Biological role of hepoxilins: Upregulation of phospholipid hydroperoxide glutathione peroxidase as a cellular response to oxidative stress?

2007 ◽  
Vol 77 (3-4) ◽  
pp. 209-215 ◽  
Author(s):  
M.P. Zafiriou ◽  
R. Deva ◽  
R. Ciccoli ◽  
A. Siafaka-Kapadai ◽  
S. Nigam
Keyword(s):  
Oxidative Stress ◽  
Glutathione Peroxidase ◽  
Cellular Response ◽  
Biological Role ◽  
Phospholipid Hydroperoxide Glutathione Peroxidase ◽  
Phospholipid Hydroperoxide

scholarly journals Distribution and Possible Novel Role of Phospholipid Hydroperoxide Glutathione Peroxidase in Rat Epididymal Spermatozoa1

1997 ◽  
Vol 57 (6) ◽  
pp. 1502-1508 ◽  
Author(s):  
Cristiana Godeas ◽  
Federica Tramer ◽  
Fulvio Micali ◽  
Mariarosa Soranzo ◽  
Gabriella Sandri ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Phospholipid Hydroperoxide Glutathione Peroxidase ◽  
Phospholipid Hydroperoxide

scholarly journals The Role of Phospholipid Hydroperoxide Glutathione Peroxidase Isoforms in Murine Embryogenesis

2006 ◽  
Vol 281 (28) ◽  
pp. 19655-19664 ◽  
Author(s):  
Astrid Borchert ◽  
Chi Chiu Wang ◽  
Christoph Ufer ◽  
Heike Schiebel ◽  
Nicolai E. Savaskan ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Phospholipid Hydroperoxide Glutathione Peroxidase ◽  
Phospholipid Hydroperoxide ◽  
Peroxidase Isoforms

Two novel phospholipid hydroperoxide glutathione peroxidase genes of Paragonimus westermani induced by oxidative stress

Parasitology ◽  
2009 ◽  
Vol 136 (5) ◽  
pp. 553-565 ◽  
Author(s):  
S.-H. KIM ◽  
G.-B. CAI ◽  
Y.-A. BAE ◽  
E.-G. LEE ◽  
Y.-S. LEE ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Glutathione Peroxidase ◽  
Single Copy ◽  
Structure Characteristic ◽  
Sequence Motif ◽  
Lipid Hydroperoxides ◽  
Phospholipid Hydroperoxide Glutathione Peroxidase ◽  
Interaction Domain ◽  
Paragonimus Westermani ◽  
Phospholipid Hydroperoxide

SUMMARYPhospholipid hydroperoxide glutathione peroxidase (PHGPx; GPx4) plays unique roles in the protection of cells against oxidative stress by catalysing reduction of lipid hydroperoxides. We characterized 2 novel GPx genes from a lung fluke, Paragonimus westermani (designated PwGPx1 and PwGPx2). These single copy genes spanned 6559 and 12 371 bp, respectively, and contained each of 5 intervening introns. The PwGPx2 harboured a codon for Sec and a Sec insertion sequence motif. Proteins encoded by the Paragonimus genes demonstrated a primary structure characteristic to the PHGPx family, including preservation of catalytic and glutathione-binding domains and absence of the subunit interaction domain. Expression of PwGPx1 increased gradually as the parasite matured, whereas that of PwGPx2 was temporally regulated. PwGPx2 was expressed at the basal level from the metacercariae to the 3-week-old juveniles; however, the expression was significantly induced in the 7-week-old immature worms and reached a plateau in the 12-week-old adults and eggs. PwGPx1 and PwGPx2 were largely localized in vitellocytes within vitelline glands and eggs. Oxidative stress-inducible paraquat, juglone and H2O2 substantially augmented the PwGPx1 and PwGPx2 expressions in viable worms by 1·5- to 11-fold. Our results strongly suggested that PwGPxs may actively participate in detoxification of oxidative hazards in P. westermani.

scholarly journals Role of the 3′ untranslated region in the regulation of cytosolic glutathione peroxidase and phospholipid-hydroperoxide glutathione peroxidase gene expression by selenium supply

1996 ◽  
Vol 320 (3) ◽  
pp. 891-895 ◽  
Author(s):  
Giovanna BERMANO ◽  
John R. ARTHUR ◽  
John E. HESKETH
Keyword(s):  
Gene Expression ◽  
Glutathione Peroxidase ◽  
Selenium Deficiency ◽  
Type I ◽  
Mrna Levels ◽  
Phospholipid Hydroperoxide Glutathione Peroxidase ◽  
Iodothyronine Deiodinase ◽  
Phospholipid Hydroperoxide ◽  
Cytosolic Glutathione

Selenium is an essential nutrient and synthesis of selenoproteins is affected by limited selenium supply. During selenium deficiency there is a differential regulation of selenoprotein synthesis and gene expression; for example, there is a decrease in abundance of mRNA for cytosolic glutathione peroxidase (cGSH-Px) and a preservation of mRNA for phospholipid-hydroperoxide glutathione peroxidase (PHGSH-Px). This difference is not due to an alteration in the rate of transcription but might reflect differences in translation. The aim of the present work was to assess the role of cGSH-Px and PHGSH-Px 3´ untranslated regions (UTRs) in the regulation of selenoprotein mRNA stability and translation by using H4-II-E-C3 cells transfected with different constructs containing a type I iodothyronine deiodinase-coding region linked to different selenoprotein mRNA 3´ UTRs. Translational efficiency results showed that the efficiency of the 3´ UTRs in permitting selenocysteine incorporation is similar in selenium-replete conditions but, when selenium is limiting, the 3´ UTR of cGSH-Px is less efficient than the 3´ UTR of PHGSH-Px. The results suggest that the 3´ UTR of these selenoprotein mRNA species influences their extent of translation when selenium levels are low. The different sensitivity of the 3´ UTRs to selenium deficiency can explain the differential effect that selenium deficiency has on cGSH-Px and PHGSH-Px activity and mRNA levels, stability and translation. This might be partly responsible for channelling selenium for synthesis of PHGSH-Px rather than cGSH-Px.

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