Heat shock protects neuronal cells from programmed cell death by apoptosis

Mailhos, Carolina; Howard, M. Keith; Latchman, David S.

doi:10.1016/0306-4522(93)90428-i

Cited by 155 publications

(90 citation statements)

References 36 publications

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“…expression also preconditions the worms against subsequent high temperature challenge that would rather be lethal to the organism development. Several studies have reported HSP to correlate with acquired stress resistance termed hormesis, which is the ability of a moderate stress to protect the animal from a subsequent and lethal stress (Lindquist and Craig, 1988;Jaattela and Wissing, 1992;Mailhos et al, 1993;Hercus et al, 2003). The detectable decrease in the expression of CeHSP17 at a high temperature of 408C, and even at subsequent 428C degree challenge is not clear, but may be explained by the lack of protein translation at such high temperatures which hinder the steps involved in protein synthesis (Sciandra and Subjeck, 1984).…”

Section: Discussionmentioning

confidence: 99%

Chemical Signals of Vector Beetle Facilitate the Prevalence of a Native Fungus and the Invasive Pinewood Nematode

Zhang

Lü

et al. 2017

Journal of Nematology

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Small heat shock proteins (sHSP) are ubiquitously found in all organisms, and with other heat shock proteins (HSP) such as HSP60, HSP70, HSP90, HSP100 made up the molecular chaperone family. They are involved in a wide range of biological processes which include among others cell resistance to biological and environmental stress conditions. In this study, we show by western blotting that CeHSP17, an sHSP of Caenorhabiditis elegans, is significantly induced by high temperatures. Furthermore, in response to metal stress, the CeHSP17 protein expression was significantly induced by cadmium and zinc at high concentration of clearly cytotoxic range in wild-type C. elegans. Altogether, our results show the involvement of CeHSP17 protein in both environmental and biological stresses in C. elegans and establish for the first time the expression pattern of the CeHSP17 protein in response to thermal and metal stress conditions in C. elegans. The responses of CeHSP17 protein expression may serve as potential sensitive biomarker for metal-induced toxicity monitoring and environmental risk assessment.

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Section: Discussionmentioning

confidence: 99%

Chemical Signals of Vector Beetle Facilitate the Prevalence of a Native Fungus and the Invasive Pinewood Nematode

Zhang

Lü

et al. 2017

Journal of Nematology

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“…Exposure of neurons to elevated temperature is sufficient to induce the heat shock response and to provide neuroprotection (Mailhos et al, 1993). The major role of HSP-60 is its involvement in the folding of proteins during mitochondrial import.…”

Section: Discussionmentioning

confidence: 99%

Genomic and proteomic analysis of the effects of cannabinoids on normal human astrocytes

et al. 2008

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Delta-9-tetrahydrocannabinol (Δ 9 -THC), the main psychoactive component of marijuana, is known to dysregulate various immune responses. Cannabinoid (CB)-1 and -2 receptors are expressed mainly on cells of the central nervous system (CNS) and the immune system. The CNS is the primary target of cannabinoids and astrocytes are known to play a role in various immune responses. Thus we undertook this investigation to determine the global molecular effects of cannabinoids on normal human astrocytes (NHA) using genomic and proteomic analyses. NHA were treated with Δ 9 -THC and assayed using gene microarrays and two-dimensional (2D) difference gel electrophoresis (DIGE) coupled with mass spectrometry (MS) to elucidate their genomic and proteomic profiles respectively. Our results show that the expression of more than 20 translated protein gene products from NHA was differentially dysregulated by treatment with Δ 9 -THC compared to untreated, control NHA.

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“…In addition, intracellular problems (spontaneous transcriptional and translational errors, sudden increase in protein synthesis or excess of synthesized subunits, incorrect cellular localization, or the damaging effect of highly reactive free radicals) as well as extracellular stressors (high temperature, hypoxia, radiation, toxic chemicals, endotoxins, and osmotic pressure) can alter the folding capacity of a cell leading to translational arrest as well as the accumulation of misfolded or unfolded proteins. [9][10][11][12][13][14] To insure protein homeostasis, cells employ several systems. These include intracellular removal or processing of misfolded proteins, 15 involving cellular chaperones, the ubiquitin-proteasome system, and autophagy.…”

Section: Basic Conceptsmentioning

confidence: 99%

Heat shock response and autophagy—cooperation and control

2015

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Abbreviations: AKT, v-akt murine thymoma viral oncogene homolog 1; AMPK, adenosine monophosphate-activated protein kinase; ATG, autophagy-related; BECN1, Beclin 1, autophagy related; EIF4EBP1, eukaryotic translation initiation factor 4E binding protein 1; ER, endoplasmic reticulum; FOXO, forkhead box O; HSF1, heat shock transcription factor 1; HSP, heat shock protein; HSPA8/ HSC70, heat shock 70kDa protein 8; IL, interleukin; LC3, MAP1LC3, microtubule-associated protein 1 light chain 3; MTMR14/ hJumpy, myotubularin related protein 14; MTOR, mechanistic target of rapamycin; NR1D1/Rev-Erb-a, nuclear receptor subfamily 1, group D, member 1; PBMC, peripheral blood mononuclear cell; PPARGC1A/PGC-1a, peroxisome proliferator-activated receptor, gamma, coactivator 1 a; RHEB, Ras homolog enriched in brain; SOD, superoxide dismutase; SQSTM1/p62, sequestosome 1; TPR, translocated promoter region, nuclear basket protein; TSC, tuberous sclerosis complex; ULK1, unc-51 like autophagy activating kinase 1.Protein quality control (proteostasis) depends on constant protein degradation and resynthesis, and is essential for proper homeostasis in systems from single cells to whole organisms. Cells possess several mechanisms and processes to maintain proteostasis. At one end of the spectrum, the heat shock proteins modulate protein folding and repair. At the other end, the proteasome and autophagy as well as other lysosome-dependent systems, function in the degradation of dysfunctional proteins. In this review, we examine how these systems interact to maintain proteostasis. Both the direct cellular data on heat shock control over autophagy and the time course of exercise-associated changes in humans support the model that heat shock response and autophagy are tightly linked. Studying the links between exercise stress and molecular control of proteostasis provides evidence that the heat shock response and autophagy coordinate and undergo sequential activation and downregulation, and that this is essential for proper proteostasis in eukaryotic systems.

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Heat shock protects neuronal cells from programmed cell death by apoptosis

Cited by 155 publications

References 36 publications

Chemical Signals of Vector Beetle Facilitate the Prevalence of a Native Fungus and the Invasive Pinewood Nematode

Chemical Signals of Vector Beetle Facilitate the Prevalence of a Native Fungus and the Invasive Pinewood Nematode

Genomic and proteomic analysis of the effects of cannabinoids on normal human astrocytes

Heat shock response and autophagy—cooperation and control

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