Inhibition of the oxidative stress response by heat stress in<i>Caenorhabditis elegans</i>

Crombie, Timothy A.; Tang, Lanlan; Choe, Keith P.; Julian, David

doi:10.1242/jeb.135327

Cited by 20 publications

(27 citation statements)

References 78 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Lack of induction and/or suppression of mRNA levels of antioxidants at the elevated temperatures (such that induce molecular chaperones) may indicate antagonistic interactions between the transcriptional activation of antioxidant response and heat shock pathways in C. fluminea . Similar antagonism between the heat shock (HSR) and oxidative stress (OxSR) response has been shown in a model organism C. elegans 53. Prioritization of heat shock over antioxidant response may come at a cost of oxidative damage to the tissues, as indicated by accumulation of oxidative lesions (MDA and 4-HNE) and ubiquitinated proteins in the CR and CWD clams at high temperatures (32–38 °C).…”

Section: Discussionmentioning

confidence: 64%

Long-Term Acclimation to Different Thermal Regimes Affects Molecular Responses to Heat Stress in a Freshwater Clam Corbicula Fluminea

Falfushynska

Phan

Sokolova

2016

Sci Rep

View full text Add to dashboard Cite

Global climate change (GCC) can negatively affect freshwater ecosystems. However, the degree to which freshwater populations can acclimate to long-term warming and the underlying molecular mechanisms are not yet fully understood. We used the cooling water discharge (CWD) area of a power plant as a model for long-term warming. Survival and molecular stress responses (expression of molecular chaperones, antioxidants, bioenergetic and protein synthesis biomarkers) to experimental warming (20–41 °C, +1.5 °C per day) were assessed in invasive clams Corbicula fluminea from two pristine populations and a CWD population. CWD clams had considerably higher (by ~8–12 °C) lethal temperature thresholds than clams from the pristine areas. High thermal tolerance of CWD clams was associated with overexpression of heat shock proteins HSP70, HSP90 and HSP60 and activation of protein synthesis at 38 °C. Heat shock response was prioritized over the oxidative stress response resulting in accumulation of oxidative lesions and ubiquitinated proteins during heat stress in CWD clams. Future studies should determine whether the increase in thermal tolerance in CWD clams are due to genetic adaptation and/or phenotypic plasticity. Overall, our findings indicate that C. fluminea has potential to survive and increase its invasive range during warming such as expected during GCC.

show abstract

Section: Discussionmentioning

confidence: 64%

Long-Term Acclimation to Different Thermal Regimes Affects Molecular Responses to Heat Stress in a Freshwater Clam Corbicula Fluminea

Falfushynska

Phan

Sokolova

2016

Sci Rep

View full text Add to dashboard Cite

show abstract

“…Increased HSP expression has also been shown to be mediated by activation of the transcription factor HSF-1, which is in an inactive monomeric state in unstressed cells. 21,22 These results and findings suggest that under heat stress, SWHE may promote HSP- worm. L1 worms preincubated with SHWE for 72 hours at 20°C were exposed to heat stress for 8 hours at 35°C on the nematode growth medium agar plates.…”

mentioning

confidence: 63%

A Hot Water Extract of Sideritis scardica Prolongs Life Span and Enhances Heat Shock Resistance in Caenorhabditis elegans

Nishioka

Nishikawa²,

Shibata

2020

Natural Product Communications

View full text Add to dashboard Cite

Sideritis scardica is a Lamiaceae plant that is endemic to the alpine zone of the Balkan Peninsula. The tea of S. scardica has been handed down as a “tea of longevity” in the Rhodope region of Bulgaria for an unknown amount of time. In this study, we prepared a hot water extract of S. scardica (SHWE) and examined its effects on both life span and stress response in living tissue using Caenorhabditis elegans and its transgenic mutants. The life span of wild-type N2 worms was prolonged by approximately 15% at the SHWE concentration of 5 µg/mL and approximately 22% at the SHWE concentration of 50 µg/mL, as compared with the control group. The effect of SHWE on the expression of heat shock protein 16.2 (HSP-16.2) under heat stress was investigated using TJ375 worms, a transgenic mutant of C. elegans. In the TJ375 worms pretreated with SHWE, the fluorescence intensity of green fluorescent protein fluorescence, which indicates the expression of HSP-16.2, was significantly increased. In the assay using TJ356 worms, the worms pretreated with SHWE did not show the translocation of DAF-16, a forkhead transcription factor class O homolog, from the cytoplasm to nucleus under heat stress. Additionally, under heat stress, the pretreatment of SHWE improved the survival rate of GR1307 worms, a knockout mutant of daf-16. These results indicate that SHWE enhances HSP-16.2 expression through a stress-response pathway (eg, HSF-1 pathway) other than the DAF-16 pathway, resulting in a prolonged life span of C. elegans under heat stress.

show abstract

“…In C. elegans , induction of molecular chaperone proteins under various types of cellular stress is primarily regulated by HSF-1, a FOXO-family transcription factor (TF; DAF-16), or a Nrf family TF (SKN-1) [ 49 , 50 ]. Because SKN-1 regulates the oxidative stress response [ 51 , 52 ] and does not respond to heat shock treatment [ 53 ], we did not study it in the following experiment. To determine which TF induces the expression of C09F5.1 upon heat shock, we analyzed the expression pattern of C09F5.1 in worms harboring mutations in HSF-1 or DAF-16 (see Figure 3 C).…”

Section: Resultsmentioning

confidence: 99%

Caenorhabditis elegans BRICHOS Domain–Containing Protein C09F5.1 Maintains Thermotolerance and Decreases Cytotoxicity of Aβ42 by Activating the UPR

Song

Kim

et al. 2018

Genes

View full text Add to dashboard Cite

Caenorhabditis elegans C09F5.1 is a nematode-specific gene that encodes a type II transmembrane protein containing the BRICHOS domain. The gene was isolated as a heat-sensitive mutant, but the function of the protein remained unclear. We examined the expression pattern and subcellular localization of C09F5.1 as well as its roles in thermotolerance and chaperone function. Expression of C09F5.1 under heat shock conditions was induced in a heat shock factor 1 (HSF-1)–dependent manner. However, under normal growth conditions, most cells types exposed to mechanical stimuli expressed C09F5.1. Knockdown of C09F5.1 expression or deletion of the N-terminal domain decreased thermotolerance. The BRICHOS domain of C09F5.1 did not exhibit chaperone function unlike those of other proteins containing this domain, but the domain was essential for the proper subcellular localization of the protein. Intact C09F5.1 was localized to the Golgi body, but the N-terminal domain of C09F5.1 (C09F5.1-NTD) was retained in the ER. C09F5.1-NTD delayed paralysis by beta-amyloid (1-42) protein (Aβ42) in Alzheimer’s disease model worms (CL4176) and activated the unfolded protein response (UPR) by interacting with Aβ42. An intrinsically disordered region (IDR) located at the N-terminus of C09F5.1 may be responsible for the chaperone function of C09F5.1-NTD. Taken together, the data suggest that C09F5.1 triggers the UPR by interacting with abnormal proteins.

show abstract

Inhibition of the oxidative stress response by heat stress inCaenorhabditis elegans

Cited by 20 publications

References 78 publications

Long-Term Acclimation to Different Thermal Regimes Affects Molecular Responses to Heat Stress in a Freshwater Clam Corbicula Fluminea

Long-Term Acclimation to Different Thermal Regimes Affects Molecular Responses to Heat Stress in a Freshwater Clam Corbicula Fluminea

A Hot Water Extract of Sideritis scardica Prolongs Life Span and Enhances Heat Shock Resistance in Caenorhabditis elegans

Caenorhabditis elegans BRICHOS Domain–Containing Protein C09F5.1 Maintains Thermotolerance and Decreases Cytotoxicity of Aβ42 by Activating the UPR

Contact Info

Product

Resources

About