Heat shock protein 70 in the rat nasal cavity: localisation and response to hyperthermia

Simpson, Sharon Anne; Alexander, David; Reed, Celia J.

doi:10.1007/s00204-004-0541-8

Cited by 10 publications

(14 citation statements)

References 50 publications

(57 reference statements)

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“…In the present study as well as in all studies examining the expression of stress-induced HSPs in the OE (Kilgour et al, 2000;Carr et al, 2001Carr et al, , 2004Simpson et al, 2004Simpson et al, , 2005, the predominant cell type exhibiting HSP upregulation was the sustentacular cell. This observation is surprising given our hypothesis of a P2R role in HSP induction, as P2Rs are present on both ORNs and sustentacular cells.…”

Section: Discussionmentioning

confidence: 76%

“…In support of our hypothesis for a purinergic role in HSP25 induction, we observed that strong odorant stimulated a 3-fold increase in ATP release from OE slices in vitro. Moreover, heat shock and toxic chemicals caused a reduction in intracellular ATP levels in a rat nasal explant culture system that was concurrent with an increase in HSP70 (Simpson et al, 2004(Simpson et al, , 2005.…”

Section: Discussionmentioning

confidence: 98%

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Purinergic receptor antagonists inhibit odorant‐induced heat shock protein 25 induction in mouse olfactory epithelium

Hegg

Lucero

2005

Glia

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Heat shock proteins (HSPs) accumulate in cells exposed to a variety of physiological and environmental factors, such as heat shock, oxidative stress, toxicants, and odorants. Ischemic, stressed, and injured cells release ATP in large amounts. Our hypothesis is that noxious stimulation (in this case, strong odorant) evokes the release of ATP in the olfactory epithelium (OE). Extracellular ATP, a signal of cellular stress, induces the expression of HSPs via purinergic receptors. In the present study, in vivo odorant exposure (heptanal or R-carvone) led to a selective induction of HSP25 in glia-like sustentacular cells in the Swiss Webster mouse OE, as previously shown in rats (Carr et al., 2001). Furthermore, in vitro and in vivo administration of purinergic receptor antagonists suramin and pyridoxalphosphate-6-azophenyl-2',4'-disulfonic acid (PPADS) blocked the expression of HSP25 immunoreactivity in sustentacular cells. ATP released by acutely injured cells could act as an early signal of cell and tissue damage, causing HSP expression and initiating a stress signaling cascade to protect against further damage. Sustentacular cells have a high capacity to detoxify xenobiotics and thereby protect the olfactory epithelium from airborne pollutants. Thus, the robust, rapid induction of HSPs in sustentacular cells may help maintain the integrity of the OE during exposure to toxicants.

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Section: Discussionmentioning

confidence: 76%

Section: Discussionmentioning

confidence: 98%

Purinergic receptor antagonists inhibit odorant‐induced heat shock protein 25 induction in mouse olfactory epithelium

Hegg

Lucero

2005

Glia

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“…Similarly, in the rat olfactory system, stress-induced HSP70 production occurs primarily in supporting (sustentacular) cells and not in olfactory sensory neurons (39). In addition, olfactory sensory neurons are protected by HSP induction (40). Targeted overexpression of HSP70 in astrocytes protects CA1 hippocampal neurons from death caused by transient forebrain ischemia (41).…”

Section: Figurementioning

confidence: 99%

Inner ear supporting cells protect hair cells by secreting HSP70

May¹,

Kramarenko²,

Brandon³

et al. 2013

J. Clin. Invest.

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Mechanosensory hair cells are the receptor cells of hearing and balance. Hair cells are sensitive to death from exposure to therapeutic drugs with ototoxic side effects, including aminoglycoside antibiotics and cisplatin. We recently showed that the induction of heat shock protein 70 (HSP70) inhibits ototoxic drug-induced hair cell death. Here, we examined the mechanisms underlying the protective effect of HSP70. In response to heat shock, HSP70 was induced in glia-like supporting cells but not in hair cells. Adenovirus-mediated infection of supporting cells with Hsp70 inhibited hair cell death. Coculture with heat-shocked utricles protected nonheatshocked utricles against hair cell death. When heat-shocked utricles from Hsp70 -/-mice were used in cocultures, protection was abolished in both the heat-shocked utricles and the nonheat-shocked utricles. HSP70 was detected by ELISA in the media surrounding heat-shocked utricles, and depletion of HSP70 from the media abolished the protective effect of heat shock, suggesting that HSP70 is secreted by supporting cells. Together our data indicate that supporting cells mediate the protective effect of HSP70 against hair cell death, and they suggest a major role for supporting cells in determining the fate of hair cells exposed to stress.

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“…The 2-and 6-h timepoints were selected based on literature indicating that HSP expression peaks 2-6 h after heat shock (Yoshida et al 1999;Simpson et al 2004). Utricles were homogenized, and total RNA was collected (RNAEasy, Qiagen).…”

Section: Real-time Quantitative Rt-pcrmentioning

confidence: 99%

“…In pilot experiments, we examined the effects of various temperatures and durations of heat shock, based on protocols found in the literature (Poe and O'Neill 1997;Braiden et al 2000;Ju and Tseng 2004;Simpson et al 2004). We found that exposure to temperatures above 44-C for periods as short as 10 min resulted in a significant loss of hair cells (data not shown).…”

Section: Development Of the Heat Shock Protocolmentioning

confidence: 99%

Heat Shock Inhibits both Aminoglycoside- and Cisplatin-Induced Sensory Hair Cell Death

Cunningham

Brandon

2006

JARO

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Human hearing and balance impairments are often attributable to the death of sensory hair cells in the inner ear. These cells are hypersensitive to death induced by noise exposure, aging, and some therapeutic drugs. Two major classes of ototoxic drugs are the aminoglycoside antibiotics and the antineoplastic agent cisplatin. Exposure to these drugs leads to hair cell death that is mediated by the activation of specific apoptotic proteins, including caspases. The induction of heat shock proteins (HSPs) in response to cellular stress is a ubiquitous and highly conserved response that can significantly inhibit apoptosis in some systems by inhibiting apoptotic proteins. Induction of HSPs occurs in hair cells in response to a variety of stimuli. Given that HSPs can directly inhibit apoptosis, we hypothesized that heat shock may inhibit apoptosis in hair cells exposed to ototoxic drugs. To test this hypothesis, we developed a method for inducing HSP expression in the adult mouse utricle in vitro. In vitro heat shock reliably produces a robust up-regulation of HSP-70 mRNA and protein, as well as more modest up-regulation of HSP-90 and HSP-27. The heat shock does not result in death of hair cells. Heat shock has a significant protective effect against both aminoglycoside-and cisplatin-induced hair cell death in the utricle preparation in vitro. These data indicate that heat shock can inhibit ototoxic drug-induced hair cell death, and that the utricle preparation can be used to examine the molecular mechanism(s) underlying this protective effect.

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Heat shock protein 70 in the rat nasal cavity: localisation and response to hyperthermia

Cited by 10 publications

References 50 publications

Purinergic receptor antagonists inhibit odorant‐induced heat shock protein 25 induction in mouse olfactory epithelium

Purinergic receptor antagonists inhibit odorant‐induced heat shock protein 25 induction in mouse olfactory epithelium

Inner ear supporting cells protect hair cells by secreting HSP70

Heat Shock Inhibits both Aminoglycoside- and Cisplatin-Induced Sensory Hair Cell Death

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