Increased levels of 4‐hydroxynonenal in human monocytes fed with malarial pigment hemozoin A possible clue for hemozoin toxicity

Schwarzer, Evelin; Müller, Oliver; Arese, Paolo; Siems, Werner; Grune, Tilman

doi:10.1016/0014-5793(96)00523-6

Cited by 72 publications

(73 citation statements)

References 22 publications

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“…To further examine the mechanism of GGT mRNA V-2 induction by HNE, we first determined its expression pattern in response to HNE. The physiological concentration of HNE in the plasma is reported to be less than 1 µM [23,39], but its concentration can reach as high as 10 µM to 5 mM in plasma membrane under conditions of oxidative stress [40,41]. HNE concentrations used in this study were between 5 and 20 µM.…”

Section: Increase Of Ggt Mrna V-2 By Hne In L2 Cellsmentioning

confidence: 86%

γ-Glutamyl transpeptidase is induced by 4-hydroxynonenal via EpRE/Nrf2 signaling in rat epithelial type II cells

Zhang

Liu

Dickinson

et al. 2006

Free Radical Biology and Medicine

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Abstractγ-Glutamyl transpeptidase (GGT) plays key roles in glutathione homeostasis and metabolism of glutathione S-conjugates. Rat GGT is transcribed via five tandemly arranged promoters into seven transcripts. The transcription of mRNAV is controlled by promoter 5. Previously we found that GGT mRNAV-2 was responsible for the induction of GGT in rat alveolar epithelial cells by 4-hydroxynonenal (HNE). In the current study, the underlying mechanism was investigated. Reporter deletion and mutation analysis demonstrated that an electrophile-response element (EpRE) in the proximal region of GGT promoter 5 (GP5) was responsible for the basal-and HNE-induced promoter activity. Gel-shift assays showed an increased binding activity of GP5 EpRE after HNE exposure. The nuclear content of NF-E2-related factor 2 (Nrf2) was significantly increased by HNE. The recruitment of Nrf2 to GP5 EpRE after HNE treatment was demonstrated by supershift and chromatin immunoprecipitation assays. The tissue expression pattern of GGT mRNA V was previously unknown. Using polymerase chain reaction, we found that GGT mRNAV-2 was expressed in many tissues in rat. Taken together, GGT mRNAV-2 is widely expressed in rat tissues and its basal and HNE-induced expression is mediated through EpRE/Nrf2 signaling.

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Section: Increase Of Ggt Mrna V-2 By Hne In L2 Cellsmentioning

confidence: 86%

γ-Glutamyl transpeptidase is induced by 4-hydroxynonenal via EpRE/Nrf2 signaling in rat epithelial type II cells

Zhang

Liu

Dickinson

et al. 2006

Free Radical Biology and Medicine

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“…The physiological concentration of HNE in the plasma is reportedly from 0.3-0.7 μM (164,165) but its concentration can reach as high 10 μM or more in plasma membrane under conditions of oxidative stress (166,167). While HNE is therefore considered as a biomarker of oxidative stress (167,168), it is also implicated in various oxidative stress-related diseases, including atherosclerosis (169), neurodegenerative diseases (170), and fibrosis (171).…”

Section: A Hne: Production Reaction and Eliminationmentioning

confidence: 99%

The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal

Forman

Fukuto

Miller

et al. 2008

Archives of Biochemistry and Biophysics

219

165

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During the past several years, major advances have been made in understanding how reactive oxygen species (ROS) and nitrogen species (RNS) participate in signal transduction. Identification of the specific targets and the chemical reactions involved still remains to be resolved with many of the signaling pathways in which the involvement of reactive species has been determined. Our understanding is that ROS and RNS have second messenger roles. While cysteine residues in the thiolate (ionized) form found in several classes of signaling proteins can be specific targets for reaction with H 2 O 2 and RNS, better understanding of the chemistry, particularly kinetics, suggests that for many signaling events in which ROS and RNS participate, enzymatic catalysis is more likely to be involved than non-enzymatic reaction. Due to increased interest in how oxidation products, particularly lipid peroxidation products, also are involved with signaling, a review of signaling by 4-hydroxy-2-nonenal (HNE) is included. This article focuses on the chemistry of signaling by ROS, RNS, and HNE and will describe reactions with selected target proteins as representatives of the mechanisms rather attempt to comprehensively review the many signaling pathways in which the reactive species are involved. Keywords signaling; glutathione; thioredoxin; oxidants; reactive oxygen species; thiols; peroxide; nitric oxide; peroxynitrite; 4-hydroxynonenal; cysteine; hydrogen peroxide; protein tyrosine phosphatase; reactive nitrogen species; eNOS; iNOS; nNOS; soluble guanylate cyclase; cGMP; tyrosine nitration; fatty acid nitration; NO-heme; NO-metal complexes; nitrite; protein kinase C; ERK; JNK; p38MAPK; tyrosine kinase receptors; calcium OVERVIEW OF SIGNALING BY REACTIVE SPECIESUnderstanding of the roles of reactive oxygen species (ROS), reactive nitrogen species (RNS) and the lipid peroxidation product, 4-hydroxy-2-nonenal (HNE) in signaling has evolved rapidly during the last decade. This has been markedly helped by identification of the specific targets in signaling pathways. In previous reviews, we defined how ROS, H 2 O 2 in particular,

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“…Moreover, they have to overcome the oxidant attack of phagocytes during the critical period between dissemination from, and reinvasion of the host cell (6,7). Within the infected erythrocytes, Plasmodia species appear to enhance oxidative stress, as indicated by the generation of methemoglobin (8) and hydroxyalkenals (9,10). On the other hand, they are known to be sensitive to oxidant killing, as evident from the peroxide nature and pro-oxidant potential of many antimalarial drugs and impaired survival in host cells with disturbed hydroperoxide metabolism (for review see Ref.…”

mentioning

confidence: 99%

The Putative Glutathione Peroxidase Gene ofPlasmodium falciparum Codes for a Thioredoxin Peroxidase

Sztajer

Gamain

Aumann

et al. 2001

Journal of Biological Chemistry

150

112

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A putative glutathione peroxidase gene (Swiss-Prot accession number Z 68200) of Plasmodium falciparum, the causative agent of tropical malaria, was expressed in Escherichia coli and purified to electrophoretic homogeneity. Like phospholipid hydroperoxide glutathione peroxidase of mammals, it proved to be monomeric. It was active with H 2 O 2 and organic hydroperoxides but, unlike phospholipid hydroperoxide glutathione peroxidase, not with phosphatidylcholine hydroperoxide. With glutathione peroxidases it shares the ping-pong mechanism with infinite V max and K m when analyzed with GSH as substrate. As a homologue with selenocysteine replaced by cysteine, its reactions with hydroperoxides and GSH are 3 orders of magnitude slower than those of the selenoperoxidases. Unexpectedly, the plasmodial enzyme proved to react faster with thioredoxins than with GSH and most efficiently with thioredoxin of P. falciparum

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Increased levels of 4‐hydroxynonenal in human monocytes fed with malarial pigment hemozoin A possible clue for hemozoin toxicity

Cited by 72 publications

References 22 publications

γ-Glutamyl transpeptidase is induced by 4-hydroxynonenal via EpRE/Nrf2 signaling in rat epithelial type II cells

γ-Glutamyl transpeptidase is induced by 4-hydroxynonenal via EpRE/Nrf2 signaling in rat epithelial type II cells

The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal

The Putative Glutathione Peroxidase Gene ofPlasmodium falciparum Codes for a Thioredoxin Peroxidase

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