The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions

Lim, Yongseok; Cha, Mee‐Kyung; Kim, Ha-Kun; Kim, Il-Han

doi:10.1016/0378-1119(94)90558-4

Cited by 64 publications

(28 citation statements)

References 25 publications

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“…They are divided into two major subfamilies: peroxiredoxins (PRXs) and glutathione peroxidases (GPXs). PRXs were initially identified in yeast and mammals as thiol-specific antioxidants protecting glutamine synthetase from oxidation (Kim et al 1989;Chae et al 1993Chae et al , 1994aLim et al 1994; for a historical review see Rhee et al 2005b). Since then, PRXs have been identified in many organisms and constitute a ubiquitous family of thiol-dependent peroxidases catalyzing the reduction of hydrogen peroxide, alkylhydroperoxides, and peroxynitrite to water, the corresponding alcohol, or nitrite, respectively (Nogoceke et al 1997;Bryk et al 2000;Hillas et al…”

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The Peroxiredoxin and Glutathione Peroxidase Families in Chlamydomonas reinhardtii

et al. 2008

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Thiol/selenol peroxidases are ubiquitous nonheme peroxidases. They are divided into two major subfamilies: peroxiredoxins (PRXs) and glutathione peroxidases (GPXs). PRXs are present in diverse subcellular compartments and divided into four types: 2-cys PRX, 1-cys PRX, PRX-Q , and type II PRX (PRXII). In mammals, most GPXs are selenoenzymes containing a highly reactive selenocysteine in their active site while yeast and land plants are devoid of selenoproteins but contain nonselenium GPXs. The presence of a chloroplastic 2-cys PRX, a nonselenium GPX, and two selenium-dependent GPXs has been reported in the unicellular green alga Chlamydomonas reinhardtii. The availability of the Chlamydomonas genome sequence offers the opportunity to complete our knowledge on thiol/selenol peroxidases in this organism. In this article, Chlamydomonas PRX and GPX families are presented and compared to their counterparts in Arabidopsis, human, yeast, and Synechocystis sp. A summary of the current knowledge on each family of peroxidases, especially in photosynthetic organisms, phylogenetic analyses, and investigations of the putative subcellular localization of each protein and its relative expression level, on the basis of EST data, are presented. We show that Chlamydomonas PRX and GPX families share some similarities with other photosynthetic organisms but also with human cells. The data are discussed in view of recent results suggesting that these enzymes are important scavengers of reactive oxygen species (ROS) and reactive nitrogen species (RNS) but also play a role in ROS signaling. L IFE in an oxygen-rich environment has to deal with the danger of oxidative stress. During normal cell metabolism, reactive oxygen species (ROS) and reactive nitrogen species (RNS) are constantly produced, essentially by respiratory and photosynthetic electron transfer chains. These highly reactive molecules can react with many cell components and damage DNA, proteins, and lipids. Thus, their concentration has to be strictly controlled. For this purpose, aerobic organisms are equipped with nonenzymatic (ascorbate, glutathione, tocopherol, and carotenoid) or enzymatic (catalase, ascorbate peroxidase, superoxide dismutase, glutathione peroxidase, and peroxiredoxin) antioxidant systems to remove ROS from the cells. To control their concentrations, ROS and RNS have to be sensed. It has been established in many organisms that ROS, and especially hydrogen peroxide, are signaling molecules that diffuse across membranes and induce specific signal transduction pathways. Furthermore, ROS can also be produced on purpose by cells in response to several stimuli to function as second messengers inside the cell. Finally, ROS and RNS can control enzyme activities by triggering several post-translational modifications such as disulfide bond formation, thiol oxidation to sulfenic/sulfinic/sulfonic acid, glutathionylation, nitrosylation, or carbonylation.Thiol/selenol peroxidases have emerged, during recent years, as important scavengers of ROS/RNS but they ...

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The Peroxiredoxin and Glutathione Peroxidase Families in Chlamydomonas reinhardtii

et al. 2008

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“…Instead of active site of selenocysteine within glutathione peroxidase, they have one conserved cysteine within TPx as a primary site of catalysis. In mammalian tissue, at least, five types of TPx isoenzyme were identified (5). However, based on cellular compartmentalization and tissue distribution, their cellular functions remain still debatable.…”

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Distinct Physiological Functions of Thiol Peroxidase Isoenzymes in Saccharomyces cerevisiae

Park

Kyung

Jeong

et al. 2000

Journal of Biological Chemistry

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219

241

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A new type of peroxidase ("thiol peroxidase"; TPx) having cysteine as the primary site of catalysis has been discovered from prokaryotes to eukaryotes. In addition to two yeast TPx isoforms (TSA I and TSA II/AHPC1) previously described, three additional TPx homologues were identified by analysis of the open reading frame data base for Saccharomyces cerevisiae. Three novel isoforms showed a distinct thiol peroxidase activity supported by thioredoxin, and appeared to be distinctively localized in cytoplasm, mitochondria, and nucleus.

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“…However, its physiological significance as a peroxidase is still debatable because of the existence of conventional catalases and peroxidases in eukaryotic cytoplasm. Yeast and human genes that encode the 25-kDa TSA have been cloned and sequenced (7,8). The deduced amino acid sequences showed no homology to known antioxidant enzymes (8,9).…”

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“…Yeast and human genes that encode the 25-kDa TSA have been cloned and sequenced (7,8). The deduced amino acid sequences showed no homology to known antioxidant enzymes (8,9). An analysis of data bases revealed 27 additional protein sequences showing homology to the 25-kDa TSA.…”

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Thioredoxin-linked "Thiol Peroxidase" from Periplasmic Space of Escherichia coli

Cha

Kim

1995

Journal of Biological Chemistry

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132

124

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Three different molecular masses (24, 22, and 20 kDa) of antioxidant proteins were purified in Escherichia coli. These proteins exhibited the preventive effects against the inactivation of glutamine synthetase activity and the cleavage of DNA by a metal-catalyzed oxidation system capable of generating reactive oxygen species. Their antioxidant activities were supported by a thiol-reducing equivalent such as dithiothreitol. Analysis of the amino-terminal amino acid sequences and the immunoblots between 24-and 22-kDa proteins indicates that the 24-kDa protein is an intact form of the 22-kDa protein that was previously identified 22-kDa subunit (AhpC) of E. coli alkyl hydroperoxide reductase (AhpC/ AhpF). We isolated and sequenced an E. coli genomic DNA fragment that encodes 20-kDa protein. Comparison of the deduced amino acid sequence of the 20-kDa protein with that of AhpC revealed no sequence homology.A search of a data bank showed that the 20-kDa protein is a new type of antioxidant enzyme. The synthesis of this novel 20-kDa protein was increased in response to oxygen stress during growth. The 20-kDa protein resides mainly in the periplasmic space of E. coli, whereas the 24-kDa AhpC resides mainly in the matrix. The 20-kDa protein was functionally linked to the thioredoxin as an in vivo thiol-regenerating system and exerted a peroxidase activity. This 20-kDa protein is thus named "thiol peroxidase," which could act as an antioxidant enzyme removing peroxides or H 2 O 2 within the catalase-and peroxidase-deficient periplasmic space of E. coli.

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The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions

Cited by 64 publications

References 25 publications

The Peroxiredoxin and Glutathione Peroxidase Families in Chlamydomonas reinhardtii

The Peroxiredoxin and Glutathione Peroxidase Families in Chlamydomonas reinhardtii

Distinct Physiological Functions of Thiol Peroxidase Isoenzymes in Saccharomyces cerevisiae

Thioredoxin-linked "Thiol Peroxidase" from Periplasmic Space of Escherichia coli

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