Involvement of molecular chaperone in protein-misfolding brain diseases
Nitu L. Wankhede, Mayur B. Kale, Aman B. Upaganlawar, Brijesh G. Taksande, Milind Umekar, Tapan Behl, Ahmed A. H. Abdellatif, Prasanna Mohana Bhaskaran, Sudharshan Reddy Dachani, Aayush Sehgal, Sukhbir Singh, Neelam Sharma, Hafiz A. Makeen, Mohammed Albratty, Hamed Ghaleb Dailah, Saurabh Bhatia, Ahmed Al‐Harrasi, Simona Bungău
Abstract
Protein misfolding causes aggregation and build-up in a variety of brain diseases. There are numeral molecules that are linked with the protein homeostasis mechanism. Molecular chaperones are one of such molecules that are responsible for protection against protein misfolded and aggregation-induced neurotoxicity. Many studies have explored the participation of molecular chaperones in Parkinson's disease, Alzheimer's disease, Amyotrophic lateral sclerosis, and Huntington's diseases. In this review, we highlighted the constructive role of molecular chaperones in neurological diseases characterized by protein misfolding and aggregation and their capability to control aberrant protein interactions at an early stage thus successfully suppressing pathogenic cascades. A comprehensive understanding of the protein misfolding associated with brain diseases and the molecular basis of involvement of chaperone against aggregation-induced cellular stress might lead to the progress of new therapeutic intrusion-related to protein misfolding and aggregation.