Metabolism of oxidized linoleic acid by glutathione transferases: Peroxidase activity toward 13-hydroperoxyoctadecadienoic acid
Biochimica et Biophysica Acta (BBA) -- General Subjects
The oxidation of linoleic acid produces several products with biological activity including the hydroperoxy fatty acid 13-hydroperoxyoctadecadienoic acid (13-HPODE), the hydroxy fatty acid 13-hydroxyoctadecadienoic acid (13-HODE), and the 2,4-dienone 13-oxooctadecadienoic acid (13-OXO). In the present work, the peroxidase activity of glutathione transferases (GST) A1-1, M1-1, M2-2, and P1-1(Val 105) toward 13-HPODE has been examined. The alpha class enzyme is the most efficient peroxidase while the two enzymes from the mu class exhibit weak peroxidase activity toward 13-HPODE. It was also determined that the conjugated diene 13-HODE is not a substrate for GST from the alpha and mu classes but that 13-HODE does inhibit the GST-catalyzed conjugation of CDNB by enzymes from the alpha, mu, and pi classes. Finally, both 13-HODE and 13-OXO were shown to be inducers of GST activity in HT-29 and HCT-116 colon tumor cells. These data help to clarify the role of GST in the metabolic disposition of linoleic acid oxidation products.
Seeley, Stacy K.; Poposki, Julie A.; Maksimchuk, John; Tebbe, Jill; Gaudreau, Jon; Mannervik, Bengt; and Bull, Arthur W., "Metabolism of oxidized linoleic acid by glutathione transferases: Peroxidase activity toward 13-hydroperoxyoctadecadienoic acid" (2006). Chemistry & Biochemistry Publications. 92.