Simple method for visual detection of glutathione S-transferase activity and inhibition using cysteamine-capped gold nanoparticles as colorimetric probes

Ren, Shuhang; Zhou, Fulin; Xu, Chunli; Li, Baoxin

doi:10.1007/s13404-015-0171-3

Cited by 26 publications

(18 citation statements)

References 24 publications

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“…This indicates a possible interaction of CDNB with the GSH coating of QDs, which is prevented in the presence of GST. This further points out that if CDNB‐GSH conjugate (CDNB‐SG) is formed, that does not cause particle precipitation or detrimental drop in the luminescence of the particles (Ren, Zhou, Xu, & Li, ).…”

Section: Resultsmentioning

confidence: 91%

In vitro interaction of glutathione S‐transferase‐pi enzyme with glutathione‐coated silver sulfide quantum dots: A novel method for biodetection of glutathione S‐transferase enzyme

et al. 2019

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Quantum dots (QD) are being evaluated as inorganic nanoparticles for both in vitro and in vivo optical imaging. They are also used as sensors or vehicles for targeted drug delivery combined with optical imaging. In this study, we demonstrated that glutathione‐coated Ag2S QDs (GSH‐Ag2S QDs) act as a substrate analogue of glutathione S‐transferase (GST) enzymes for the first time in the literature. The GSTs belong to a major group of detoxification enzymes involved in the detoxification metabolism responsible for the protection of cells against reactive oxygen species (ROS) or electrophiles. GST isozymes are impaired in the various diseases such as neurological diseases and cancer. We evaluated the interaction of GST‐pi enzyme with GSH‐Ag2S QDs, which have never been studied in the literature before, using both fluorometric and spectrophotometric methods. Our data showed that GSH‐Ag2S QDs gave reaction with GST enzyme as a substrate analogue. In conclusion, our data may help to guide researchers for further development of sensing systems for GST activity which is impaired in various diseases including cancer.

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Section: Resultsmentioning

confidence: 91%

In vitro interaction of glutathione S‐transferase‐pi enzyme with glutathione‐coated silver sulfide quantum dots: A novel method for biodetection of glutathione S‐transferase enzyme

et al. 2019

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“…Phytochemicals of soybean, including saponins and isoflavones, are considered good sources of anticancer activity (Yoon et al 2005). Recent studies revealed GST-pi enzymes are frequently over expressed in neoplastic tissues and have been considered as important markers of a number of tumors, such as lung, ovarian, breast, and gastric carcinoma (Ren et al 2015). Thus, a component that inhibits GSTpi enzyme activity could be considered to possess good anticancer activity.…”

Section: Discussionmentioning

confidence: 99%

Differential anticancer effect of fermented squid jeotgal due to varying concentrations of soymilk additive

Akther

Cheng

Yang

et al. 2017

JABC

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Fermentation plays a vital role in the nutritional enrichment of food. Korea has a long tradition of adding fermented food to the daily diet and jeotgal is one of the common fermented and salted foods in Korean cuisine. In our study, we added soymilk as an additive to squid jeotgal to improve its functionality. We mixed different concentrations of soymilk (2, 5, and 10 mg/g) with squid jeotgal samples, fermented them for one week, and then tested their antioxidant and anticancer activities to compare with those of squid jeotgal samples without soymilk additive. To investigate the anticancer characteristics, glutathione-S-transferase (GST)-pi enzyme assay was used. To test the antioxidant activities, various assays were performed, including 2,2-diphenyl-1-picryl hydrazyl free radical scavenging activity, 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium saltradical cation scavenging assay, and reducing power assay. Samples fermented with a small amount of soymilk showed excellent anticancer activity. The addition of only 2 mg/g of soymilk to squid jeotgal inhibited the activity of GST-pi by almost 50% when compared with the sample with no addition. Moreover, no undesirable bitterness or astringency was noticed. Our results could help to improve the current food status of squid jeotgal and it could be used to reduce the risk of chronic disease along with its basic nutritional function.

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“…Cells were harvested by ultrasonic treatment, and the GSTP enzymatic activity was determined by using glutathione S -transferase (GSH-ST) kit (Nanjing Jiancheng Bioengineering Institute, Nanjing, China). The reactions were terminated, and the enzyme kinetics of the conjugation of 1-chloro-2,4-dinitrobenzene to GSH was determined as previously described ( 43 ).…”

Section: Methodsmentioning

confidence: 99%

Glutathione S-Transferase Pi Prevents Sepsis-Related High Mobility Group Box-1 Protein Translocation and Release

et al. 2018

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Glutathione S-transferase Pi (GSTP) was originally identified as one of cytosolic phase II detoxification enzymes and also was considered to function via its non-catalytic, ligand-binding activity. We have reported that GSTP played an anti-inflammatory role in macrophages, suggesting that GSTP may have a protective role in inflammation. In this study, we deleted the murine Gstp gene cluster and found that GSTP significantly decreased the mortality of experimental sepsis and reduced related serum level of high mobility group box-1 protein (HMGB1). As HMGB1 is the key cytokine involved in septic death, we further studied the effect of GSTP on HMGB1 release. The results demonstrated that a classic protein kinase C (cPKC) dependent phosphorylation of cytoplasmic GSTP at Ser184 occurred in macrophages in response to lipopolysaccharide (LPS) stimulation. Phosphorylated GSTP was then translocated to the nucleus. In the nucleus, GSTP bound to HMGB1 and suppressed LPS-triggered and cPKC-mediated HMGB1 phosphorylation. Consequently, GSTP prevented the translocation of HMGB1 to cytoplasm and release. Our findings provide the new evidence that GSTP inhibited HMGB1 release via binding to HMGB1 in the nucleus independent of its transferase activity. cPKC-mediated GSTP phosphorylation was essential for GSTP to translocate from cytoplasm to nucleus. To our knowledge, we are the first to report that nuclear GSTP functions as a negative regulator to control HMGB1 release from macrophages and decreases the mortality of sepsis.

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Simple method for visual detection of glutathione S-transferase activity and inhibition using cysteamine-capped gold nanoparticles as colorimetric probes

Cited by 26 publications

References 24 publications

In vitro interaction of glutathione S‐transferase‐pi enzyme with glutathione‐coated silver sulfide quantum dots: A novel method for biodetection of glutathione S‐transferase enzyme

In vitro interaction of glutathione S‐transferase‐pi enzyme with glutathione‐coated silver sulfide quantum dots: A novel method for biodetection of glutathione S‐transferase enzyme

Differential anticancer effect of fermented squid jeotgal due to varying concentrations of soymilk additive

Glutathione S-Transferase Pi Prevents Sepsis-Related High Mobility Group Box-1 Protein Translocation and Release

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