Role of glutathione peroxidase 1 in glucose and lipid metabolism-related diseases

Huang, Jia‐Qiang; Zhou, Jinchuan; Wu, Yuanyuan; Ren, Fazheng; Lei, Xin Gen

doi:10.1016/j.freeradbiomed.2018.05.077

Cited by 84 publications

(55 citation statements)

References 127 publications

(186 reference statements)

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“…Given the sensitive H 2 O 2 ‐sensing performance of HRP‐A@ZIF‐8, we also established a new platform for sensing of biothiols. Glutathione (GSH) is a biothiol that has a variety of physiological functions related to diabetes, liver diseases, cataracts and Alzheimer's and Parkinson's disease . GSH is facile to be oxidized by H 2 O 2 , and thus can inhibit the catalytic efficiency of HRP‐A@ZIF‐8.…”

Section: Resultsmentioning

confidence: 99%

Modulating the Biofunctionality of Metal–Organic‐Framework‐Encapsulated Enzymes through Controllable Embedding Patterns

et al. 2020

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Embedding an enzyme within a MOF as exoskeleton (enzyme@MOF) offers new opportunities to improve the inherent fragile nature of the enzyme, but also to impart novel biofunctionality to the MOF. Despite the remarkable stability achieved for MOF‐embedded enzymes, embedding patterns and conversion of the enzymatic biofunctionality after entrapment by a MOF have only received limited attention. Herein, we reveal how embedding patterns affect the bioactivity of an enzyme encapsulated in ZIF‐8. The enzyme@MOF can maintain high activity when the encapsulation process is driven by rapid enzyme‐triggered nucleation of ZIF‐8. When the encapsulation is driven by slow coprecipitation and the enzymes are not involved in the nucleation of ZIF‐8, enzyme@MOF tends to be inactive owing to unfolding and competing coordination caused by the ligand, 2‐methyl imidazole. These two embedding patterns can easily be controlled by chemical modification of the amino acids of the enzymes, modulating their biofunctionality.

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Section: Resultsmentioning

confidence: 99%

Modulating the Biofunctionality of Metal–Organic‐Framework‐Encapsulated Enzymes through Controllable Embedding Patterns

et al. 2020

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“…Selenoproteins other than SELENOP, such as glutathione peroxidase 1 (GPX1) and selenoprotein S, are known to play a major role in regulation of glucose metabolism 33 , 34 . For example, overexpression of GPX1 was reported to exhibit insulin resistance and obesity in mice 35 .…”

Section: Discussionmentioning

confidence: 99%

Serum selenoprotein P, but not selenium, predicts future hyperglycemia in a general Japanese population

Makino

Saito

et al. 2018

Sci Rep

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We aimed to test the hypothesis that selenoprotein P (SELENOP), a hepatokine involved in the development of both insulin resistance and impaired insulin production in mice, is related to future onset of hyperglycemia in humans. 76 healthy non-pregnant human subjects without diabetes underwent oral glucose tolerance test (OGTT) at baseline and 4-years follow-up. Nine subjects developed either impaired glucose tolerance or type 2 diabetes at follow-up. At baseline, SELENOP concentrations correlated negatively with insulinogenic index, but not with homeostasis model assessment-estimated insulin resistance (HOMA-IR). Multivariate analysis showed that baseline SELENOP predicted fasting plasma glucose at follow-up independently of the other parameters. The receiver operating characteristic (ROC) curve analysis showed that baseline concentrations of serum SELENOP, but not of selenium, were a reliable test to predict future onset of glucose intolerance. In conclusion, elevation of circulating SELENOP, but not of circulating selenium, was positively and independently associated with future onset of glucose intolerance in a general Japanese population.

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“…[49] Given the sensitive H 2 O 2 -sensing performance of HRP-A@ZIF-8, we also established an ew platform for sensing of biothiols.Glutathione (GSH) is abiothiol that has avariety of physiological functions related to diabetes,l iver diseases, cataracts and Alzheimersand Parkinsonsdisease. [50][51][52] GSH is facile to be oxidized by H 2 O 2 ,a nd thus can inhibit the catalytic efficiencyofHRP-A@ZIF-8. Such acatalytic inhibition effect could be utilized for visual GSH sensing (Figure 6A).…”

Section: Boosting the Performance For Biosensing And Catalytic Cascadesmentioning

confidence: 99%

Modulating the Biofunctionality of Metal–Organic‐Framework‐Encapsulated Enzymes through Controllable Embedding Patterns

et al. 2020

View full text Add to dashboard Cite

Embedding an enzyme within aMOF as exoskeleton (enzyme@MOF) offers new opportunities to improve the inherent fragile nature of the enzyme,but also to impart novel biofunctionality to the MOF.D espite the remarkable stability achieved for MOF-embedded enzymes,e mbedding patterns and conversion of the enzymatic biofunctionality after entrapment by aM OF have only received limited attention. Herein, we reveal howe mbedding patterns affect the bioactivity of an enzyme encapsulated in ZIF-8. The enzyme@MOF can maintain high activity when the encapsulation process is driven by rapid enzyme-triggered nucleation of ZIF-8. When the encapsulation is driven by slow coprecipitation and the enzymes are not involved in the nucleation of ZIF-8, enzy-me@MOF tends to be inactive owing to unfolding and competing coordination caused by the ligand, 2-methyl imidazole.T hese two embedding patterns can easily be controlled by chemical modification of the amino acids of the enzymes,modulating their biofunctionality.Supportinginformation and the ORCID identification number(s) for the author(s) of this article can be found under: https://doi.

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Role of glutathione peroxidase 1 in glucose and lipid metabolism-related diseases

Cited by 84 publications

References 127 publications

Modulating the Biofunctionality of Metal–Organic‐Framework‐Encapsulated Enzymes through Controllable Embedding Patterns

Modulating the Biofunctionality of Metal–Organic‐Framework‐Encapsulated Enzymes through Controllable Embedding Patterns

Serum selenoprotein P, but not selenium, predicts future hyperglycemia in a general Japanese population

Modulating the Biofunctionality of Metal–Organic‐Framework‐Encapsulated Enzymes through Controllable Embedding Patterns

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