The Effect of Soybean Trypsin Inhibitor on the Generation of Oxygen Free Radical in Pancreas of Mice during Different Growth Periods

Gu, Chao; Zhao, Linlin; Han, Lingling; Song, Xinxiu; Qu, Hongsheng

doi:10.3136/fstr.20.431

Cited by 2 publications

(2 citation statements)

References 27 publications

(20 reference statements)

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“…The following candidate serum proteins were first selected based on their abundance in serum to illuminate them with our CTZ indicators: (i) human, bovine, and egg albumins (HAS, BSA, and OVA) were selected for the investigation, because they are the most abundant proteins in serum (35,000-52,000 mg/L) [15]; (ii) HIgG and BIgG were also selected, because they show the second-highest abundance among serum proteins (7000-16,000 mg/L); (iii) HTF was also chosen for the measurement, because it occupies the third abundant position among serum proteins (2000-3600 mg/mL); (iv) HγG and BγG were chosen, because γ-globulin grouping IgA, IgM, and IgY is the fourth abundant among serum proteins (i.e., 700-4000 mg/mL for IgA); (v) HFG was also selected, because it is the sixth abundant protein in serum; and (vi) STI and HFN were chosen for the measurement, because they are key components for the retardation of growth, digestive, and metabolic diseases [16] and human infective diseases [17], although they are the 19th and 26th abundant serum proteins, respectively.…”

Section: Reagents and Materialsmentioning

confidence: 99%

Coelenterazine Indicators for the Specific Imaging of Human and Bovine Serum Albumins

Kim

Kamiya

Furuta

et al. 2023

Sensors

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Albumin assays in serum are important for the prognostic assessment of many life-threatening diseases, such as heart failure, liver disease, malnutrition, inflammatory bowel disease, infections, and kidney disease. In this study, synthetic coelenterazine (CTZ) indicators are developed to quantitatively illuminate human and bovine serum albumins (HSA and BSA) with high specificity. Their functional groups were chemically modified to specifically emit luminescence with HSA and BSA. The CTZ indicators were characterized by assaying the most abundant serum proteins and found that the CTZ indicators S6 and S6h were highly specific to HSA and BSA, respectively. Their colors were dramatically converted from blue, peaked at 480 nm, to yellowish green, peaked at 535 nm, according to the HSA–BSA mixing ratios, wherein the origins and mixing levels of the albumins can be easily determined by their colors and peak positions. The kinetic properties of HSA and BSA were investigated in detail, confirming that the serum albumins catalyze the CTZ indicators, which act as pseudo-luciferases. The catalytic reactions were efficiently inhibited by specific inhibitors, blocking the drug-binding sites I and II of HSA and BSA. Finally, the utility of the CTZ indicators was demonstrated through a quantitative imaging of the real fetal bovine serum (FBS). This study is the first example to show that the CTZ indicators specify HSA and BSA with different colors. This study contributes to the expansion of the toolbox of optical indicators, which efficiently assays serum proteins in physiological samples. Considering that these CTZ indicators immediately report quantitative optical signals with high specificity, they provide solutions to conventional technical hurdles on point-of-care assays of serum albumins.

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Section: Reagents and Materialsmentioning

confidence: 99%

Coelenterazine Indicators for the Specific Imaging of Human and Bovine Serum Albumins

Kim

Kamiya

Furuta

et al. 2023

Sensors

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“…It is not only a major source of ROS, but also the main target of ROS injury. The early studies indicated that STI could do harm to pancreas by increasing the formation of lipid peroxidation [11], but the mechanism remains unclear. So this paper aims to explore the effect of STI on the generation of free radicals in pancreatic mitochondria.…”

Section: Introductionmentioning

confidence: 99%

The Effects of Soybean Trypsin Inhibitor on Free Radicals Levels in Pancreatic Mitochondria of Mice

Gu¹,

Li²,

Zhao³

et al. 2014

JFNR

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This paper aims to explore the effect of soybean trypsin inhibitor(STI) on oxygen free radicals levels in pancreatic mitochondria of mice. 36 male KM mice were randomly divided into three groups and fed with different diets as follows: control group was fed on control diet, STI group was fed on control diet containing STI, and VC (vitamin C) group was fed on STI diet supplemented with vitamin C. Mice were sacrificed by decapitation after being fed for 3 weeks. Pancreas was quickly removed and mitochondria were prepared for determining the oxidative and antioxidative index. The results showed that, compared with mice fed with control diet, malondialdehyde (MDA) content and activity of nitric oxide synthase (NOS) in pancreatic mitochondria of mice fed with STI diet were significantly increased (P < 0.05), the content of glutathione (GSH), total antioxidant capacity (T-AOC), the activities of glutathione peroxidase (GSH-Px), catalase(CAT) and superoxide dismutase (SOD) were significantly dropped. After STI diet was supplemented with antioxidant, the contents of oxidation parameters were significantly decreased (P < 0.05), but their values were still higher than those of control group; the activities of antioxidant parameters in pancreatic mitochondria were significantly increased (P < 0.05), but still lower than those of control group. These results supported that STI could cause oxidative stress in pancreatic mitochondria. In addition, vitamin C could interfere with the role of STI on the organism and effectively improve the status of oxidative stress.

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The Effect of Soybean Trypsin Inhibitor on the Generation of Oxygen Free Radical in Pancreas of Mice during Different Growth Periods

Cited by 2 publications

References 27 publications

Coelenterazine Indicators for the Specific Imaging of Human and Bovine Serum Albumins

Coelenterazine Indicators for the Specific Imaging of Human and Bovine Serum Albumins

The Effects of Soybean Trypsin Inhibitor on Free Radicals Levels in Pancreatic Mitochondria of Mice

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