Cloning of the mouse gene encoding plasma glutathione peroxidase: organization, sequence and chromosomal localization

Schwaab, Véronique; Baud, Eric; Ghyselinck, Norbert B.; Matteï, Marie‐Geneviève; Dufaure, Jean-Pierre; Drevet, Joël R.

doi:10.1016/0378-1119(95)00551-x

Cited by 30 publications

(16 citation statements)

References 24 publications

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“…With regard to the 19 trapped exons (16%) containing novel sequence but no ORF (Table 2), it is interesting to note that selenoprotein genes contain internal amber stop codons, which code for selenocysteine in the presence of a unique cis-acting mRNA stem-loop structure and the selenocysteine tRNA. The genes for two known human selenoproteins, glutathione peroxidase 3 (GPX3) and plasma selenoprotein P, map to chromosome 5q31-q32 (Yoshimura et al, 1994;Hill et al, 1996), and at least mouse Gpx3 maps to chromosome 11 (Schwaab et al, 1995), so it is possible that another gene encoding a selenoprotein may map within our contig. It is also possible that ribozyme or snRNA exons lacking ORFs could be trapped; a Ro RNA-like hY gene was mapped to human chromosome 5q31 (Frazer et al, 1997).…”

Section: Discussionmentioning

confidence: 96%

Identification of 40 Genes on a 1-Mb Contig around the IL-4 Cytokine Family Gene Cluster on Mouse Chromosome 11

et al. 2000

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Section: Discussionmentioning

confidence: 96%

Identification of 40 Genes on a 1-Mb Contig around the IL-4 Cytokine Family Gene Cluster on Mouse Chromosome 11

et al. 2000

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“…Mouse Gpx3 is encoded by a single copy gene (20). Exon 1 of the mouse Gpx3 gene contains two potential ATG start sites separated by 66 nucleotides, but only the second of them has been proposed to initiate protein translation (20,26). However, even if both start sites are utilized the two translation products would contain the same predicted signal peptide cleavage site and both should yield the same mature ϳ23-kDa protein (2).…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Extracellular glutathione peroxidase (Gpx3) binds specifically to basement membranes of mouse renal cortex tubule cells

Olson¹,

Whitin

Hill

et al. 2010

American Journal of Physiology-Renal Physiology

135

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Glutathione peroxidase-3 (Gpx3), also known as plasma or extracellular glutathione peroxidase, is a selenoprotein secreted primarily by kidney proximal convoluted tubule cells. In this study Gpx3(-/-) mice have been produced and immunocytochemical techniques have been developed to investigate Gpx3 metabolism. Gpx3(-/-) mice maintained the same whole-body content and urinary excretion of selenium as did Gpx3(+/+) mice. They tolerated selenium deficiency without observable ill effects. The simultaneous knockout of Gpx3 and selenoprotein P revealed that these two selenoproteins account for >97% of plasma selenium. Immunocytochemistry experiments demonstrated that Gpx3 binds selectively, both in vivo and in vitro, to basement membranes of renal cortical proximal and distal convoluted tubules. Based on calculations using selenium content, the kidney pool of Gpx3 is over twice as large as the plasma pool. These data indicate that Gpx3 does not serve in the regulation of selenium metabolism. The specific binding of a large pool of Gpx3 to basement membranes in the kidney cortex strongly suggests a need for glutathione peroxidase activity in the cortical peritubular space.

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“…Subsequently, the cDNA from mouse and rat allowed the screening of various tissues, and in these rodents the kidney had the highest content of mRNA. GPX-3 mRNA was also found in heart, lung and other tissues [23,88,89]. In humans, the kidney has the highest levels of GPX mRNA followed by other organs [25].…”

Section: Gpx-3 Functionsmentioning

confidence: 99%

The glutathione peroxidases

Arthur¹

2001

CMLS, Cell. Mol. Life Sci.

774

497

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There are several proteins in mammalian animals. Additionally, cellular glutathione peroxidase knockout mice have been used to investigate the funccells that can metabolize hydrogen peroxide and lipid hydroperoxides. These proteins include four selenium-tions of this protein. From this work it is clear that the selenoperoxidases are involved in cell antioxidant syscontaining glutathione peroxidases that are found in tems. However, they also have more subtle functions different cell fractions and tissues of the body. This in ensuring the regulation and formation of arachareview considers the structure and distribution of the selenoperoxidases and how this relates to their biologi-donic acid metabolites that are derived from hydroperoxide intermediates. The range of biological processes, cal function. The functions of the selenoperoxidases were originally studied in systems where their activity which are potentially dependent on optimal selenoperwas manipulated by changing dietary selenium levels. oxidase activity in mammals, emphasises the imporMore recently, molecular techniques have allowed tance of achieving adequate selenium intake in the overexpression of selenoperoxidases in cell lines and diet.

show abstract

Cloning of the mouse gene encoding plasma glutathione peroxidase: organization, sequence and chromosomal localization

Cited by 30 publications

References 24 publications

Identification of 40 Genes on a 1-Mb Contig around the IL-4 Cytokine Family Gene Cluster on Mouse Chromosome 11

Identification of 40 Genes on a 1-Mb Contig around the IL-4 Cytokine Family Gene Cluster on Mouse Chromosome 11

Extracellular glutathione peroxidase (Gpx3) binds specifically to basement membranes of mouse renal cortex tubule cells

The glutathione peroxidases

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