HSP72 can protect cells from heat-induced apoptosis by accelerating the inactivation of stress kinase JNK

Volloch, Vladimir; Gabai, Vladimir L.; Rits, Sophia; Force, Thomas; Sherman, Michael Y.

doi:10.1379/1466-1268(2000)005<0139:hcpcfh>2.0.co;2

Cited by 46 publications

(33 citation statements)

References 33 publications

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“…HSP72 is postulated to ameliorate insulin resistance by direct inhibition of JNK (13,42) and accelerating the rate of JNK dephosphorylation (53). Consistent with this, we observed that GGA decreased the phosphorylation of JNK in high-fatfed mice.…”

Section: Discussionsupporting

confidence: 88%

An acylic polyisoprenoid derivative, geranylgeranylacetone protects against visceral adiposity and insulin resistance in high-fat-fed mice

Adachi

Kondo

Ogawa

et al. 2010

American Journal of Physiology-Endocrinology and Metabolism

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Section: Discussionsupporting

confidence: 88%

An acylic polyisoprenoid derivative, geranylgeranylacetone protects against visceral adiposity and insulin resistance in high-fat-fed mice

Adachi

Kondo

Ogawa

et al. 2010

American Journal of Physiology-Endocrinology and Metabolism

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“…Two different mechanisms may contribute to this function. Sherman and colleagues have suggested that Hsp70 reduces JNK activity by increasing the rate of its dephosphorylation (Meriin et al, 1999;Volloch et al, 2000;Gabai et al, 2000a). An alternative mechanism is suggested by studies of Park et al (2001a) who provided evidence that Hsp70 binds to JNK to prevent its phosphorylation by upstream kinases.…”

Section: How Do Hsp Protect Cells Against Oxidative Damage?mentioning

confidence: 99%

Cellular response to oxidative stress: Signaling for suicide and survival*

Martindale

Holbrook

2002

Journal Cellular Physiology

2,094

1,596

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Reactive oxygen species (ROS), whether produced endogenously as a consequence of normal cell functions or derived from external sources, pose a constant threat to cells living in an aerobic environment as they can result in severe damage to DNA, protein, and lipids. The importance of oxidative damage to the pathogenesis of many diseases as well as to degenerative processes of aging has becoming increasingly apparent over the past few years. Cells contain a number of antioxidant defenses to minimize fluctuations in ROS, but ROS generation often exceeds the cell's antioxidant capacity, resulting in a condition termed oxidative stress. Host survival depends upon the ability of cells and tissues to adapt to or resist the stress, and repair or remove damaged molecules or cells. Numerous stress response mechanisms have evolved for these purposes, and they are rapidly activated in response to oxidative insults. Some of the pathways are preferentially linked to enhanced survival, while others are more frequently associated with cell death. Still others have been implicated in both extremes depending on the particular circumstances. In this review, we discuss the various signaling pathways known to be activated in response to oxidative stress in mammalian cells, the mechanisms leading to their activation, and their roles in influencing cell survival. These pathways constitute important avenues for therapeutic interventions aimed at limiting oxidative damage or attenuating its sequelae. Published 2002 Wiley‐Liss, Inc.

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“…The extent of activation of these pathways may affect the fate of cells exposed to heat shock. Indeed, inhibition of JNK dramatically suppressed heat-induced apoptosis of lymphoid cells (11,40,58) and rat fibroblasts (60), whereas inhibition of Akt or ERK strongly increased apoptosis (35,61).…”

Section: Cell Death and Survival Pathways Activated By Heat Shockmentioning

confidence: 99%

Invited Review: Interplay between molecular chaperones and signaling pathways in survival of heat shock

Gabai

Sherman

2002

Journal of Applied Physiology

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156

109

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. Invited Review: Interplay between molecular chaperones and signaling pathways in survival of heat shock. J Appl Physiol 92: 1743-1748, 2002; 10.1152/ japplphysiol.01101.2001.-Heat shock of mammalian cells causes protein damage and activates a number of signaling pathways. Some of these pathways enhance the ability of cells to survive heat shock, e.g., induction of molecular chaperones [heat shock protein (HSP) HSP72 and HSP27], activation of the protein kinases extracellular signal-regulated kinase and Akt, and phosphorylation of HSP27. On the other hand, heat shock can activate a stress kinase, c-Jun NH 2-terminal kinase, thus triggering both apoptotic and nonapoptotic cell death programs. Recent data indicate that kinases activated by heat shock can regulate synthesis and functioning of the molecular chaperones, and these chaperones modulate activity of the cell death and survival pathways. Therefore, the overall balance of the pathways and their interplay determine whether a cell exposed to heat shock will die or survive and become stress tolerant. thermotolerance; heat shock proteins; mitogen-activated protein kinases; apoptosis EXPOSURE OF MAMMALIAN CELLS to elevated temperatures (heat shock) triggers several signaling pathways, some that facilitate cell survival and some that initiate cell death programs. The outcome of a cell's exposure to heat shock may be either a development of a state of tolerance to heat shock and other stresses, if survival pathways prevail, or cell death, if death pathways prevail. The first-discovered survival pathway activated by heat shock was the heat shock response, i.e., induction of heat shock proteins (HSPs) such as HSP72, HSP27, HSP40, and HSP90, mediated by heat shock transcription factors (HSFs) (see Ref. 46 for a recent review). HSPs confer thermotolerance as well as resistance to other stresses, such as ethanol, heavy metals, oxidative stress, ischemia, or tumor necrosis factor (see Refs. 16 and 23 for review).Heat shock causes extensive denaturation and aggregation of intracellular proteins; therefore, early studies focused on the search of labile critical proteins whose damage when exposed to heat shock may lead to cell death (see Refs. 25 and 26 for review). Among major proteins easily denatured and aggregated in heat-shocked cells were components of nuclear matrix and cytoskeleton (2,25,26,31,41), although it should be noted that there are no data directly linking damage of these proteins to cell death. HSPs serve as molecular chaperones in refolding, disaggregation, and degradation of damaged polypeptides (see Refs. 15 and 21 for review). In fact, aggregation of nuclear proteins as well as a reporter enzyme (firefly luciferase) after heat shock was reduced in thermotolerant cells expressing HSPs, and these cells demonstrated faster solubilization of aggregated proteins during the recovery period (2,26,42,53). Furthermore, expression of HSP72 (the major inducible member of the HSP70 family) alone was sufficient to reduce nuclear protein aggregation and accelera...

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HSP72 can protect cells from heat-induced apoptosis by accelerating the inactivation of stress kinase JNK

Cited by 46 publications

References 33 publications

An acylic polyisoprenoid derivative, geranylgeranylacetone protects against visceral adiposity and insulin resistance in high-fat-fed mice

An acylic polyisoprenoid derivative, geranylgeranylacetone protects against visceral adiposity and insulin resistance in high-fat-fed mice

Cellular response to oxidative stress: Signaling for suicide and survival*

Invited Review: Interplay between molecular chaperones and signaling pathways in survival of heat shock

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