Affiliation:
1. Department of Biology, Aarhus University, Aarhus C 8000, Denmark
Abstract
ABSTRACT
Hibernation is a powerful response of a number of mammalian species to reduce energy during the cold winter season, when food is scarce. Mammalian hibernators survive winter by spending most of the time in a state of torpor, where basal metabolic rate is strongly suppressed and body temperature comes closer to ambient temperature. These torpor bouts are regularly interrupted by short arousals, where metabolic rate and body temperature spontaneously return to normal levels. The mechanisms underlying these changes, and in particular the strong metabolic suppression of torpor, have long remained elusive. As summarized in this Commentary, increasing evidence points to a potential key role for hydrogen sulfide (H2S) in the suppression of mitochondrial respiration during torpor. The idea that H2S could be involved in hibernation originated in some early studies, where exogenous H2S gas was found to induce a torpor-like state in mice, and despite some controversy, the idea persisted. H2S is a widespread signaling molecule capable of inhibiting mitochondrial respiration in vitro and studies found significant in vivo changes in endogenous H2S metabolites associated with hibernation or torpor. Along with increased expression of H2S-synthesizing enzymes during torpor, H2S degradation catalyzed by the mitochondrial sulfide:quinone oxidoreductase (SQR) appears to have a key role in controlling H2S availability for inhibiting respiration. Specifically, in thirteen-lined squirrels, SQR is highly expressed and inhibited in torpor, possibly by acetylation, thereby limiting H2S oxidation and causing inhibition of respiration. H2S may also control other aspects associated with hibernation, such as synthesis of antioxidant enzymes and of SQR itself.
Publisher
The Company of Biologists
Subject
Insect Science,Molecular Biology,Animal Science and Zoology,Aquatic Science,Physiology,Ecology, Evolution, Behavior and Systematics
Cited by
3 articles.
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