@article{Gopinathan_Gayathri_2015, title={PROTECTIVE EFFECTS OF Α - CRYSTALLIN ON Î’ - AMYLOID (Aβ) INDUCED TOXICITY}, volume={7}, url={https://journals.innovareacademics.in/index.php/ijpps/article/view/4979}, abstractNote={<p><strong>Objectives:</strong> To investigate the protective role of α-crystallin against β-amyloid aggregation.</p><p><strong>Methods:</strong> <em>In vitro</em> spectroscopic methods and cell culture studies were done to validate our objective.</p><p><strong>Results:</strong> 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.</p><p><strong>Conclusions:</strong> Research findings in this study provide the basis for the development of novel pharmacotherapy for Alzhemier’s disease.</p>}, number={2}, journal={International Journal of Pharmacy and Pharmaceutical Sciences}, author={Gopinathan, K. Gomathi and Gayathri, D.}, year={2015}, month={Feb.}, pages={588} }