Primary Structure of Human Plasma Glutathione Peroxidase Deduced from eDNA Sequences1

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

doi:10.1093/oxfordjournals.jbchem.a123172

Cited by 139 publications

(17 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…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: 91%

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

Munz

Frank

Hübner

et al. 1997

Biochemical Journal

116

View full text Add to dashboard Cite

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.

show abstract

Section: Introductionmentioning

confidence: 91%

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

Munz

Frank

Hübner

et al. 1997

Biochemical Journal

116

View full text Add to dashboard Cite

show abstract

“…The primary structure of human pGSHPx shows only limited identity with the other two enzymes, 44% with human cGSHPx and 25% with pig PHGPx (Takahashi et al, 1990;Schuckelt et al, 1991). However, higher conservations in these three glutathione peroxidases are observed among the amino acids constituting the active site (Epp et al, 1983).…”

Section: Introductionmentioning

confidence: 95%

“…Their primary structures are poorly related. It has been shown that they are encoded by different genes and that they have different enzymatic properties (Takahashi et al, 1990;Schuckelt et al, 1991;Yamamoto & Takahashi, 1993;Esworthy, Chu, Geiger, Girotti & Doroshow, 1993). cGSHPx and PHGPx occur as cytosolic or membrane-bound forms, cGSHPx can reduce hydrogen peroxide, organic hydroperoxides as well as lipid hydroperoxides, while PHGPx in particular reduces phospholipid and cholesterol hydroperoxides in biological membranes (Thomas, Maiorino, Ursini & Girotti, 1990).…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary X-ray diffraction analysis of glutathione peroxidase from human plasma

Ren

Huang²,

Åkesson³

et al. 1995

Acta Cryst D

View full text Add to dashboard Cite

The extracellular form of glutathione peroxidase from human plasma has been crystallized by the sitting-drop vapourdiffusion method. The crystals belong to tetragonal space group /41o with cell dimensions of a----b = 83.1 and c = 131.0 A. They diffract beyond 2.9 ,A resolution and have one dimer in the asymmetric unit. A self-rotation function analysis shows the possible (222) symmetry for the tetramers of this enzyme.

show abstract

“…The first indication that selenocysteine is inserted cotranslationally was provided by the finding that the genes for two selenoproteins-namely, fdhF coding for a formate dehydrogenase from Escherichia coli (5) and gpx coding for a glutathione peroxidase from mouse (6)-contain an in-frame TGA (UGA) codon. Since then, a number of genes coding for other selenoproteins also have been found to possess an in-frame TGA (UGA) codon (7)(8)(9)(10)(11)(12)(13)(14)(15). With the exception of the gene for plasma selenoprotein P, which contains 10 TGA (UGA) codons, all these genes contain only 1 such codon.…”

Section: Introductionmentioning

confidence: 99%

Interaction of translation factor SELB with the formate dehydrogenase H selenopolypeptide mRNA.

Baron¹,

Heider²,

Böck³

1993

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The SELB protein from Escherichia coli is a specialized elongation factor required for the UGA-directed insertion of the amino acid selenocysteine into selenopolypeptides. Discrimination of the UGA codon requires the presence of a recognition element within the mRNA, which is located at the 3' side of the UGA codon; a hairpin structure can be formed within this mRNA region. By gel shift assays, a specific interaction between SELB and the mRNA recognition element could be demonstrated. Footprinting experiments, using nucleases or iodine as cleaving agents, showed that SELB binds to the loop region of the hairpin structure. In the presence of selenocysteinyl-tRNA, SELB formed a complex with the charged tRNA and the mRNA. The results indicate that targeted insertion of selenocysteine is accomplished by the binding of the SELB protein to this mRNA recognition element, resulting in the formation of a selenocysteinyl-tRNA-SELB complex at the mRNA in the immediate neighborhood of the UGA codon.A number of unusual coding events, which contradict the hitherto paradigmatic scheme ofprotein synthesis, have been discovered during the last few years (for review, see refs. 1 and 2). Besides ribosome hopping and frameshifting, a particularly intriguing finding was that the genetic capacity of a cell can be expanded in such a way that a nonstandard amino acid, selenocysteine, is incorporated into polypeptides. This amino acid is present in several proteins from organisms belonging to all three lines of descent, archaea, bacteria, and eukarya (for review, see refs. 3 and 4). The first indication that selenocysteine is inserted cotranslationally was provided by the finding that the genes for two selenoproteins-namely, fdhF coding for a formate dehydrogenase from Escherichia coli (5) and gpx coding for a glutathione peroxidase from mouse (6)-contain an in-frame TGA (UGA) codon. Since then, a number of genes coding for other selenoproteins also have been found to possess an in-frame TGA (UGA) codon (7-15). With the exception of the gene for plasma selenoprotein P, which contains 10 TGA (UGA) codons, all these genes contain only 1 such codon.A biologically basic question bearing considerable relevance for the understanding of the translation and the evolution of the genetic code is how the translational machinery can cope with the situation that one and the same triplet can signal either chain termination or selenocysteine insertion. The best-examined systems up to now are those of the E. coli formate dehydrogenase H (fdhF) and N (fdnG) genes (5, 10).Their analysis has revealed that a sequence of 40 bases in the mRNA at the 3' side of the UGA codon, which can be folded into a putative hairpin structure, is required for selenocysteine insertion (16, 17). Mutagenesis of this hairpin structure showed that the sequence of the loop region is particularly important and that it may serve as a recognition element for some putative factor directing the selenocysteine-inserting tRNA species (tRNASec) to decode that particular UGA (18)...

show abstract

Primary Structure of Human Plasma Glutathione Peroxidase Deduced from eDNA Sequences1

Cited by 139 publications

References 0 publications

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

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

Crystallization and preliminary X-ray diffraction analysis of glutathione peroxidase from human plasma

Interaction of translation factor SELB with the formate dehydrogenase H selenopolypeptide mRNA.

Contact Info

Product

Resources

About