cDNA sequence coding for human glutathione peroxidase

Sukenaga, Yoshikazu; Ishida, Koichi; Takeda, Teruyo; Takagi, Kenkichi

doi:10.1093/nar/15.17.7178

Cited by 99 publications

(34 citation statements)

References 2 publications

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“…Sequence analysis of the full-length cDNA revealed the presence of a single open reading frame encoding a 224 amino acid protein which revealed striking similarity to a bovine non-selenium glutathione peroxidase (Shichi and Demar, 1990). This enzyme is distinct from the selenoenzymes and from the pi-class glutathione S-transferase which also exhibits peroxidase activity (Mullenbach et al, 1987;Sukenaga et al, 1987;Esworthy et al, 1994;Kano et al, 1987;Wendel, 1981;Flohe, 1982). The striking sequence homology of the non-selenium glutathione peroxidase and the product of KRG-1, the identical size of both proteins, and the sequence similarities of the KRG-1 product with other glutathione peroxidases or with glutathione S-transferase highly suggest that we had cloned the human homologue of this gene.…”

Section: Discussionmentioning

confidence: 90%

“…The sequence of the human protein is shown on the top. The sequence of the bovine protein is shown below the human selenium glutathione peroxidase (Mullenbach et al, 1987;Sukenaga et al, 1987), the human phospholipid hydroperoxide glutathione peroxidase (Esworthy et al, 1994) and the human class pi glutathione S-transferase (Kano et al, 1987) which also exhibits peroxidase activity (Wendel, 1981) did not reveal obvious similarities. However, after a more detailed comparison of these sequences we identi®ed several sequence motifs in our protein which revealed similarities to at least one of the other enzymes (Table 1).…”

Section: High Stringencymentioning

confidence: 99%

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The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene

1997

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Keratinocyte growth factor is a potent and speci®c mitogen for dierent types of epithelial cells, including keratinocytes of the skin. Furthermore, it has been implicated in morphogenetic processes of several organs. To further de®ne the mechanisms of KGF action in the skin, we attempted to identify genes which are regulated by KGF in keratinocytes. Using the dierential display RT ± PCR technology, a gene was identi®ed which was strongly induced in these cells by treatment with KGF but not with serum growth factors or pro-in¯ammatory cytokines. Molecular cloning of the full-length cDNA revealed a strong homology of the corresponding gene product with a bovine non-selenium glutathione peroxidase. Upon transfection of COS cells with the fulllength cDNA, a 27 kD cytoplasmic protein was obtained which had the expected size of glutathione peroxidase. Expression of the novel gene was detected in normal human skin and at particularly high levels in psoriatic skin, indicating a possible in vivo function of the protein in this tissue. Identi®cation of a peroxidase as a KGFregulated gene suggests that prevention from oxygen toxicity is a novel and speci®c mechanism of KGF action.

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Section: Discussionmentioning

confidence: 90%

Section: High Stringencymentioning

confidence: 99%

The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene

1997

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“…They represent a large and, with respect to tissue distribution and intracellular localization, heterogeneous group of functionally similar enzymes [9]. Nevertheless, our novel protein displayed only low sequence identity with the various known members of this family, such as the tetrameric cytosolic selenoenzyme [10,11], the membrane-bound selenoenzyme phospholipid hydroperoxide GPx [12], the glycosylated extracellular enzyme [13], and the Alpha and Theta subclasses of glutathione S-transferases, which also exhibit GPx acitvity [14]. However, it was strikingly similar to a novel GPx from bovine ciliary body, of which only a 29-amino-acid N-terminal peptide had been sequenced [15].…”

Section: Introductionmentioning

confidence: 89%

A novel type of glutathione peroxidase: expression and regulation during wound repair

Munz

Frank

Hübner

et al. 1997

Biochemical Journal

116

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We have previously identified and cloned a novel keratinocyte growth factor (KGF)-regulated gene in human keratinocytes that encodes the human homologue of a bovine non-selenium glutathione peroxidase (GPx). To gain insight into the regulation of this gene in vivo, we isolated the murine homologue from a mouse skin cDNA library. In vitro transcription/translation demonstrated that the cDNA encodes a 27 kDa protein. Furthermore, we amplified by PCR a partial cDNA that most likely corresponds to a related gene. RNase protection analysis revealed tissue-specific expression of both genes and the occurrence of alternative splicing or RNA editing of at least one of the primary transcripts. Similar to that of KGF, expression of GPx was strongly induced after cutaneous injury, and each isoform displayed unique kinetics of expression during the repair process. In situ hybridization studies demonstrated high levels of GPx mRNA in keratinocytes of the hyperproliferative epithelium at the wound edge. Since these cells express functional KGF receptors, induction of GPx expression by KGF might also occur in vivo. These data suggest a role for GPx in the protection of epithelial cells against oxidative stress, particularly during the inflammatory phase of wound repair.

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“…Selenium presents as selenocysteine (Sty) in some seleno-proteins, such as cellular glutathione peroxidase (GPx) [2], plasma glutathione peroxidase 133, S'-iodothyronine monodeiodinase (S'DI) [4], plasma seleno-protein (SeP) [S], and phospholipid hydroperoxide glutathione peroxidase (PHGPx) [6]. We previously reported the sequences of human cellular GPx cDNA and genomic DNA [7,8]. The Sty codon on mRNAs of these proteins is UGA which also functions as a stop codon.…”

Section: Introductionmentioning

confidence: 99%

“…However, it is possible that a key structure for recognition of the Sty UGA codon presents in the frame of mRNAs of mammalian selenoproteins and is located near the Sty UGA codon. In [20], Human GPx genes used were the cDNA and gcnomic DNA previously reported [7,8]. Genomic DNA and cDNA of GPx were subcloned in pcD [21] or pSV [22] which contain the SV40 ori and early promoter.…”

Section: Introductionmentioning

confidence: 99%

The 5′ untranslated region of the human cellular glutathione peroxidase gene is indispensable for its expression in COS‐7 cells

et al. 1992

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WC studied the expression of the human cellular glutathionc peroxidase (GPx) gene, from which a key enzyme containing sclenocysteine (Sty) at the active site is produced. Expression of some human GPx gene mutants in COS-7 cells revealed that the 5' untranslated region (utr) was necessary for expression of the GPx gene, since mutant genes having 10 base pairs (bps) at the S'utr (the complete had 311 bps) expressed GPx at very low levels. The genes with 31 I or 405 bps at the S'utr wcrc better expressed than those having 257 bps. The GPx gene having 133 bps at the 3'utr (80 bps shorter than the entire length) was highly expressed. This deletion did not influence expression. We constructed some mutants in which 3 bases were altered at the upstream region of the Sty UGA codon i. *. the frame ,of the GPx Ben.+ by site-directed mutagenesis. GPx expression decreased but the expression was restored. Therefore, the upstream region of the in-frame Sty codon was nL?t essential in the Sty decoding mechanisms. Finally, the S'utr was essential for the expression of GPx gene. However, the deletion of a part of the 3'utr and the siw-directed mutation upstream of the Sty codon did not show drastic effects on the expression.

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cDNA sequence coding for human glutathione peroxidase

Cited by 99 publications

References 2 publications

The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene

The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene

A novel type of glutathione peroxidase: expression and regulation during wound repair

The 5′ untranslated region of the human cellular glutathione peroxidase gene is indispensable for its expression in COS‐7 cells

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