A human eDNA sequence for a novel glutathione peroxidase-related protein

Akasaka, Masami; Mizoguchi, Junzo; Takahashi, Kazuhiko

doi:10.1093/nar/18.15.4619

Cited by 34 publications

(9 citation statements)

References 3 publications

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“…In contrast, GPx3 exhibits tissue-specific expression, and has been detected in plasma, milk, and the lungs [31e34]. GPx2 mRNA, isolated from human hepatoma HepG2 cells, was expressed in gastrointestinal tissues but not in other tissues such as the kidneys, heart, lungs, placenta, or uterus [35]. In crustaceans, GPx activity has been detected in the hepatopancreas and gills of the giant freshwater prawn, Macrobrachium rosenbergii [14], and has also been demonstrated to be present in haemocytes of the white shrimp, L. vannamei [16].…”

Section: Discussionmentioning

confidence: 99%

Identification and cloning of the antioxidant enzyme, glutathione peroxidase, of white shrimp, Litopenaeus vannamei, and its expression following Vibrio alginolyticus infection

Liu

Tseng

Cheng

2007

Fish & Shellfish Immunology

140

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Section: Discussionmentioning

confidence: 99%

Identification and cloning of the antioxidant enzyme, glutathione peroxidase, of white shrimp, Litopenaeus vannamei, and its expression following Vibrio alginolyticus infection

Liu

Tseng

Cheng

2007

Fish & Shellfish Immunology

140

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“…is highly expressed in the mucosal epithelium of the gastrointestinal tract [9,10]. Of these forms, GSHPx-1 has been well studied [3].…”

Section: Introductionmentioning

confidence: 99%

Cloning and expression of a single-chain catalytic antibody that acts as a glutathione peroxidase mimic with high catalytic efficiency

et al. 2001

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Glutathione peroxidase (GPX) has a powerful role in scavenging reactive oxygen species. In previous papers we have developed a new strategy for generating abzymes : the monoclonal antibody with a substrate-binding site is first prepared, then a catalytic group is incorporated into the monoclonal antibody's binding site by using chemical mutation [Luo, Zhu, Ding, Gao, Sun, Liu, Yang and Shen (1994) [251][252][253][254][255]. Since then we have established a series of catalytic antibodies capable of catalysing the decomposition of hydroperoxides by GSH. The monoclonal antibody 2F3 was raised against GSH-S-2,4-dinitrophenyl t-butyl ester and exhibited high catalytic efficiency, exceeding that of rabbit liver GPX, after chemical mutation. To produce pharmaceutical proteins and to study the reason why it exhibits high catalytic efficiency, we sequenced, cloned and expressed the variable regions of 2F3 antibody as a single-chain Fv fragment (2F3-

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“…A third GPx in plasma, now called extracellular GPx (eGPx), is reported to reduce both hydrogen peroxide and phospholipid hydroperoxides (7,8). A fourth GPx, originally called GPx-related selenoprotein (9), is now called gastrointestinal GPx (GI-GPx) and has been found to be highly expressed in the gastrointestinal tract mucosal epithelium (10). Furthermore, type I, type II, and type III iodothyronine deiodinase (11)(12)(13) and thioredoxin reductase (14) were identified as selenoproteins.…”

mentioning

confidence: 99%

Selenoprotein P in Human Plasma as an Extracellular Phospholipid Hydroperoxide Glutathione Peroxidase

Saito

Hayashi

Tanaka

et al. 1999

Journal of Biological Chemistry

251

188

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Selenoprotein P is an extracellular protein containing presumably 10 selenocysteines that are encoded by the UGA stop codon in the open reading frame of the mRNA. The function of selenoprotein P is currently unknown, although several indirect lines of evidence suggest that selenoprotein P is a free radical scavenger. We first developed a conventional procedure to isolate selenoprotein P from human plasma. Next, we investigated the reactivities of selenoprotein P against various hydroperoxides in the presence of glutathione. Although selenoprotein P reduces neither hydrogen peroxide nor tertiary butyl hydroperoxide, it does reduce phospholipid hydroperoxide such as 1-palmitoyl-2-(13-hydroperoxy-cis-9,trans-11-octadecadienoyl)-3-phosphatidylcholine hydroperoxide. Kinetic analysis demonstrated a tert-uni ping-pong mechanism, similar to those described for classical glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase. Not only glutathione, but also dithiothreitol, mercaptoethanol, cysteine, and homocysteine, were effective as reducing substances, as in the case of phospholipid hydroperoxide glutathione peroxidase. These results show that selenoprotein P functions as a phospholipid hydroperoxide glutathione peroxidase in extracellular fluids.

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A human eDNA sequence for a novel glutathione peroxidase-related protein

Cited by 34 publications

References 3 publications

Identification and cloning of the antioxidant enzyme, glutathione peroxidase, of white shrimp, Litopenaeus vannamei, and its expression following Vibrio alginolyticus infection

Identification and cloning of the antioxidant enzyme, glutathione peroxidase, of white shrimp, Litopenaeus vannamei, and its expression following Vibrio alginolyticus infection

Cloning and expression of a single-chain catalytic antibody that acts as a glutathione peroxidase mimic with high catalytic efficiency

Selenoprotein P in Human Plasma as an Extracellular Phospholipid Hydroperoxide Glutathione Peroxidase

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