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Heat shock proteins and hypometabolism: adaptive strategy for proteome preservation

Authors Storey KB, Storey JM

Published 30 March 2011 Volume 2011:2 Pages 57—68

DOI https://doi.org/10.2147/RRB.S13351

Review by Single-blind

Peer reviewer comments 2

Kenneth B Storey, Janet M Storey
Departments of Biology and Chemistry, Carleton University, Ottawa, ON, Canada

Abstract: To survive under harsh environmental conditions many organisms retreat into hypometabolic states where metabolic rate may be reduced by 80% or more and energy use is reprioritized to emphasize key functions that sustain viability and provide cytoprotection. ATP-expensive activities, such as gene expression, protein turnover (synthesis and degradation), and the cell cycle, are largely shut down. As a consequence, mechanisms that stabilize the existing cellular proteome can become critical for long-term survival. Heat shock proteins (HSPs) are well-known for their actions as chaperones that act to fold new proteins or refold proteins that are damaged. Indeed, they are part of the “minimal stress proteome” that appears to be a ubiquitous response by all cells as they attempt, successfully or unsuccessfully, to deal with stress. The present review summarizes evidence that HSPs are also a conserved feature of natural animal hypometabolism including the phenomena of estivation, hibernation, diapause, cold-hardiness, anaerobiosis, and anhydrobiosis. That is, organisms that retreat into dormant or torpid states in anticipation that environmental conditions may become too difficult for normal life also integrate the use of HSPs to protect their proteome while hypometabolic. Multiple studies show a common upregulation of expression of hsp genes and/or HSP proteins prior to or during hypometabolism in organisms as diverse as ground squirrels, turtles, land snails, insects, and brine shrimp and in situations of both preprogrammed dormancies (eg, seasonal or life stage specific) and opportunistic hypometabolism (eg, triggered by desiccation or lack of oxygen). Hence, HSPs are not just a “shock” response that attempts to rescue cells from damaging stress but are a key protective strategy that is an integral component of natural states of torpor and dormancy.

Keywords: chaperone proteins, metabolic rate depression, estivation, anaerobiosis, hibernation, diapause, cold-hardiness
 

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