[44] Glutathione peroxidase

Wendel, Albrecht

doi:10.1016/s0076-6879(81)77046-0

Cited by 1,380 publications

(422 citation statements)

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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: 88%

“…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: 88%

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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“…GSH peroxidase from bovine red blood cells was purified to 800U/mg by our standard procedure [16] with minor variances [17]. The activity was determined according to [18].…”

Section: Methodsmentioning

confidence: 99%

Non‐reactivity of the selenoenzyme glutathione peroxidase with enzymatically hydroperoxidized phospholipids

Grossmann

Wendel

1983

European Journal of Biochemistry

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167

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Selenium‐containing glutathione peroxidase (EC 1.11.1.9) was purified 6000‐fold from bovine red blood cells to apparent homogeneity. Lipoxygenase (EC 1.13.11.12) was enriched 20‐fold from soybean acetone powder. Linoleic acid was peroxidized with lipoxygenase and then used as a substrate in the glutathione peroxidase reaction. Analogous experiments were conducted with synthetic 1,2‐dilinoleoyl‐l‐α‐glycerophosphocholine and with natural bovine heart cardiolipin. The peroxidized phospholipids were reactive with glutathione peroxidase only after enzymatic attack by phospholipase A2 (EC 3.1.1.4). This result implies that the membrane‐protective function of glutathione peroxidase includes preceeding phospholipase action and excludes a direct interaction of this enzyme with membrane‐bound lipid hydroperoxides.

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“…Peroxidase activity with cumene hydroperoxide as substrate was determined by a coupled assay with 0.05 mg/ml purified His 6 -mPGES-1, 1 mM GSH, 0.2 mM NADPH, 0.5 mM cumene hydroperoxide (dissolved in alcohol), and an excess amount of glutathione reductase as the linear decrease in NADPH absorption at 340 nm (33).…”

Section: Cloning and Bacterial Expression Of Human Mpges-1-mentioning

confidence: 99%

Human Microsomal Prostaglandin E Synthase-1

Thorén

Weinander

Saha

et al. 2003

Journal of Biological Chemistry

153

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Human, microsomal, and glutathione-dependent prostaglandin (PG) E synthase-1 (mPGES-1) was expressed with a histidine tag in Escherichia coli. mPGES-1 was purified to apparent homogeneity from Triton X-100-solubilized bacterial extracts by a combination of hydroxyapatite and immobilized metal affinity chromatography. The purified enzyme displayed rapid glutathionedependent conversion of PGH 2 to PGE 2 (V max ; 170 mol min ؊1 mg ؊1 ) and high k cat /K m (310 mM ؊1 s ؊1 ). Purified mPGES-1 also catalyzed glutathione-dependent conversion of PGG 2 to 15-hydroperoxy-PGE 2 (V max ; 250 mol min ؊1 mg ؊1 ). The formation of 15-hydroperoxy-PGE 2 represents an alternative pathway for the synthesis of PGE 2 , which requires further investigation. Purified mPGES-1 also catalyzed glutathione-dependent peroxidase activity toward cumene hydroperoxide (0.17 mol min ؊1 mg ؊1 ), 5-hydroperoxyeicosatetraenoic acid (0.043 mol min ؊1 mg ؊1 ), and 15-hydroperoxy-PGE 2 (0.04 mol min ؊1 mg ؊1 ). In addition, purified mPGES-1 catalyzed slow but significant conjugation of 1-chloro-2,4-dinitrobenzene to glutathione (0.8 mol min ؊1 mg ؊1 ). These activities likely represent the evolutionary relationship to microsomal glutathione transferases. Two-dimensional crystals of purified mPGES-1 were prepared, and the projection map determined by electron crystallography demonstrated that microsomal PGES-1 constitutes a trimer in the crystal, i.e. an organization similar to the microsomal glutathione transferase 1. Hydrodynamic studies of the mPGES-1-Triton X-100 complex demonstrated a sedimentation coefficient of 4.1 S, a partial specific volume of 0.891 cm 3 /g, and a Stokes radius of 5.09 nm corresponding to a calculated molecular weight of 215,000. This molecular weight, including bound Triton X-100 (2.8 g/g protein), is fully consistent with a trimeric organization of mPGES-1.Prostaglandin (PG) 1 E 2 is a prostanoid with potent biological functions; among those functions, its role as a mediator of pain and fever in inflammatory reactions is considered of major importance (1-4). The biosynthesis of PGE 2 from arachidonic acid is catalyzed in a sequential action by PGH synthase (PGHS) forming first the endoperoxide PGG 2 and then PGH 2 by reduction. Subsequently, PGE synthase (PGES) (EC 5.3.99.3) converts PGH 2 into PGE 2 (5). Two forms of PGHS exist, PGHS-1 and PGHS-2, with similar enzymatic properties but distinctly different biological functions. PGHS-1 is constitutively expressed in many cells and organs and takes part in housekeeping functions such as the regulation of vascular homeostasis. PGHS-2, in contrast, is strongly induced in response to proinflammatory stimuli and takes part in various pathophysiological events (6, 7). PGES activity, in most cases glutathione (GSH)-dependent, has been detected both in microsomal and cytosolic fractions of various cells, and apparently, more than one form of PGES exist (8 -12). Microsomal, inducible PGES-1 (mPGES-1) is a member of the membrane-associated proteins in eicosanoid and glutathione metabo...

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[44] Glutathione peroxidase

Cited by 1,380 publications

References 9 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

Non‐reactivity of the selenoenzyme glutathione peroxidase with enzymatically hydroperoxidized phospholipids

Human Microsomal Prostaglandin E Synthase-1

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