Heat shock proteins (HSPs) in the homeostasis of regulatory T cells (Tregs)

Abstract

Heat shock proteins (HSPs) belong to the family of conservative polypeptides with a high homology of the primary structure. The uniqueness of this family lies in their ability to interact with a large number of different proteins and provide protection from cellular and environmental stress factors as molecular chaperones to keep protein homeostasis. While intracellular HSPs play a mainly protective role, extracellular or membrane-bound HSPs mediate immunological functions and immunomodulatory activity. In immune system are subsets of cells including regulatory T cells (Tregs) with suppressive functions. HSPs are implicated in the function of innate and adaptive immune systems, stimulate T lymphocyte proliferation and immunomodulatory functions, increase the effectiveness of cross-presentation of antigens, and induce the secretion of cytokines. HSPs are also important in the induction, proliferation, suppressive function, and cytokine production of Tregs, which are a subset of CD4+ T cells maintaining peripheral tolerance. Together HSPs and Tregs are potential tools for future clinical interventions in autoimmune disease.

Exploration of Survival Traits, Probiotic Determinants, Host Interactions, and Functional Evolution of Bifidobacterial Genomes Using Comparative Genomics

“…Similarly, the bacterial DnaJ protein is found to induce pro-inflammatory cytokine production in macrophages through the PI3K/JNK signaling pathway [ 84 ]. It also inhibits the proliferation of autoreactive T cells and induces the expression of IL-10 in the patients with rheumatoid arthritis [ 85 ]. The extracellular PHBifsCore was also found to harbor von Willebrand A (VWA) domain-containing proteins, which are known to interact with the epithelial extracellular matrix [ 86 ].…”

Copper or/and arsenic induce oxidative stress-cascaded, nuclear factor kappa B-dependent inflammation and immune imbalance, trigging heat shock response in the kidney of chicken

“…As sophisticated stress response mechanisms to maintain or re-establish cellular homeostasis, heat shock proteins unselectively bind to hydrophobic protein sequences liberated by denaturation and keep protein homeostasis from cellular and environmental stress factors as molecular chaperones [ 43 ]. Exposure to arsenic stimulation greatly increases the phosphorylation levels of Hsp27/40/60/70/90, inhibiting protein phosphatase activity in human urothelial cells [ 44 ], Bursa of Fabricius, spleen and thymus of chickens [ 25 ].…”

Mild hypothermia provides Treg stability

“…As hypothermia is associated with cold stress, we aimed to analyse expression of heat shock proteins (HSPs) −60, −70 and −90 that are molecular chaperones known to protect cells from cellular and environmental stress factors 22 . However, no differences in intracellular expression of HSP-60, −70 and −90 (Figure S2 ), as well as their gene transcription (Table S1 ) were found between Tregs expanded at 33 and 37 °C.…”

“…Prolonged hypothermia is associated with cold stress, therefore in the current study we measured intracellular expression and gene transcription of HSPs, phylogenetically conserved proteins known to protect the cells from cellular and environmental stress 22 . We hypothesized that hypothermia enhances expression of these molecules and that HSPs are responsible for preservation of Treg stability in vitro .…”