Abstract
Glutathione peroxidases are considered essential for the prevention of lipid peroxidation in biomembranes (1). Whereas the “classical” tetrameric Glutathione peroxidases (GPX) only reduce hydroperoxy fatty acids previously cleaved from phospholipids by phospholipases, a monomeric variant called phospholipid hydroperoxide glutathione peroxidase (PHGPX) was reported to directly attack the peroxo groups within biomembranes (2). Thereby, the enzyme would not only be superior to GPX in biomembrane protection, but could also, in concert with e.g. 15-lipoxygenase, modulate cellular functions by specifically inserting hydroxy groups into biomembranes. It is the aim of the present study to clarify the chemical identity of PHGPX.
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Brigelius-Flohé, R., Schuckelt, R., StraβBurgher, W., Ursini, F., Wolf, B., Flohé, I.L. (1993). Phospholipid Hydroperoxide Glutathione Peroxidase: A Selenoprotein Distinct from Glutathione Peroxidase. In: Nigam, S., Honn, K.V., Marnett, L.J., Walden, T.L. (eds) Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation and Radiation Injury. Developments in Oncology, vol 71. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3520-1_18
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DOI: https://doi.org/10.1007/978-1-4615-3520-1_18
Publisher Name: Springer, Boston, MA
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