Heat shock protein expression
Changes in the expression levels of 70kDa heat shock cognate form (Hsc70), the heat-inducible form (Hsp70), and Hsp90 in both kidney and foot during the activity–estivation cycle are shown in Fig.3. Hsp70 was significantly higher than the cognate form in active control animals, as well as in estivating animals and those 20min after arousal (Fig.3A,C). The difference between both proteins was not significant 24h after arousal.
Kidney levels of Hsc70 and Hsp70 showed no significant changes during the activity–estivation cycle (Fig.3A). Nevertheless, foot levels of Hsc70 showed a significant decrease 24h after arousal, when compared with those in active controls and in animals 24h after arousal (Fig.3C). Hsp70 levels in the foot were variable, displaying a significant decrease in both aroused groups (Fig.3C).
The 90kDa heat shock protein showed a significant decrease in the kidney during estivation, and the levels raised after arousal (Fig.3B). In the foot, the changes followed the same pattern as those of Hsp70, being non-significantly different between active controls and estivating animals but decreasing significantly after arousal (Fig.3D).
Unfortunately, we were unable to detect any protein (Hsc70, Hsp70, Hsp90 or β-tubulin) by immunoblot of midgut gland extracts.