Journal of Comparative Physiology B

, Volume 173, Issue 4, pp 269–276 | Cite as

Hibernation induces glutathione redox imbalance in ground squirrel intestine

Original Paper

Abstract

Glutathione (GSH) is the major thiol-disulfide redox buffer in cells and is a critical component of antioxidant defense. Here we examined GSH redox balance in the intestinal mucosa during the annual cycle of 13-lined ground squirrels (Spermophilus tridecemlineatus). The ratio of reduced GSH to its oxidized form (glutathione disulfide, GSSG), which is an index of oxidative stress, was five-fold lower in hibernating compared with summer-active squirrels, an effect due primarily to elevated GSSG concentration in hibernators. During hibernation the total pool of GSH equivalents was lowest in squirrels undergoing arousal and highest in squirrels during interbout arousals. Hibernation decreased intestinal GSSG reductase activity by ~50%, but had no effect on activities of glutathione peroxidase or glucose-6-phosphate dehydrogenase. Within the hibernation season, expression of the stress protein HSP70 in intestinal mucosa was highest in squirrels entering torpor and early in a torpor bout, and lowest in squirrels arousing from torpor and during interbout euthermia. The results suggest that hibernation in ground squirrels is associated with a shift in intestinal GSH redox balance to a more oxidized state. Higher levels of HSP70 during the early phases of torpor may reflect induction of the stress response due to aberrations in protein folding or may be a mechanism to increase enterocyte tolerance to subsequent stress imposed by extended torpor or the arousal process.

Key words

HSP70 Oxidative stress Spermophilus tridecemlineatus Torpor 

Abbreviations

AR

arousing from torpor

EN

entrance into torpor

ET

early torpor

G6PD

glucose-6-phosphate dehydrogenase

GPx

glutathione peroxidase

GR

glutathione reductase

GRP75

glucose regulated protein 75

GSH

glutathione

GSSG

glutathione disulfide

IBA

interbout arousal

LT

late torpor

NF-κB

nuclear factor κB

HSP70

heat shock protein 70

ROS

reactive oxygen species

TCA

trichloroacetic acid

Tb

body temperature

Notes

Acknowledgements

The authors thank Dr. Murray Clayton for help in statistical analyses and Courtney Fleck, Michael Grahn and Timothy Piazza for assistance with animals. This study was supported by grants from the National Science Foundation (IBN-9723860) and the U.S. Army Research Office (DAAD190110455) to HVC and from the National Institutes of Health (RO1-DK44510) to TYA.

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Copyright information

© Springer-Verlag 2003

Authors and Affiliations

  1. 1.Department of Comparative BiosciencesUniversity of Wisconsin School of Veterinary MedicineMadisonUSA
  2. 2.Department of Molecular and Cellular PhysiologyLouisiana State University Health Sciences CenterShreveportUSA

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