Transient cold shock induces the heat shock response upon recovery at 37 degrees C in human cells.

Liu, A. Y.-C.; Bian, Hongjin; Huang, Lanqing; Lee, Yoon Kwang

doi:10.1016/s0021-9258(17)36691-7

Cited by 94 publications

(11 citation statements)

References 41 publications

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“…A previous study showed that exposure to a cold temperature (4 °C) increases the level of tau phosphorylation in 3xTg-AD mice ( 36 ). Together with our studies, these findings lead us to speculate that the stress of a temperature change, either low or high temperature, may increase the level of Hsp90 ( 37 ) and lead to increased γ-secretase complex formation and Aβ production. Hsp90 accounts for 1–2% of protein in a normal, unstressed cell; however, when cells become stressed, the level of Hsp90 increases up to 3–5% ( 38 , 39 , 40 ).…”

Section: Discussionsupporting

confidence: 78%

High temperature promotes amyloid β-protein production and γ-secretase complex formation via Hsp90

Noorani

Yamashita

Gao

et al. 2020

Journal of Biological Chemistry

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Alzheimer’s disease (AD) is characterized by neuronal loss and accumulation of amyloid β-protein (Aβ) in the brain parenchyma. Sleep impairment is associated with AD and affects about 25-40% of patients in the mild-to-moderate stages of the disease. Sleep deprivation leads to increased Aβ production; however, its mechanism remains largely unknown. We hypothesized that the increase in core body temperature induced by sleep deprivation may promote Aβ production. Here, we report temperature-dependent regulation of Aβ production. We found that an increase in temperature, from 37°C to 39°C, significantly increased Aβ production in amyloid precursor protein-overexpressing cells. We also found that high temperature (39°C) significantly increased the expression levels of heat shock protein 90 (Hsp90) and the C-terminal fragment of presenilin 1 (PS1-CTF), and promoted γ-secretase complex formation. Interestingly, Hsp90 was associated with the components of the premature γ-secretase complex, anterior pharynx defective-1 (APH-1) and nicastrin (NCT), but was not associated with PS1-CTF or presenilin enhancer-2. Hsp90 knockdown abolished the increased level of Aβ production and the increased formation of the γ-secretase complex at high temperature in culture. Furthermore, with in vivo experiments, we observed increases in the levels of Hsp90, PS1-CTF, NCT, and the γ-secretase complex in the cortex of mice housed at higher room temperature (30°C) compared with those housed at standard room temperature (23°C). Our results suggest that high temperature regulates Aβ production by modulating γ-secretase complex formation through the binding of Hsp90 to NCT/APH-1.

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Section: Discussionsupporting

confidence: 78%

High temperature promotes amyloid β-protein production and γ-secretase complex formation via Hsp90

Noorani

Yamashita

Gao

et al. 2020

Journal of Biological Chemistry

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“…Thus, cold-induced cell damage may lead to heat shock-like response. In several studies demonstrating hypothermia-induced upregulation of HSP70, other stresses such as oxygen-glucose deprivation or ischemia were not applied [ 33 , 35 ]. Therefore, heat shock-like response might have been induced by hypothermia itself.…”

Section: Discussionmentioning

confidence: 99%

“…Third, expression of HSP70 requires active cell metabolism. Heat shock response can be activated only after reperfusion [ 33 ]. However, a recent in vitro study has shown hypothermia-induced upregulation of HSP70 during oxygen-glucose deprivation period [ 37 ].…”

Section: Discussionmentioning

confidence: 99%

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HSP70-mediated neuroprotection by combined treatment of valproic acid with hypothermia in a rat asphyxial cardiac arrest model

Park

Jeong

et al. 2021

PLoS ONE

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It has been reported that valproic acid (VPA) combined with therapeutic hypothermia can improve survival and neurologic outcomes in a rat asphyxial cardiac arrest model. However, neuroprotective mechanisms of such combined treatment of valproic acid with hypothermia remains unclear. We hypothesized that epigenetic regulation of HSP70 by histone acetylation could increase HSP70-mediated neuroprotection suppressed under hypothermia. Male Sprague-Dawley rats that achieved return of spontaneous circulation (ROSC) from asphyxial cardiac arrest were randomized to four groups: normothermia (37°C ± 1°C), hypothermia (33°C ± 1°C), normothermia + VPA (300 mg/kg IV initiated 5 minutes post-ROSC and infused over 20 min), and hypothermia + VPA. Three hours after ROSC, acetyl-histone H3 was highly expressed in VPA-administered groups (normothermia + VPA, hypothermia + VPA). Four hours after ROSC, HSP70 mRNA expression levels were significantly higher in normothermic groups (normothermia, normothermia + VPA) than in hypothermic groups (hypothermia, hypothermia + VPA). The hypothermia + VPA group showed significantly higher HSP70 mRNA expression than the hypothermia group. Similarly, at five hours after ROSC, HSP70 protein levels were significantly higher in normothermic groups than in hypothermic groups. HSP70 levels were significantly higher in the hypothermia + VPA group than in the hypothermia group. Only the hypothermia + VPA group showed significantly attenuated cleaved caspase-9 levels than the normothermia group. Hypothermia can attenuate the expression of HSP70 at transcriptional level. However, VPA administration can induce hyperacetylation of histone H3, leading to epigenetic transcriptional activation of HSP70 even in a hypothermic status. Combining VPA treatment with hypothermia may compensate for reduced activation of HSP70-mediated anti-apoptotic pathway.

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“…Future research should therefore apply a real-time biochemical indicator of cell injury, e.g. heat shock proteins [46,47], to distinguish between the factors of vibration, cold storage and re-warming and their contribution to necrosis or apoptosis. The effects of the addition of vibration to the cell samples shown at 50 Hz 48 h vibration were a transition from expression of annexin Vþ to an expression dominated by PIþ.…”

Section: Mode Of Cell Death Induced By Vibration and Cold Storagementioning

confidence: 99%

The sensitivity of human mesenchymal stem cells to vibration and cold storage conditions representative of cold transportation

Nikolaev

Liu

Hussein

et al. 2012

J. R. Soc. Interface.

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In the current study, the mechanical and hypothermic damage induced by vibration and cold storage on human mesenchymal stem cells (hMSCs) stored at 2-88C was quantified by measuring the total cell number and cell viability after exposure to vibration at 50 Hz (peak acceleration 140 m s 22 and peak displacement 1.4 mm), 25 Hz (peak acceleration 140 m s 22, peak displacement 5.7 mm), 10 Hz (peak acceleration 20 m s 22, peak displacement 5.1 mm) and cold storage for several durations. To quantify the viability of the cells, in addition to the trypan blue exclusion method, the combination of annexin V-FITC and propidium iodide was applied to understand the mode of cell death. Cell granularity and a panel of cell surface markers for stemness, including CD29, CD44, CD105 and CD166, were also evaluated for each condition. It was found that hMSCs were sensitive to vibration at 25 Hz, with moderate effects at 50 Hz and no effects at 10 Hz. Vibration at 25 Hz also increased CD29 and CD44 expression. The study further showed that cold storage alone caused a decrease in cell viability, especially after 48 h, and also increased CD29 and CD44 and attenuated CD105 expressions. Cell death would most likely be the consequence of membrane rupture, owing to necrosis induced by cold storage. The sensitivity of cells to different vibrations within the mechanical system is due to a combined effect of displacement and acceleration, and hMSCs with a longer cold storage duration were more susceptible to vibration damage, indicating a coupling between the effects of vibration and cold storage.

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Transient cold shock induces the heat shock response upon recovery at 37 degrees C in human cells.

Cited by 94 publications

References 41 publications

High temperature promotes amyloid β-protein production and γ-secretase complex formation via Hsp90

High temperature promotes amyloid β-protein production and γ-secretase complex formation via Hsp90

HSP70-mediated neuroprotection by combined treatment of valproic acid with hypothermia in a rat asphyxial cardiac arrest model

The sensitivity of human mesenchymal stem cells to vibration and cold storage conditions representative of cold transportation

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