Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPx) in Rat Testis Nuclei Is Bound to Chromatin

Godeas, Cristiana; Tramer, Federica; Micali, Fulvio; Roveri, Antonella; Maiorino, Matilde; Nisii, Carla; Sandri, Gabriella; Panfili, Enrico

doi:10.1006/bmme.1996.0076

Cited by 82 publications

(42 citation statements)

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“…Plasma GPx (GPx3) and phospholipid GPx (GPx4), mainly expressed in kidney and testis, respectively [34,35], were significantly induced in the present study. GPx3 is proposed to be a major scavenger of ROS in the extracellular space and within the vasculature [36].…”

Section: Discussionsupporting

confidence: 53%

Acute effects of microcystins exposure on the transcription of antioxidant enzyme genes in three organs (liver, kidney, and testis) of male Wistar rats

Xiong¹,

Xie²,

Li³

et al. 2010

J Biochem & Molecular Tox

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Microcystins (MCs) induce the production of reactive oxygen species (ROS) in various tissues in mammals, whereas the endogenous antioxidant enzymes are responsible to scavenge the ROS. ROS can modulate the antioxidant enzyme activities by regulating the mRNA levels. The present study was undertaken to find out the relationship between the transcriptional alterations of antioxidant enzymes and MCs stimulation in rats. The timedependent changes of relative transcription abundance of catalase (CAT), Mn-superoxide dismutase (Mn-SOD), Cu,Zn-superoxide dismutase (Cu,Zn-SOD), glutathione reductase (GR), glutathione peroxidase (GPx), and gamma-glutamylcysteine synthetase (γ-GCS) were investigated in three organs (liver, kidney, and testis) of male Wistar rats injected intravenously (i.v.) with 80 μg MC-LR equivalent /kg body weight using the quantitative real-time PCR (qPCR) method. We found that MCs could affect the transcriptional activities of these antioxidant enzymes in liver, kidney, and testis of MCstreated rats and we speculated the possible causation of the transcriptional change. The altered transcription of antioxidant enzymes may play an important role in counteracting the potential deleterious effects of elevated oxidative stress induced by MCs, and this will provide us new insights into the possible role of antioxidant enzymes in the toxicological mechanisms of MCs at molecular level. C

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Section: Discussionsupporting

confidence: 53%

Acute effects of microcystins exposure on the transcription of antioxidant enzyme genes in three organs (liver, kidney, and testis) of male Wistar rats

Xiong¹,

Xie²,

Li³

et al. 2010

J Biochem & Molecular Tox

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“…The kinetic pattern of PfTPx is identical to that of the selenium-containing glutathione peroxidases (28 -31 low efficiency of PfTPx in GSH-dependent hydroperoxide reduction and the sequence similarities to the less GSH-specific pGPx (32) and PHGPx (33,34), its activity with alternative reducing substrates, notably thioredoxins, was investigated. Table II shows that PfTPx indeed accepts thioredoxins of various species.…”

Section: Heterologous Expression and Purification Of Pftpx-e Colimentioning

confidence: 99%

The Putative Glutathione Peroxidase Gene ofPlasmodium falciparum Codes for a Thioredoxin Peroxidase

Sztajer

Gamain

Aumann

et al. 2001

Journal of Biological Chemistry

150

112

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A putative glutathione peroxidase gene (Swiss-Prot accession number Z 68200) of Plasmodium falciparum, the causative agent of tropical malaria, was expressed in Escherichia coli and purified to electrophoretic homogeneity. Like phospholipid hydroperoxide glutathione peroxidase of mammals, it proved to be monomeric. It was active with H 2 O 2 and organic hydroperoxides but, unlike phospholipid hydroperoxide glutathione peroxidase, not with phosphatidylcholine hydroperoxide. With glutathione peroxidases it shares the ping-pong mechanism with infinite V max and K m when analyzed with GSH as substrate. As a homologue with selenocysteine replaced by cysteine, its reactions with hydroperoxides and GSH are 3 orders of magnitude slower than those of the selenoperoxidases. Unexpectedly, the plasmodial enzyme proved to react faster with thioredoxins than with GSH and most efficiently with thioredoxin of P. falciparum

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“…This enzyme is expressed in most tissues but is particularly abundant in testis, where it is targeted to the mitochondrial and nuclear membranes (18,19). Outside the realm of oxidized lipids, the apparent association of a significant fraction of PHGPx with chromatin (20) is of particular interest in light of recent data that suggests that oxidized DNA may be a substrate for PHGPx enzymatic activity (21).…”

mentioning

confidence: 99%

Purification, Redox Sensitivity, and RNA Binding Properties of SECIS-binding Protein 2, a Protein Involved in Selenoprotein Biosynthesis

Copeland

Driscoll

1999

Journal of Biological Chemistry

135

118

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In mammalian selenoprotein mRNAs, the highly structured 3 UTR contains selenocysteine insertion sequence (SECIS) elements that are required for the recognition of UGA as the selenocysteine codon. Our previous work demonstrated a tight correlation between codon-specific translational read-through and the activity of a 120-kDa RNA-binding protein that interacted specifically with the SECIS element in the phospholipid hydroperoxide glutathione peroxidase mRNA. This study reports the RNA binding and biochemical properties of this protein, SECIS-binding protein 2 (SBP2). We detected SBP2 binding activity in liver, hepatoma cell, and testis extracts from which SBP2 has been purified by anion exchange and RNA affinity chromatography. This scheme has allowed us to identify a 120-kDa polypeptide that co-elutes with SBP2 binding activity from wild-type but not mutant RNA affinity columns. A characterization of SBP2 biochemical properties reveals that SBP2 binding is sensitive to oxidation and the presence of heparin, rRNA, and poly(G). SBP2 activity elutes with a molecular mass of ϳ500 kDa during gel filtration chromatography, suggesting the existence of a large functional complex. Direct cross-linking and competition experiments demonstrate that the minimal phospholipid hydroperoxide glutathione peroxidase 3 UTR binding site is between 82 and 102 nucleotides, which correlates with the minimal sequence necessary for translational read-through. SBP2 also interacts specifically with the minimally functional 3 UTR of another selenoprotein mRNA, deiodinase 1.

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Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPx) in Rat Testis Nuclei Is Bound to Chromatin

Cited by 82 publications

References 0 publications

Acute effects of microcystins exposure on the transcription of antioxidant enzyme genes in three organs (liver, kidney, and testis) of male Wistar rats

Acute effects of microcystins exposure on the transcription of antioxidant enzyme genes in three organs (liver, kidney, and testis) of male Wistar rats

The Putative Glutathione Peroxidase Gene ofPlasmodium falciparum Codes for a Thioredoxin Peroxidase

Purification, Redox Sensitivity, and RNA Binding Properties of SECIS-binding Protein 2, a Protein Involved in Selenoprotein Biosynthesis

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