PROTECTIVE EFFECTS OF Α - CRYSTALLIN ON Β - AMYLOID (Aβ) INDUCED TOXICITY

Authors

  • K. Gomathi Gopinathan Department of Biotechnology, Dr MGR Educational Research Institute and University, Chennai 95 India.
  • D. Gayathri Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai 25 India.

Keywords:

Alzhemiers disease, Nil, Proteasome, HSP70, Nil

Abstract

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.

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Published

01-02-2015

How to Cite

Gopinathan, K. G., and D. Gayathri. “PROTECTIVE EFFECTS OF Α - CRYSTALLIN ON Î’ - AMYLOID (Aβ) INDUCED TOXICITY”. International Journal of Pharmacy and Pharmaceutical Sciences, vol. 7, no. 2, Feb. 2015, p. 588, https://journals.innovareacademics.in/index.php/ijpps/article/view/4979.

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Section

Erratum