1Department of Biotechnology, Dr MGR Educational Research Institute and University, Chennai 95 India. 2Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai 25 India.
Ref: tp:// www.ijppsjournal.com/Vol6Issue6/3524.pdf
Objectives: To investigate the protective role of α-crystallin against β-amyloid aggregation.
Methods: In vitro spectroscopic methods and cell culture studies were done to validate our objective.
Results: The molecular basis of alzhemiers disease has been proposed to be accumulation and aggregation of β-amyloid (Aβ). However, prevention of β-amyloid aggregation is still a promising means to reduce its neurotoxicity. In this work, we show that α-crystallin was able to inhibit cellular toxicity of Aβ on astrocytes and lymphocytes. Theα−crystallin (αA and αB): the two vertebrate eye lens proteins that are related to the small heat shock protein family, was able to reverse the oxidative stress induced by Aβ1-42. Treatment of α-crystallin enhances the activity of proteasome and it also induces the expression of Hsp70 which is known to inhibit the intramolecular misfolding. We also demonstrate that Aβ1-42 suppresses the expression of TriC chaperonin subunits TCPβ and TCPε, which are known to play a role in folding of misfolded proteins.α-crystallin reverses this effect and enhances the expression of TCPβ and TCPε.
Conclusions: Research findings in this study provide the basis for the development of novel pharmacotherapy for Alzhemier’s disease.
Keywords: Alzhemiers disease, α-crystallin, Proteasome, HSP70, TCPβ and TCPε.
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KGG acknowledges Director CLRI, HEAD Biorganic Lab(Late Dr. Neela Kanta Reddy), Er. ACS. Arun Kumar -President Dr MGR Educational Research Institute and Univesity for Providing Lab Support, Dr. P. T Perumal Emeritus scientist Organic Chemistry for Valuable Suggestions.