Physiological role of phospholipid hydroperoxide glutathione peroxidase in mammals

2007 ◽  
Vol 388 (10) ◽  
Author(s):  
Marcus Conrad ◽  
Manuela Schneider ◽  
Alexander Seiler ◽  
Georg W. Bornkamm
Keyword(s):  
Glutathione Peroxidase ◽  
Physiological 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

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.

Sign in / Sign up

Export Citation Format

Share Document