Heat Shock Proteins and Regulatory T Cells

Abstract

Heat shock proteins (HSPs) are important molecules required for ideal protein function. Extensive research on the functional properties of HSPs indicates that HSPs may be implicated in a wide range of physiological functions including immune function. In the immune system, HSPs are involved in cell proliferation, differentiation, cytokine release, and apoptosis.Therefore, the ability of the immune system, in particular immune cells, to function optimally and in unison with other physiological systems is in part dependent on signaling transduction processes, including bidirectional communication with HSPs. Regulatory T cells (Tregs) are important T cells with suppressive functions and impairments in their function have been associated with a number of autoimmune disorders. The purpose of this paper is to examine the relationship between HSPs and Tregs. The interrelationship between cells and proteins may be important in cellular functions necessary for cell survival and expansion during diseased state. 1. Introduction Optimal cellular function is regulated by several molecules including heat shock proteins (HSPs). These proteins have chaperone properties and are important in both stressed and unstressed cells. HSPs can be categorized into six diverse highly or less-conserved families. These include HSP10, HSP40, HSP60, HSP70, HSP90, and HSP100 [1-4]. HSP60 is found in themitochondria [5]. HSP70 is implicated in protein transport assembly and synthesis. It has anti-apoptotic properties that are implicated in intrinsic and extrinsic apoptotic pathways. HSP70