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Dynamics of Heat Shock Proteins in Immunity and Aging

  • Udayakumar Prithika
  • Krishnaswamy Balamurugan
Chapter
Part of the Heat Shock Proteins book series (HESP, volume 17)

Abstract

Heat Shock Proteins (HSP) are one of the classical molecules that regulate cellular homeostasis. HSP play multifunctional roles that are crucial for folding/unfolding of proteins, cell-cycle control and signaling, and protection of cells against stress/apoptosis. HSP have also been implicated in antigen presentation with the role of chaperoning and transferring antigenic peptides and providing immunity. HSP have been referred as molecular chaperones since they assist in the repair of denatured proteins or promote their degradation after stress or injury. Moreover, HSP are likely to have anti-apoptotic properties and have been reported to be significantly elevated in a plethora of human cancers. The increase in expression levels of HSP has been robustly related with therapeutic resistance and poor survival. The immunological functions and prospective immunological repertoire of HSP put them in critical position that serves as important therapeutic implications for specific drug targets. In this chapter, we have discussed on the existing scientific data about HSP with an effort to highlight the possible future implication of HSP during stress, aging, apoptosis and their status at post-translational and mitochondrial level and the possible drug targets for improving prognosis and treatment of various diseases.

Keywords

Aging C. elegans Heat shock factor -1 Heat shock proteins Immunity 

Abbreviations

HSF

heat shock factor

HSP

heat shock proteins

PTM

post translational modification

RNAi

ribonucleic acid interference

ROS

reactive oxygen species

Notes

Acknowledgements

Dr. K. Balamurugan acknowledges the DST-SERC Fast Track Young Scientist Scheme (No. SR/FT/LS-83/2009 (G)), DST (SERB) (No. SR/SO/AS-80/2010), DBT (BT/PR14932/MED/29/233/2010), ICMR (Sanction No: 5/3/3/13/2010-ECD-I), UGC Major Research Project (No. 42-222/2013 (SR) and CSIR (No. 37(1460)/11/EMR-II), DST- FIST (Grant No. SRFST/ LSI-087/2008), PURSE (Grant No. SR/S9Z-23/2010/42(G)) and UGC SAP-DRS-I [Grant No. F.3-28/2011 (SAP-II)], New Delhi, India for financial assistances. Authors gratefully acknowledge the computational and bioinformatics facility provided by the Alagappa University Bioinformatics Infrastructure Facility (funded by DBT, GOI; Grant No. BT/BI/25/015/2012).

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Copyright information

© Springer Nature Switzerland AG 2019

Authors and Affiliations

  • Udayakumar Prithika
    • 1
  • Krishnaswamy Balamurugan
    • 1
  1. 1.Department of Biotechnology, Science CampusAlagappa UniversityKaraikudiIndia

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