Effect of pridoindole stobadine on liver tissue protein oxidation of STZ-Diabetic rats

The oxidatve protein damage provoked by reactve ree radicals has been demonstrated o play a signicant role n several pathological events such as diabetes. Proteins can also be damaged by oxygen and nirogen radicals, eading o a oss of enzymatc actviy and the conversion of amno acids to carbonyl derivatves and t has already been shown hat ree radicals cause oxidaton of protein - H groups. Considerable evidence ndicates hat he maintenance of protein redox status s of fundamental mportance or cell functon, herefore structural changes n proteins are considered o be among he molecular mechanisms eading o diabetc complcatons, in he present study, we determned he efect of pridoindole stobadine supplementaton (STB; 24.7 mg/kg/day) on he markers of oxidatve protein damage n he ver ssue of TZ- diabetc rats and heir control and reated groups. Dabetes was nduced by ntraperitonal njecton of streptozotosin (55 mg/kg) and rats were randomy divided nto our groups as olows: control (K; n = 7), controlSTB (KTB; n=7), Dabet (DiA; n=7) and DabetSTB (DTB; n=7). 3- Nrotyrosine evels were measured by ELiSA. Thiols and AOPP evels of ver homogenates were studied by spectrophotometric methodand Protein carbonyl levels were determned by colorimetric assay kit. Total, protein and non-protein hiol levels were signicanty decreased n diabetc rats. On he other hand protein carbonyl content and advanced oxidaton protein product levels were signicanty ncreased n diabetc group compared w h hose of he controls (p<0,05). Stobadine reatment ed o signicanty ncrease hiol parameters and decreased protein carbonyl content and advanced oxidaton protein product (AOPP) evels n diabetSTB group (p<0.05). 3-nirotyrosine evels weren't dierent in all groups. Tssue protein oxidaton parameters n he our groups of Wstar-Abino rats were compared using he Mann-Whiney U-test. When not specied p<0.05 was considered signicant. The resuls of his study suggest hat stobadine decreased oxidatve stres and may be efectve n preventng oxidatve protein damage, which may contribute to the development of diabetc complcatons.