The role of ribosylated-BSA in regulating PC12 cell viability

摘要: Glycation, one of the post-translational modifications, is known to influence protein structure and biological function. Advanced glycation end products (AGEs) have been shown cause pathologies diabetes. Glycation levels in patients with Alzheimer’s disease (AD) are higher than normal people. However, whether susceptible proteins a triggering event for cell damage or simply result remains be elucidated. In this study, we demonstrated that ribose-conjugated BSA (Rib-BSA) directly induces PC12 death dose- time-dependent manner. The IC50 4.6 μM. Unlike glucose-incubated BSA, Rib-BSA rapidly forms cytotoxic AGEs. vulnerable Rib-BSA. fructose can induce AGE formation, although no effect on survival was observed. This reversed by pretreatment pioglitazone rosiglitazone, which belongs thiazolidinediones (TZDs) peroxisome proliferator-activated receptor (PPAR-γ) ligands. Moreover, upregulates inducible nitric oxide synthase (iNOS), cycloxygenase 2 (COX-2) expression, p-38 phosphorylation leaves extracellular regulated protein1/2 (ERK1/2) unchanged. Rib-BSA-induced signaling changes blocked rosiglitazone confirmed PPAR-γ small-interfering RNA transfection. reduction iNOS inhibitor p38 inhibitor. No observed using COX-2 Consequently, these results show inducing TZDs protect from damage. Signaling molecules, such as PPAR-γ, P38, iNOS, involved Rib-BSA-mediated cytotoxicity.