Molecular chaperones biochemistry and role in neurodegenerative diseases

Abstract

Many neurodegenerative diseases including Parkinson's disease, Alzheimer's disease, Prion's disease, polyQ and Huntington's disease share abnormal folding of potentially cytotoxic protein species associated with degeneration and death of specific neuronal populations. In order to maintain cellular protein homeostasis, neurons have developed an intrinsic protein quality control system as a strategy to counteract protein aggregation and their toxicity. Heat shock proteins are an essential component for regulating protein quality control and contribute potentially in the process of protein folding, prevent protein aggregation and in disaggregation in several neurodegenerative diseases. Therefore, molecular chaperones are considered an exciting therapeutic target. In this book chapter, we will focus on the potential importance of different heat shock proteins in neurodegenerative diseases and understand their mechanisms to protect neurons form aggregates and their toxicity.

Keywords: Misfolded protein; Molecular chaperones; Neurodegenerative diseases; Protein aggregation; Protein toxicity.