The Effect Of Rutin And Anti-XD5on IAPP And β-amyloid Protein

Amyloid disease, also called conformational diseases, their common characteristics are that they are accompanied by some abnormal accumulation of endogenous protein during the course of these diseases. By continuously permeating surrounding tissue, these deposits can induce toxicity and inflammatory reactions of cells, which are strongly linked to damage and pathological changes of the related organization. The abnormal aggregation of the amyloid deposits such as the islet amyloid polypeptide, Ap\a-synuclein and Lysozyme significantly affect pathogenesis of T2DM, Alzheimer’s Disease, Parkinson’s Disease and Lysozyme accumulations respectively. Immunotherapy and Polyphenols therapy are promising strategy for amyloidoses treatment. Thus, in this study, we investigated the effect of flavonoid antioxidant rutin on amylin aggregation, cytotoxicity, oxidative stress, as well as the generation of nitric oxide (NO) and pro-inflammatory cytokines, and the function of Anti-XD5on several amyloids such as A(342, Lysozyme, a-synuclein.Our results indicated that rutin inhibited amylin cytotoxicity, decreased the production of reactive oxygen species, NO, glutathione disulfide (GSSG), malondialdehyde, and pro-inflammatory cytokines TNF-a and IL-1β,attenuated mitochondrial damage, and increased the glutathione/GSSG ratio. These protective effects of rutin may have resulted from its ability to inhibit IAPP aggregation, enhance the antioxidant enzyme activity of superoxide dismutase, catalase, and glutathione peroxidase, and reduce inducible nitric oxide synthase activity. Moreover, we previously obtained the oligomer-specific epitope (XD5), and developed the antibody Anti-XD5. Through further empirical study, we found that Anti-XD5inhibited the aggregation of these three amyloids and specifically recognized the assembled oligomers.These results indicate that flavonoid antioxidant rutin may be a promising therapeutic agent for T2DM treatment. And as a polyclonal antibody of the antigen epitope peptide, our results laid a good foundation for the further reseatch of Anti-XD5.