Dynamics of Heat Shock Proteins in Immunity and Aging
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.
KeywordsAging C. elegans Heat shock factor -1 Heat shock proteins Immunity
heat shock factor
heat shock proteins
post translational modification
ribonucleic acid interference
reactive oxygen species
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).
- Li Z, Srivastava P (2004) Heat-shock proteins. Curr Protoc Immunol Appendix 1:Appendix 1T https://doi.org/10.1002/0471142735.ima01ts58
- Morrison JK, Friday AJ, Henderson MA, Hao E, Keiper BD (2014) Induction of cap-independent BiP (hsp-3) and Bcl-2 (ced-9) translation in response to eIF4G (IFG-1) depletion in C. elegans. Translation (Austin) 2:e28935Google Scholar
- Riddle DL, Albert PS (1997) Genetic and environmental regulation of dauer larva development. Cold Spring Harbor Laboratory, Cold Spring HarborGoogle Scholar
- Ritossa F (1962) A new puffing pattern induced by temperature shock and DNP in Drosophila. Exp Dermatol 18:571–573Google Scholar
- Shojadoost B, Kulkarni RR, Brisbin JT, Quinteiro-Filho W, Alkie TN, Sharif S (2017) Interactions between lactobacilli and chicken macrophages induce antiviral responses against avian influenza virus. Res Vet Sci. https://doi.org/10.1016/j.rvsc.2017.10.007