Phenylethyl isothiocyanate induces oxidative damage of porcine kidney cells mediated by reactive oxygen species

Zhu, Yuanyuan; Liu, Shuiping; Yan, Sisi; Wang, Ji; Zhang, Linyu; Li, Xin; Wen, Lixin; Wu, Jing

doi:10.1002/jbt.22428

Cited by 6 publications

(3 citation statements)

References 26 publications

(22 reference statements)

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“…Cells will produce reactive oxygen species during normal physiological metabolism. At the same time, some environmental factors, such as ultraviolet radiation, strong osmotic pressure, high or low temperature, and oxidation, can also induce the production of reactive oxygen species [ 27 ]. There are a variety of antioxidants in cells, including antioxidant macromolecules, antioxidant small molecules and enzymes, which can remove reactive oxygen species in cells.…”

Section: Resultsmentioning

confidence: 99%

Modular Assembly of Ordered Hydrophilic Proteins Improve Salinity Tolerance in Escherichia coli

Guo

Zhao

Tang

et al. 2021

IJMS

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Most late embryogenesis abundant group 3 (G3LEA) proteins are highly hydrophilic and disordered, which can be transformed into ordered α-helices to play an important role in responding to diverse stresses in numerous organisms. Unlike most G3LEA proteins, DosH derived from Dinococcus radiodurans is a naturally ordered G3LEA protein, and previous studies have found that the N-terminal domain (position 1–103) of DosH protein is the key region for its folding into an ordered secondary structure. Synthetic biology provides the possibility for artificial assembling ordered G3LEA proteins or their analogues. In this report, we used the N-terminal domain of DosH protein as module A (named DS) and the hydrophilic domains (DrHD, BnHD, CeHD, and YlHD) of G3LEA protein from different sources as module B, and artificially assembled four non-natural hydrophilic proteins, named DS + DrHD, DS + BnHD, DS + CeHD, and DS + YlHD, respectively. Circular dichroism showed that the four hydrophile proteins were highly ordered proteins, in which the α-helix contents were DS + DrHD (56.1%), DS + BnHD (53.7%), DS + CeHD (49.1%), and DS + YLHD (64.6%), respectively. Phenotypic analysis showed that the survival rate of recombinant Escherichia coli containing ordered hydrophilic protein was more than 10% after 4 h treatment with 1.5 M NaCl, which was much higher than that of the control group. Meanwhile, in vivo enzyme activity results showed that they had higher activities of superoxide dismutase, catalase, lactate dehydrogenase and less malondialdehyde production. Based on these results, the N-terminal domain of DosH protein can be applied in synthetic biology due to the fact that it can change the order of hydrophilic domains, thus increasing stress resistance.

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Section: Resultsmentioning

confidence: 99%

Modular Assembly of Ordered Hydrophilic Proteins Improve Salinity Tolerance in Escherichia coli

Guo

Zhao

Tang

et al. 2021

IJMS

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“…The importance of this class of molecules relies on their anticancer properties by downgrading the factors that are responsible for the cellular detoxification [50,64]. More specifically, ITCs can form an adduct with glutathione (GSH) during the mercapturic acid pathway, causing GSH depletion [65][66][67]. As a result, the levels of reactive oxygen species (ROS) are elevated, leading to down-stream activation of caspases and other apoptotic markers, thereby promoting the induction of apoptosis [68][69][70][71].…”

Section: Itcs Source Genus Species (Sub Species) Isothiocyanates (Itc...mentioning

confidence: 99%

Assessment of Methodological Pipelines for the Determination of Isothiocyanates Derived from Natural Sources

et al. 2022

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Isothiocyanates are biologically active secondary metabolites liberated via enzymatic hydrolysis of their sulfur enriched precursors, glucosinolates, upon tissue plant disruption. The importance of this class of compounds lies in their capacity to induce anti-cancer, anti-microbial, anti-inflammatory, neuroprotective, and other bioactive properties. As such, their isolation from natural sources is of utmost importance. In this review article, an extensive examination of the various parameters (hydrolysis, extraction, and quantification) affecting the isolation of isothiocyanates from naturally-derived sources is presented. Overall, the effective isolation/extraction and quantification of isothiocyanate is strongly associated with their chemical and physicochemical properties, such as polarity-solubility as well as thermal and acidic stability. Furthermore, the successful activation of myrosinase appears to be a major factor affecting the conversion of glucosinolates into active isothiocyanates.

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“…High PEITC intake reduced palatability (due to their bitter taste), stimulated the mucosa to produce gastroenteritis, inhibited the synthesis of iodine, caused liver, kidney and thyroid hypertrophy and increased mortality ( Burel et al., 2000 ; Duchamp et al., 1996 ; Mawson et al., 1994 ; Tripathi and Mishra, 2007 ). It has previously been observed that a high dose of PEITC had a cytotoxic by inducing oxidative stress and apoptosis in vitro ( Liu et al., 2019 ; Zhu et al., 2020 ). Further, several studies have demonstrated that PEITC could exert an anti-inflammatory and antioxidant capacity in some cancer cells by inhibiting NF-κB or activating the Nrf2 signaling pathway ( Krajka-Kuźniak et al., 2020 ; Liu, 2017 ; Okubo et al., 2010 ).…”

Section: Introductionmentioning

confidence: 99%

Phenethyl isothiocyanate as an anti-nutritional factor attenuates deoxynivalenol-induced IPEC-J2 cell injury through inhibiting ROS-mediated autophagy

Liu

Hou

et al. 2022

Animal Nutrition

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Deoxynivalenol (DON) is considered to be the most harmful mycotoxin that affects the intestinal health of animals and humans. Phenethyl isothiocyanate (PEITC) in feedstuff is an anti-nutritional factor and impairs nutrient digestion and absorption in the animal intestinal. In the current study, we aimed to explore the effects of PEITC on DON-induced apoptosis, intestinal tight junction disorder, and its potential molecular mechanism in the porcine jejunum epithelial cell line (IPEC-J2). Our results indicated that PEITC treatment markedly alleviated DON-induced cytotoxicity, decreasing the apoptotic cell percentage and pro-apoptotic mRNA/protein levels, and increasing zonula occludens-1 (ZO-1), occludin and claudin-1 mRNA/protein expression. Meanwhile, PEITC treatment ameliorated DON-induced an increase of the inducible nitric oxide synthase ( iNOS ) and cyclooxygenase 2 ( COX-2 ) mRNA levels and intracellular reactive oxygen species (ROS) level, and a decrease of glutathione peroxidase 1 ( GPx1 ), superoxide dismutase 2 ( SOD2 ), catalase ( CAT ) and heme oxygenase 1 ( HO-1 ) mRNA levels. Additionally, PEITC treatment significantly down-regulated autophagy-related protein 5 (ATG5), beclin-1 and microtubule-associated protein 1 light chain 3B (LC3-Ⅱ) mRNA/protein levels, decreased the number of green fluorescent protein-microtubule-associated protein 1 light-chain 3 (GFP-LC3) puncta and phosphatidylinositol 3 kinase (PI3K) protein expression, and up-regulated phospho-protein kinase B (p-Akt) and phospho-mammalian target of rapamycin (p-mTOR) protein expression against DON. However, the activation of autophagy by rapamycin, an autophagy agonist, abolished the protective effects of PEITC against DON-induced cytotoxicity, apoptosis and intestinal tight junction disorder. Collectively, PEITC could confer protection against DON-induced porcine intestinal epithelial cell injury by suppressing ROS-mediated autophagy.

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Phenylethyl isothiocyanate induces oxidative damage of porcine kidney cells mediated by reactive oxygen species

Cited by 6 publications

References 26 publications

Modular Assembly of Ordered Hydrophilic Proteins Improve Salinity Tolerance in Escherichia coli

Modular Assembly of Ordered Hydrophilic Proteins Improve Salinity Tolerance in Escherichia coli

Assessment of Methodological Pipelines for the Determination of Isothiocyanates Derived from Natural Sources

Phenethyl isothiocyanate as an anti-nutritional factor attenuates deoxynivalenol-induced IPEC-J2 cell injury through inhibiting ROS-mediated autophagy

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