Q000378:metabolism; D009132:Muscles / Q000378:metabolism; D018384:Oxidative Stress / Q000187:drug effects* / Q000502:physiology; D013482:Superoxide Dismutase / Q000378:metabolism
chemical_list: D000447:Aldehydes; D000975:Antioxidants; D008315:Malondialdehyde; D006147:Guanine; D002374:Catalase; D005979:Glutathione Peroxidase; D013482:Superoxide Dismutase; D000225:Adenine; C027576:4-hydroxy-2-nonenal