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1.
Sci Data ; 10(1): 800, 2023 11 14.
Article in English | MEDLINE | ID: mdl-37963885

ABSTRACT

Satellite vegetation index (VI) products, such as normalized difference vegetation index (NDVI) and enhanced vegetation index (EVI), have been widely used. However, they are severely contaminated by clouds and other factors and provide false signals of the surface vegetation conditions. In this study, the new global seamless 250 m, eight-day NDVI and EVI products from 2000-2021 were developed from Moderate Resolution Imaging Spectroradiometer (MODIS) surface reflectance data using a long short-term memory (LSTM) neural network method. High-quality globally representative time series VI samples were constructed to train the model using a combination of the Savitzky-Golay filter (SG), Global LAnd Surface Satellite (GLASS) leaf area index (LAI) fitting and upper envelope methods. To evaluate the proposed method and the 250 m VI products, the MODIS VI product (MOD13Q1) was used for the inter-comparisons using four widely used VI reconstruction methods. Assuming that the MODIS VI data of high quality represents the true values, the root mean square error (RMSE) for NDVI and EVI generated by the LSTM model are 0.0734 and 0.0509, respectively.

2.
Aging (Albany NY) ; 14(1): 443-461, 2022 01 12.
Article in English | MEDLINE | ID: mdl-35020600

ABSTRACT

Human glutathione peroxidase1 (hGPx1) is a good antioxidant and potential drug, but the limited availability and poor stability of hGPx1 have affected its development and application. To solve this problem, we prepared a hGPx1 mutant (GPx1M) with high activity in an Escherichia coli BL21(DE3)cys auxotrophic strain using a single protein production (SPP) system. In this study, the GPx1M was conjugated with methoxypolyethylene glycol-succinimidyl succinate (SS-mPEG, Mw = 5 kDa) chains to enhance its stability. SS-mPEG-GPx1M and GPx1M exhibited similar enzymatic activity and stability toward pH and temperature change, and in a few cases, SS-mPEG-GPx1M was discovered to widen the range of pH stability and increase the temperature stability. Lys 38 was confirmed as PEGylated site by liquid-mass spectrometry. H9c2 cardiomyoblast cells and Sprague-Dawley (SD) rats were used to evaluate the effects of GPx1M and SS-mPEG-GPx1M on preventing or alleviating adriamycin (ADR)-mediated cardiotoxicity, respectively. The results indicated that GPx1M and SS-mPEG-GPx1M had good antioxidant effects in vitro and in vivo, and the effect of SS-mPEG-GPx1M is more prominent than GPx1M in vivo. Thus, PEGylation might be a promising method for the application of GPx1M as an important antioxidant and potential drug.


Subject(s)
Antioxidants/pharmacology , Glutathione Peroxidase/metabolism , Animals , Antioxidants/chemistry , Antioxidants/metabolism , Cell Line , Drug Design , Escherichia coli , Glutathione Peroxidase/chemistry , Humans , Hydrogen-Ion Concentration , Models, Molecular , Mutation , Myocytes, Cardiac , Polyethylene Glycols/chemistry , Protein Conformation , Protein Stability , Rats , Rats, Sprague-Dawley , Succinimides/chemistry , Temperature , Glutathione Peroxidase GPX1
3.
Int J Pharm ; 609: 121152, 2021 Nov 20.
Article in English | MEDLINE | ID: mdl-34626796

ABSTRACT

Human glutathione peroxidase (GPx), as an important kind of antioxidant enzyme, is often used for the removal of reactive oxygen species. Unfortunately, the application has been hindered by its limited source and poor stability. To solve these problems, human glutathione peroxidase mutant (GPxM) with high activity and yield was obtained using Escherichia coli BL21(DE3) cys auxotrophic strain and the single-protein production system in our previous work. However, the antioxidant effect of this novel recombinant protein drug in animals has not been demonstrated, and its immunogenicity and short biological half-life as a biological macromolecule may have seriously hindered its clinical application. Therefore, it is important to find an effective strategy to address the above issues. In this work, PEGylated GPxM was prepared by conjugating the corresponding mutant with monomethoxy polyethylene glycol succinimidyl succinate (SS-mPEG). We researched the structure, stability, pharmacokinetic properties, antioxidant effect in vivo and protective mechanism against adriamycin (ADR)-mediated cardiotoxicity of modified products, and compared with the above properties of GPxM. The results revealed that GPxM had an excellent antioxidant effect in vivo, and PEGylation can enhance the stability, half-life and antioxidant effect of GPxM while reducing immunogenicity. In addition, the above improvement of PEGylated GPx1M was stronger than that of monoPEGylated GPx4M. Hence, PEGylation might be an effective method to broaden the applications of GPxM as the important antioxidant drug, especially the PEGylated GPx1M with high antioxidant effect.


Subject(s)
Antioxidants , Polyethylene Glycols , Animals , Glutathione Peroxidase/genetics , Half-Life , Humans , Recombinant Proteins/genetics , Succinic Acid
4.
Oxid Med Cell Longev ; 2021: 6632813, 2021.
Article in English | MEDLINE | ID: mdl-34539971

ABSTRACT

Ischemic heart disease (IHD) is a cardiovascular disease with high fatality rate, and its pathogenesis is closely related to oxidative stress. Reactive oxygen species (ROS) in oxidative stress can lead to myocardial ischemia (MI) injury in many ways. Therefore, the application of antioxidants may be an effective way to prevent IHD. In recent years, glutathione peroxidase 4 (GPx4) has received increasing attention due to its antioxidant effect. In a previous study, we used the new chimeric tRNAUTuT6 to express highly active recombinant human GPx4 (rhGPx4) in amber-less Escherichia coli. In this study, we established an isoproterenol- (ISO-) induced MI injury model in rats and an in vitro model to research the protective effect and mechanism of rhGPx4 on MI injury. The results showed that rhGPx4 could reduce the area of myocardial infarction and ameliorate the pathological injury of heart tissue, significantly reduce ISO-induced abnormalities on electrocardiogram (ECG) and cardiac serum biomarkers, protect mitochondrial function, and attenuate cardiac oxidative stress injury. In an in vitro model, the results also confirmed that rhGPx4 could inhibit ISO-induced oxidative stress injury and cardiomyocyte apoptosis. The mechanism of action of rhGPx4 involves not only the inhibition of lipid peroxidation by eliminating ROS but also keeping a normal level of endogenous antioxidant enzymes by eliminating ROS, thereby preventing oxidative stress injury in cardiomyocytes. Additionally, rhGPx4 could inhibit cardiomyocyte apoptosis through a mitochondria-dependent pathway. In short, rhGPx4, a recombinant antioxidant enzyme, can play an important role in the prevention of IHD and may have great potential for application.


Subject(s)
Myocardial Infarction/drug therapy , Phospholipid Hydroperoxide Glutathione Peroxidase/therapeutic use , Protective Agents/therapeutic use , Animals , Apoptosis/drug effects , Biomarkers/blood , Cell Line , Disease Models, Animal , Electrocardiography , Humans , Isoproterenol/toxicity , Male , Membrane Potential, Mitochondrial/drug effects , Myocardial Infarction/chemically induced , Myocardial Infarction/metabolism , Myocytes, Cardiac/cytology , Myocytes, Cardiac/drug effects , Myocytes, Cardiac/metabolism , Oxidative Stress/drug effects , Phospholipid Hydroperoxide Glutathione Peroxidase/genetics , Phospholipid Hydroperoxide Glutathione Peroxidase/metabolism , Phospholipid Hydroperoxide Glutathione Peroxidase/pharmacology , Protective Agents/pharmacology , Rats , Rats, Sprague-Dawley , Reactive Oxygen Species/metabolism , Recombinant Proteins/biosynthesis , Recombinant Proteins/pharmacology , Recombinant Proteins/therapeutic use , Troponin T/blood
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