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Physiol Behav. 1996 Nov;60(5):1369-74.

Cold-induced heat shock protein expression in rat aorta and brown adipose tissue.

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  • 1Department of Pharmacology and Toxicology, University of North Dakota School of Medicine, Grand Forks 58201-9037, USA.

Abstract

Recent reports indicate that Heat Shock Proteins (HSPs) are induced in mammalian tissues as part of a homeostatic response to environmental stressors. Administration of sympathomimetic drugs and neuroendocrine stress hormones has been shown to evoke an HSP response in unstressed animals indicating that cell signaling events exists that couple specific neurotransmitter/hormone-receptor interactions with HSP expression in mammalian tissues. Herein, we demonstrate that exposure of rats to a cold ambient temperature (6 degrees C) results in increased expression of constitutive and inducible members of the HSP70 gene family in association with increased expression of the mitochondrial uncoupling protein in brown adipose tissue (BAT). Increased HSP70 expression was not restricted to BAT because HSP70 was also induced in the aorta. This cold-induced HSP response is characterized by a transient increase in HSP70 protein and mRNA in both tissues during continued exposure. Ganglionic blockade prevented cold-induced HSP70 expression in BAT and aorta, indicating that sympathetic activity is requisite to this response. Administration of the alpha 1-adrenergic receptor antagonist, prazosin, also blocked expression, further delineating possible signaling mechanisms mediating this response. Apparently, cells in some mammalian tissues have adopted unique cellular regulatory mechanisms to support HSP induction that have been incorporated into the physiological response of the entire organism to an environmental stressor.

PMID:
8916196
[PubMed - indexed for MEDLINE]
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