Sulforaphane Activates Heat Shock Response and Enhances Proteasome Activity through Up-regulation of Hsp27

Gan, Nanqin; Wu, Yu-Chieh; Brunet, Mathilde; Garrido, Carmen; Chung, Fung‐Lung; Dai, Chengkai; Mi, Lixin

doi:10.1074/jbc.m110.152686

Cited by 126 publications

(99 citation statements)

References 47 publications

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“…Related to oxidative stress, it has been observed a NRF2-dependent induction of proteasome required for adaptation to the stress [55]. These data were corroborated by the fact that an NRF2 inducer, sulforaphane (SFN), increases the expression of NRF2-regulated genes as well as the expression of the catalytic subunits of the proteasome and proteasomal peptidase activities [56,57]. The ubiquitin-proteasome system and autophagy are crucial for maintaining the proteostasis and are interdependent pathways.…”

Section: Nrf2 Modulation Of Proteostasis Oxidative Stress and Inflamsupporting

confidence: 60%

Role of the Transcription Factor Nrf2 in Parkinson’s Disease: New Insights

Lastres‐Becker¹

2017

J Alzheimers Dis Parkinsonism

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Section: Nrf2 Modulation Of Proteostasis Oxidative Stress and Inflamsupporting

confidence: 60%

Role of the Transcription Factor Nrf2 in Parkinson’s Disease: New Insights

Lastres‐Becker¹

2017

J Alzheimers Dis Parkinsonism

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“…While no other heat shock proteins were induced in this study, the different methods and the chosen cutoff values for analysis could explain the discrepancies between the two studies. In eukaryotes, the sulforaphane analogue 6-methylsulfinyl hexyl isothiocyanate provokes transthiocarbamoylation of proteins, including the heat shock protein HSP90␤, which results in the induction of the heat shock response (74) and the stimulation of proteasome activity (75). This shared heat shock induction in both prokaryotic and eukaryotic cells in BITC.…”

Section: Discussionmentioning

confidence: 99%

Insights into the Mode of Action of Benzyl Isothiocyanate on Campylobacter jejuni

Dufour

Ståhl

Rosenfeld

et al. 2013

Appl Environ Microbiol

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cCampylobacter jejuni is a widespread pathogen responsible for most of the food-borne gastrointestinal diseases in Europe. The use of natural antimicrobial molecules is a promising alternative to antibiotic treatments for pathogen control in the food industry. Isothiocyanates are natural antimicrobial compounds, which also display anticancer activity. Several studies described the chemoprotective effect of isothiocyanates on eukaryotic cells, but the antimicrobial mechanism is still poorly understood. We investigated the early cellular response of C. jejuni to benzyl isothiocyanate by both transcriptomic and physiological approaches. The transcriptomic response of C. jejuni to benzyl isothiocyanate showed upregulation of heat shock response genes and an impact on energy metabolism. Oxygen consumption was progressively impaired by benzyl isothiocyanate treatment, as revealed by high-resolution respirometry, while the ATP content increased soon after benzyl isothiocyanate exposition, which suggests a shift in the energy metabolism balance. Finally, benzyl isothiocyanate induced intracellular protein aggregation. These results indicate that benzyl isothiocyanate affects C. jejuni by targeting proteins, resulting in the disruption of major metabolic processes and eventually leading to cell death.

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“…20) Briefly, PC12 cells were seeded in 6-well plates and incubated at 37°C in a CO 2 incubator for 24 h until confluence reached 70-80% and transfected with HSE-luc, a plasmid containing an inducible Rat Hsp70 promoter-driven luciferase reporter gene, by lipofectamine 2000 (Invitrogen) following the manufacturer's instructions. After 24 h of growth, cells were treated with either 5 µM Zligustilide for up to 4 h. As a positive control, cells were heatshocked at 42°C for 30 min and incubated at 37°C for 3 h and 30 min.…”

Section: Methodsmentioning

confidence: 99%

Protective HSP70 Induction by Z-Ligustilide against Oxygen–Glucose Deprivation Injury <i>via</i> Activation of the MAPK Pathway but Not of HSF1

Jiang

Ning

et al. 2015

Biological & Pharmaceutical Bulletin

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Key words Z-ligustilide; heat-shock protein 70; mitogen-activated protein kinase; oxygen-glucose deprivation-reoxygenation; heat-shock factor 1The World Health Organization (WHO) Global Infobase reports that stroke has become the second leading cause of mortality in the world, causing around 6000000 deaths annually. 1)However, there are currently relatively few treatment options available to minimize damage or death following a stroke. Protein aggregates containing ubiquitinated proteins are commonly present in neurodegenerative disorders and have been considered to cause neuronal degeneration. The previous study also showed that transient cerebral ischemia caused severe protein aggregation in hippocampal CA1 neurons which appeared at 4 h and progressively accumulated at 24 and 48 h. 2)Therefore, control of protein aggregation may represent an alternative treatment to neurological damage caused by ischemic stroke.Heat shock proteins (HSPs) are a group of phylogenetically and ubiquitous cytoprotective proteins found in all prokaryotic and eukaryotic cells, many of which are chaperone molecules that facilitate protein folding, trafficking and also prevent their aggregation and degradation.3) Heat shock protein 70 (HSP70) is a major inducible heat shock protein that basically functions as a molecular chaperone and plays an important role in preventing protein aggregation, degrading unstable and misfolded proteins and transporting proteins between cellular compartments.4) It's reported that over-expression of HSP70 via transgenes and viruses or systemic administration of HSP70 fusion proteins that allow it to cross the blood brain barrier protects the brain against ischemia, 5,6) suggesting that increasing HSP70 level or activity may be a potential therapeutic target for pharmacological intervention of ischemic diseases.Ligusticum chuanxiong is a commonly used Chinese herbal medicine with its empiric treatment of cardiovascular and cerebrovascular diseases.7) Z-Ligustilide as the major bioactive phthalide compound of Rhizoma chuanxiong was previously suggested for the prevention and treatment of ischemic stroke. 8,9) Our and others' studies showed that Z-ligustilide could protect ischemic injury both in vitro and in vivo via the induction of direct and indirect antioxidant response. 8,10,11) However, its effect on the heat shock response, a highly conserved and fundamental cytoprotective mechanism, under ischemic stress remains unexplored. Along this line, we characterized the effect of Z-ligustilide on HSP70 and explored the potential role of HSP70 in the protection of Z-ligustilide against oxygen-glucose deprivation and reoxygenation (OGDReoxy) induced injury in this study.

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Sulforaphane Activates Heat Shock Response and Enhances Proteasome Activity through Up-regulation of Hsp27

Cited by 126 publications

References 47 publications

Role of the Transcription Factor Nrf2 in Parkinson’s Disease: New Insights

Role of the Transcription Factor Nrf2 in Parkinson’s Disease: New Insights

Insights into the Mode of Action of Benzyl Isothiocyanate on Campylobacter jejuni

Protective HSP70 Induction by Z-Ligustilide against Oxygen–Glucose Deprivation Injury <i>via</i> Activation of the MAPK Pathway but Not of HSF1

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