title: Lipid peroxidation and lysosomal enzyme release induced by vanadate in vitro.
abstract: Incubation of premitochondrial liver homogenate supernatants of phenobarbital-induced rats with sodium vanadate led to a time- and concentration-dependent formation of malondialdehyde and a parallel release of beta-glucuronidase from lysosomes. Both were inhibited in the presence of glutathione, (+)-catechin or dithiocarb, and took place after a lag phase of 30 min. In contrast, the glutathione content dropped immediately after addition of vanadate. Scavengers of reactive oxygen species had no effect on vanadate-induced lipid peroxidation. In liver homogenates of non-induced rats vanadate-promoted lipid peroxidation was 7.3 times lower than in those of phenobarbital-induced animals, suggesting the involvement of the microsomal mixed-function oxidase system. Thus, vanadate seems to act as a pro-oxidant of the enzymatically-promoted lipid peroxidation.
mesh_terms: D000818:Animals; D005966:Glucuronidase / Q000037:antagonists & inhibitors; D005978:Glutathione / Q000378:metabolism; D066298:In Vitro Techniques; D008054:Lipid Peroxides / Q000378:metabolism*; D008247:Lysosomes / Q000201:enzymology*; D008297:Male; D008315:Malondialdehyde / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D013997:Time Factors; D014638:Vanadates; D014639:Vanadium / Q000494:pharmacology*
chemical_list: D008054:Lipid Peroxides; D014639:Vanadium; D014638:Vanadates; D008315:Malondialdehyde; D005966:Glucuronidase; D005978:Glutathione