Primary Structure of Human Plasma Glutathione Peroxidase Deduced From cDNA Sequences

Takahashi, Kazuhiko; Yamamoto, Yutaka; Kobayashi, Chigako; Koyama, Jiro; Akasaka, Masami; Mizoguchi, Junzo

doi:10.1080/10426509208045871

Cited by 32 publications

(37 citation statements)

References 14 publications

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“…To date, four enzymes with different tissue distributions have been characterized: the cytosolic GSHPX (cGSHPX) was the first to be isolated and sequenced, but a different GSHPX present in plasma and a third form of GSHPX that specifically reduces hydroperoxide derivatives of intact phospholipids have been characterized (reviewed in reference 66); very recently, another cellular GSHPX different from cGSHPX has also been characterized (12). As we first showed for cGSHPX (8), the SeCys-containing selenoproteins are unique in that the SeCys is encoded by an in-frame UGA codon; this has now been demonstrated for all four GSHPX types (12,61,67) and several other eukaryotic and bacterial SeCys-containing selenoproteins (6,20, 27,75,76). All cells contain low levels of cGSHPX, but high levels are particularly important in tissues in which peroxides are produced at high levels, for example, in erythrocytes as a by-product of the redox reactions involved in oxygen transport or during detoxification processes in liver or kidney.…”

mentioning

confidence: 99%

Transcriptional up-regulation of the mouse cytosolic glutathione peroxidase gene in erythroid cells is due to a tissue-specific 3' enhancer containing functionally important CACC/GT motifs and binding sites for GATA and Ets transcription factors.

O’Prey¹,

Ramsay²,

Chambers³

et al. 1993

Mol. Cell. Biol.

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Nuclear run-on experiments have shown that the high level of expression of the mouse cytosolic glutathione peroxidase mRNA in erythroid cells is due to up-regulation of the gene at the transcriptional level. Studies of the chromatin structure around the cytosolic glutathione peroxidase gene have revealed a series of DNase I hypersensitive sites (DHSS) in the 3' flankingregion ofthe gene in erythroid and other high-expression tissues that are lacking in low-expression cells, in addition to a DHSS over the promoter region in both high-and low-expression tissues. Functional transfection experiments have demonstrated that one of the 3' DHSS regions functions as an enhancer in erythroid cells but not in a low-expression epithelial cell line; and site-directed mutagenesis and footprinting experiments reveal that the activity of the erythroid cell-specific enhancer requires a cluster of binding sites for the CACC/GT box factors and the GATA and Ets families of transcription factors.The glutathione peroxidases (GSHPXs) constitute a family of selenocysteine (SeCys)-containing enzymes whose function is to remove organic peroxides and H202 (see references 9 and 14 for reviews). To date, four enzymes with different tissue distributions have been characterized: the cytosolic GSHPX (cGSHPX) was the first to be isolated and sequenced, but a different GSHPX present in plasma and a third form of GSHPX that specifically reduces hydroperoxide derivatives of intact phospholipids have been characterized (reviewed in reference 66); very recently, another cellular GSHPX different from cGSHPX has also been characterized (12). As we first showed for cGSHPX (8), the SeCys-containing selenoproteins are unique in that the SeCys is encoded by an in-frame UGA codon; this has now been demonstrated for all four GSHPX types (12,61,67) and several other eukaryotic and bacterial SeCys-containing selenoproteins (6,20, 27,75,76). All cells contain low levels of cGSHPX, but high levels are particularly important in tissues in which peroxides are produced at high levels, for example, in erythrocytes as a by-product of the redox reactions involved in oxygen transport or during detoxification processes in liver or kidney. We have shown previously (1,2,8)

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mentioning

confidence: 99%

Transcriptional up-regulation of the mouse cytosolic glutathione peroxidase gene in erythroid cells is due to a tissue-specific 3' enhancer containing functionally important CACC/GT motifs and binding sites for GATA and Ets transcription factors.

O’Prey¹,

Ramsay²,

Chambers³

et al. 1993

Mol. Cell. Biol.

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“…The open reading frame of GPx3 cDNA contains an TGA opal codon (15). To have a successful readthrough of GPx3 by translation complex, a selenium-cysteine must be incorporated into the protein to prevent a translational truncation (16). As a result, the expression of GPx3 is dependent on the availability of selenium, which has been successfully employed as a critical agent for chemoprevention against prostate cancer.…”

Section: Discussionmentioning

confidence: 99%

Glutathione Peroxidase 3, Deleted or Methylated in Prostate Cancer, Suppresses Prostate Cancer Growth and Metastasis

Yu¹,

Yu²,

et al. 2007

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Glutathione peroxidase 3 is a selenium-dependent enzyme playing a critical role in detoxifying reactive oxidative species and maintaining the genetic integrity of mammalian cells. In this report, we found that the expression of glutathione peroxidase 3 (GPx3) was widely inactivated in prostate cancers. Complete inactivation of GPx3 correlates with a poor clinical outcome. Deletions (hemizygous and homozygous) of GPx3 gene are frequent in prostate cancer samples, occurring in 39% of the samples studied. The rate of methylation of the GPx3 exon 1 region in prostate cancer samples reaches 90%. Overexpression of GPx3 in prostate cancer cell lines induced the suppression of colony formation and anchorage-independent growth of PC3, LNCaP, and Du145 cells. PC3 cells overexpressing GPx3 reduced invasiveness in Matrigel transmigration analysis by an average of 2.7-fold. Xenografted PC3 cells expressing GPx3 showed reduction in tumor volume by 4.8-fold, elimination of metastasis (0/16 versus 7/16), and reduction of animal death (3/16 versus 16/16). The tumor suppressor activity of GPx3 seems to relate to its ability to suppress the expression of c-met. The present findings suggest that GPx3 is a novel tumor suppressor gene.

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“…[19], other selenoproteins have been identified using radiolabeled Se [2]. Among these, only 5 have been characterized in mammalian tissues as selenoproteins containing selenocysteine which is encoded by an in-frame UGA codon, formerly known as a stop codon [3,8,15,20,23].…”

Section: Methodsmentioning

confidence: 99%

Expression Pattern of the Mitochondrial Capsule Selenoprotein mRNA in the Mouse Testis after Puberty; in situ Hybridization Study.

Nam

Maeda

Ogawa

et al. 1997

The Journal of Veterinary Medical Science

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ABSTRACT. Mitochondrial capsule selenoprotein (MCS) has been known as a structural protein of the mitochondrial sheath in spermatozoa. In this study, to determine the expression pattern of MCS mRNA in the mouse testis after puberty, in situ hybridization using digoxigeninlabeled RNA probes for MCS was performed in the testes of 8-and 20-week-old ICR mice. In the testes of both ages, MCS mRNA first appeared in step 3 round spermatids, gradually increased during early spermiogenesis, and persisted a high level until step 14 spermatids. After the step 14 spermatids, the signal began to decline and was weakly detected in steps 15-16 spermatids. On the other hand, compared with that in the testes of 8-week-old mice, MCS mRNA level in the testes of 20-week-old mice increased over 2-fold at stages VI-III, while it slightly increased at stages IV-V. These findings suggest that MCS gene transcription may be up-regulated after puberty in the mouse testis. -KEY WORDS: in situ hybridization, mitochondrial capsule selenoprotein, puberty, testis.J. Vet. Med. Sci. 59(11): 983-988, 1997 digoxigenin (DIG)-labeled RNA probes for MCS in the testes of 8-and 20-week-old mice. MATERIALS AND METHODSExperimental animals: Male ICR mice (3 weeks old) were purchased from Charles River, Japan Inc.(Yokohama). All animals were housed in the room where the temperature (22 ± 2°C), relative humidity (55 ± 10%) and light/dark cycles (14L:10D) were controlled. They received food pellets (CLEA Ltd., Tokyo, Japan) and water ad libitum. At 8 and 20 weeks of age, animals were sacrificed under pentobarbital anesthesia. For in situ hybridization studies, the testes were perfused with Bouin's fixative, immersed in the same fixative for 12 to 24 hr and subsequently processed for sectioning.In situ hybridization: RNA probes were synthesized by transcription of a pCRII plasmid (Invitrogen, Tokyo, Japan) containing the MCS cDNA (592 bp) [16] with Sp6 or T7 RNA polymerase after linearization with Hind III or Xho I. Hybridization was performed on the 5 µm sections of testes. Deparaffinized sections were incubated in 10 µg/ml of proteinase K in phosphate buffered saline (PBS) at 37°C for 5 to 30 min and treated with 4% paraformaldehyde in PBS for 10 min, 0.2 M HCl for 10 min, and 0.25% acetic anhydride in 0.1 M triethanolamine (pH 8.0) for 15 min. Sections were prehybridized in 50% formamide (FA) plus 2-strength standard saline citrate (SSC) at 42°C for 30 min and hybridized at 42°C for 16 hr by adding DIG-labeled riboprobes in the following solution: 50% FA, 10 mM TrisHCl (pH 7.6), 200 µg/ml yeast tRNA, 1-strength Denhardt's reagent (the following component diluted with 500 ml of H 2 O: 0

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Primary Structure of Human Plasma Glutathione Peroxidase Deduced From cDNA Sequences

Cited by 32 publications

References 14 publications

Transcriptional up-regulation of the mouse cytosolic glutathione peroxidase gene in erythroid cells is due to a tissue-specific 3' enhancer containing functionally important CACC/GT motifs and binding sites for GATA and Ets transcription factors.

Transcriptional up-regulation of the mouse cytosolic glutathione peroxidase gene in erythroid cells is due to a tissue-specific 3' enhancer containing functionally important CACC/GT motifs and binding sites for GATA and Ets transcription factors.

Glutathione Peroxidase 3, Deleted or Methylated in Prostate Cancer, Suppresses Prostate Cancer Growth and Metastasis

Expression Pattern of the Mitochondrial Capsule Selenoprotein mRNA in the Mouse Testis after Puberty; in situ Hybridization Study.

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