Neuroprotective Effect of Brazilin on Amyloid β (25-35)-Induced Pathology in a Human Neuroblastoma Model

Abstract

Until the recent past, the sole exemplar of proteins as infectious agents leading to neurodegenerative disorders remained the prion protein. Since then, the self-seeding mechanism characteristic of the prion protein has also been attributed to other neurodegenerative-disease-associated proteins, including amyloid-β (Aβ), tau, and α-synuclein (α-Syn). In model cell line studies, truncated Aβ, viz. amyloid beta (25-35), has been found to influence cellular homeostasis through its interactions with, and via, the disruption of key housekeeping machinery. Here, we demonstrate that the incubation of human neuroblastoma (SH-SY5Y) cell line with Brazilin ((6aS,11bR)-7,11b-dihydro-6H-indeno[2,1-c]chromene-3,6a,9,10-tetrol) prior to Aβ (25-35)-insult protected the cells from oxidative stress and apoptotic cell death. Furthermore, Brazilin mitigated Aβ-induced alterations in protein disulfide isomerase (PDI) and α-synuclein status, both of which are important biomarkers that report on Parkinson's pathogenesis. The results obtained in this study suggest that the tetrol is neuroprotective and helps resist Aβ-induced cross-pathology and amyloidogenic onset.