Diallyl tetrasulfane activates both the eIF2α and Nrf2/HO-1 pathways

Saidu, Nathaniel Edward Bennett; Touma, Rania; Asali, Imad Abu; Jacob, Claus; Montenarh, Mathias

doi:10.1016/j.bbagen.2012.10.003

Cited by 30 publications

(33 citation statements)

References 37 publications

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“…This concept assumes that the cysteine proteins and enzymes in cells are sensors of oxidative stress, and that their sequential and often reversible oxidative modification during an oxidative onslaught triggers widespread cellular signalling which enables the cell to respond adequately, either by mounting an antioxidant defence or by shutting down via apoptosis [5]. In subsequent years, numerous studies have confirmed this idea of a gradual, measured and often complicated and cell type-specific response conveyed by cysteine proteins with different reactivity or sensitivity towards different oxidative modifiers [28,36,37,38,39,40]. …”

Section: The Year 2003: Gestalt Switch In the Field Of Rss Researchmentioning

confidence: 99%

“…Traditional thiol-based antioxidants may also be considered as reducing RSS, although one has to be extraordinarily careful here. Many of these antioxidants, such as diallyltrisulfide (DATS) or diallyltetrasulfide (DATTS), do not act as reducing agents at all, but oxidize certain cysteine proteins, such as Keap-1, thereby triggering cellular signalling cascades which eventually lead to an—indirect—antioxidant response [39,40]. …”

Section: What Are Rss?mentioning

confidence: 99%

“…The link between RSS and increased levels of oxidative stress is far from surprising, as RSS often consume reduced thiols and hence directly or indirectly lead to an increase of ROS concentrations. This kind of selective oxidation can be exploited in the therapy against microbes and is also under consideration in the context of cancer therapy [39,40,107,108,115]. Recent studies involving a wide spectrum of 1,2-dithiole-3-thiones have associated some of these sulfur compounds with the induction of cytoprotective Phase 2 enzymes, but also with the inhibition of histone deacetylase enzymes [116,117].…”

Section: Food For Thoughtmentioning

confidence: 99%

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The Reactive Sulfur Species Concept: 15 Years On

et al. 2017

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Fifteen years ago, in 2001, the concept of “Reactive Sulfur Species” or RSS was advocated as a working hypothesis. Since then various organic as well as inorganic RSS have attracted considerable interest and stimulated many new and often unexpected avenues in research and product development. During this time, it has become apparent that molecules with sulfur-containing functional groups are not just the passive “victims” of oxidative stress or simple conveyors of signals in cells, but can also be stressors in their own right, with pivotal roles in cellular function and homeostasis. Many “exotic” sulfur-based compounds, often of natural origin, have entered the fray in the context of nutrition, ageing, chemoprevention and therapy. In parallel, the field of inorganic RSS has come to the forefront of research, with short-lived yet metabolically important intermediates, such as various sulfur-nitrogen species and polysulfides (Sx2−), playing important roles. Between 2003 and 2005 several breath-taking discoveries emerged characterising unusual sulfur redox states in biology, and since then the truly unique role of sulfur-dependent redox systems has become apparent. Following these discoveries, over the last decade a “hunt” and, more recently, mining for such modifications has begun—and still continues—often in conjunction with new, innovative and complex labelling and analytical methods to capture the (entire) sulfur “redoxome”. A key distinction for RSS is that, unlike oxygen or nitrogen, sulfur not only forms a plethora of specific reactive species, but sulfur also targets itself, as sulfur containing molecules, i.e., peptides, proteins and enzymes, preferentially react with RSS. Not surprisingly, today this sulfur-centred redox signalling and control inside the living cell is a burning issue, which has moved on from the predominantly thiol/disulfide biochemistry of the past to a complex labyrinth of interacting signalling and control pathways which involve various sulfur oxidation states, sulfur species and reactions. RSS are omnipresent and, in some instances, are even considered as the true bearers of redox control, perhaps being more important than the Reactive Oxygen Species (ROS) or Reactive Nitrogen Species (RNS) which for decades have dominated the redox field. In other(s) words, in 2017, sulfur redox is “on the rise”, and the idea of RSS resonates throughout the Life Sciences. Still, the RSS story isn’t over yet. Many RSS are at the heart of “mistaken identities” which urgently require clarification and may even provide the foundations for further scientific revolutions in the years to come. In light of these developments, it is therefore the perfect time to revisit the original hypotheses, to select highlights in the field and to question and eventually update our concept of “Reactive Sulfur Species”.

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Section: The Year 2003: Gestalt Switch In the Field Of Rss Researchmentioning

confidence: 99%

Section: What Are Rss?mentioning

confidence: 99%

Section: Food For Thoughtmentioning

confidence: 99%

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The Reactive Sulfur Species Concept: 15 Years On

et al. 2017

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“…Dially trisulfide inhibits phorbol ester‐induced tumor promotion, activation of AP‐1, and expression of COX‐2 in mouse skin by blocking JNK and Akt signaling. Diallyl tetrasulfane activates both the ROS‐elF2alpha and Nrf2/HO‐1 pathways in HCT116 cells . The bactericidal effects of DAS have also been documented in laboratory rodents .…”

Section: Discussionmentioning

confidence: 99%

The effects of diallyl sulfide upon Porphyromonas gingivalis lipopolysaccharide stimulated proinflammatory cytokine expressions and nuclear factor‐kappa B activation in human gingival fibroblasts

Tsai

Chin

et al. 2014

J of Periodontal Research

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“…Nrf2 has been shown to be a key factor in the ARE-mediated induction of antioxidant proteins and the regulation of inflammatory responses in response to various stimuli (37,38). Rushworth et al reported that Nrf2 regulates LPS-induced HO-1 and NQO1 protein production and thus modulates the LPS-induced proinflammatory response (9).…”

Section: Discussionmentioning

confidence: 99%