A number of acute and chronic neurodegenerative conditions are associated by protein misfolding and aggregation of proteins within and outside cells. Misfolded proteins and protein aggregation are controlled by molecular chaperones such as heat shock proteins (HSPs) that are constitutively and inducibly expressed in the nervous system. There is increasing evidence that HSPs could counteract common pathological mechanisms that take place during Alzheimer's disease (AD), Parkinson's disease (PD) and Huntington's disease (HD). Protein misfolding and its progressive accumulation in central nervous system are the common features and the leading cause of several neurodegenerative diseases. Currently no treatment is available to complete removal of these aggregates and rescue neuronal death, synaptic impairment as well as cognitive deficits. Interesting, the cell itself has a fantastic defense mechanism to remove these aggregates. One such crucial mechanism is molecular chaperones such as heat shock proteins. In general, the larger protein aggregates are removed by this system, and degraded through the proteasome or autophagy pathway.

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