Identification and characterization of two selenium-dependent glutathione peroxidase 1 isoforms from Larimichthys crocea

Xie, Xinfang; Chen, Mengnan; Zhu, Aiyi

doi:10.1016/j.fsi.2017.09.067

Cited by 21 publications

(21 citation statements)

References 76 publications

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“…Enzymes such as myeloperoxidase (MPO), lactoperoxidase (LPO) and thyroid peroxidase (TPO) belong to this group of peroxidases. The prosthetic heme group of these peroxidases is covalently linked with the apo-protein and they have been extracted from sources such as the southern bluefin tuna ( Thunnus maccoyi ), the grass carp ( Ctenopharyngodon idellus ) and Antarctic fish ( Trematomus bernacchi ) [8] , [21] , [25] . Their application is often hampered by low temperature stability, sensitivity to salt and organic solvents [10] , [13] .…”

Section: Sources Of Peroxidase Enzymesmentioning

confidence: 99%

“…Glutathione peroxidases (GPxs) (EC 1.11.1.9) are vital antioxidant enzymes which use glutathione or thioredoxins as an electron donor to catalyze the reduction of hydroperoxides to alcohols along with the oxidation of thiols to disulfides [25] , [44] .…”

Section: Peroxidase Isoformsmentioning

confidence: 99%

“…Selenenic acid group is then converted back into the selenol by a two-step process, first one being the reaction of GSH (reduced monomeric glutathione) to form GS-SeR and water (reaction 2), secondly the reduction of GS-SeR (reaction 3) intermediate to senenol by a second GSH molecule which then results in the release of GS-SG (glutathione disulfide) as a by-product. Finally, the glutathione peroxidase thereafter reduces the oxidized glutathione to complete the cycle (reaction 5) [25] .…”

Section: Peroxidase Isoformsmentioning

confidence: 99%

Section: Peroxidase Isoformsmentioning

confidence: 99%

“…Glutathione peroxidases are widely distributed in oxybiotic organisms where they maintain intra-organic oxidative status balance by catalyzing the reduction of various hydroperoxides and H 2 O 2 into corresponding alcohols and water [25] . In the mammal family, there are eight GPx isoforms (GPx1–GPx8) which are divided based on their cellular location, structure and specific substrate [25] , [44] . GPx1, GPx4, and GPx6 are selenoproteins which contain the unique amino acid selenocysteine (Sec) while the remaining three (GPx5, GPx7 & GPx8) have cysteine instead of Sec hence they are non-selenoproteins [25] .…”

Section: Peroxidase Isoformsmentioning

confidence: 99%

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Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin

et al. 2020

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Peroxidases are classified as oxidoreductases and are the second largest class of enzymes applied in biotechnological processes. These enzymes are used to catalyze various oxidative reactions using hydrogen peroxide and other substrates as electron donors. They are isolated from various sources such as plants, animals and microbes. Peroxidase enzymes have versatile applications in bioenergy, bioremediation, dye decolorization, humic acid degradation, paper and pulp, and textile industries. Besides, peroxidases from different sources have unique abilities to degrade a broad range of environmental pollutants such as petroleum hydrocarbons, dioxins, industrial dye effluents, herbicides and pesticides. Ironically, unlike most biological catalysts, the function of peroxidases varies according to their source. For instance, manganese peroxidase (MnP) of fungal origin is widely used for depolymerization and demethylation of lignin and bleaching of pulp. While, horseradish peroxidase of plant origin is used for removal of phenols and aromatic amines from waste waters. Microbial enzymes are believed to be more stable than enzymes of plant or animal origin. Thus, making microbially-derived peroxidases a well-sought-after biocatalysts for versatile industrial and environmental applications. Therefore, the current review article highlights on the recent breakthroughs in the discovery and use of peroxidase isoforms of microbial origin at a possible depth.

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Section: Sources Of Peroxidase Enzymesmentioning

confidence: 99%

Section: Peroxidase Isoformsmentioning

confidence: 99%

Section: Peroxidase Isoformsmentioning

confidence: 99%

Section: Peroxidase Isoformsmentioning

confidence: 99%

Section: Peroxidase Isoformsmentioning

confidence: 99%

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Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin

et al. 2020

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Immunotoxicity of Perfluorooctanoic Acid to the Marine Bivalve Species Ruditapes philippinarum

Liu

et al. 2022

Enviro Toxic and Chemistry

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Polyfluorinated alkylated substances are recognized as an important class of pollutants in marine environments. Bivalves are good model organisms for evaluating the toxicity of pollutants and monitoring marine environments. In the present study, immunotoxicity of perfluorooctanoic acid (PFOA) was investigated by measuring biomarkers of the immune profile of Ruditapes philippinarum. In bivalves, hemocytes are an important component of the immune system. Thus, hemocyte proliferation, phagocytosis, cell viability, and immune enzyme activities, which have been applied as marine pollution bioindicators, were identified and observed for changes after exposure to PFOA in R. philippinarum. Based on the integrated biomarker responses method, we selected five biomarkers to evaluate PFOA risk at the multibiomarker level. In addition, the histopathological alterations of hemocytes in bivalves were used as indexes of the response to environmental stress. The subcellular structure of the hemocytes in R. philippinarum changed significantly with PFOA exposure, including hemocyte and nucleus morphological changes, organelle dissolution, cytomembrane and karyotheca swelling, and cytoplasm vacuolization. The present study verifies PFOA immunotoxicity to R. philippinarum at different levels and the integrated assessment of stress levels caused by PFOA in marine environment. Our results will provide new insights into evaluating adverse effects of PFOA and monitoring marine ecosystem. Environ Toxicol Chem 2022;41:426–436. © 2021 SETAC

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Cloning and mRNA expression of selenium-dependent glutathione peroxidase from the oyster Magallana hongkongensis in response to cadmium exposure and aerial exposure at different temperatures

et al. 2023

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Identification and characterization of two selenium-dependent glutathione peroxidase 1 isoforms from Larimichthys crocea

Cited by 21 publications

References 76 publications

Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin

Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin

Immunotoxicity of Perfluorooctanoic Acid to the Marine Bivalve Species Ruditapes philippinarum

Cloning and mRNA expression of selenium-dependent glutathione peroxidase from the oyster Magallana hongkongensis in response to cadmium exposure and aerial exposure at different temperatures

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