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Heat Shock Proteins and Their Therapeutic Applications: An Overview

Pushpender Kumar Sharma, Assistant Professor, Department of Biotechnology, Sri Guru Granth Sahib World University, Fatehgarh Sahib, Punjab140406, India. , Jasleen Saini1 , Jaspreet Kaur Boparai2 , Ramanpreet Kaur2 , Pushpender Kumar Sharma3

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RFP Journal of Biochemistry and Biophysics 2(1):p 41-52, January - June 2017. | DOI:

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Abstract

 Heat shock proteins (HSPs) are a class of proteins that play important role in protein folding, maintaining homeostasis, and suppressing the aggregation of misfolded proteins. The synthesis of these proteins in the cell is highly regulated, and is induced under various stress conditions that include the pH, temperature, and starvation, UV and chemical exposure and the oxidative stresses; however few Hsps also expresses constitutively. The major classes of HSPs include the HSP60, HSP70 and HSP90 and the small heat shock proteins that ranges from 1240 kDa in size. The small heat shock proteins like Hsps 18 are well known to facilitate the refolding of substrate proteins and maintaining its biological activity, for which this protein has been explored as an efficient delivery system for the vaccines development. This review will discuss various HSPs and their close relatives involved in folding, assembly, regulation, and degradation of other proteins. The review will further highlight the various approaches by virtue of which the Hsps can be employed in therapeutic interventions.

Keywords: Molecular Chaperons; Folding; Therapeutics; Cancer; Stress; Heat Shock Protein.

 

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