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. 2020 Jul 2;12(7):e8960. doi: 10.7759/cureus.8960

Table 1. Details of some of the studies from the review.

Author’s Name Year of Publication Result Conclusion
Lyu et al. [40] 2020 In canine retinal pigment epithelium (RPE) cells, arsenite-induced stress caused a significant increase in heat shock protein 70 (HSP70) expression. In addition, leucinostatin stimulated HSP70 expression by inducing heat shock factor-1.   This study suggests that leucinostatin enhances heat shock factor-1 to increase HSP70 expression in RPE cells.
McArdle et al. [11] 2019 The ability of a skeletal muscle to respond to an increase in reactive oxygen species (ROS) generation using an increased expression of HSP-like proteins decreases with age. This affects ROS homeostasis.   Advancing age disturbs the physiological functioning of ROS. In chronic cases, this results in neurodegenerative disorders.
Yang et al. [17] 2019 4-HNE induces late apoptosis in ARPE-19 cells, with increased levels of 4-HNE-modified HSP70 which decreased the levels of XIAP. HSP70 can induce to apoptosis if it is modified by HNE.
Yang et al. [34] 2019 Intracellular HSP70 suppressed the production of pro-inflammatory cytokines. 4-HNE facilitated pro-inflammatory action in RPE cells by increasing the extracellular release of HSP70. However, when combined with efflux inhibitor methyl-β-cyclodextrin (MBC), the release of HSP70 was reduced and a decrease in levels of IL-6 was found.    HNE-induced modification of HSP70 antagonizes the anti-inflammatory role of HSP70 and boosts the level of IL-6. This effect can be blocked by administrating MBC.
Wang et al. [43] 2016 Results show that in non-damaging retinal therapy (NRT) the activation of protein can take place in a range of 25%-40%.    This study shows that there is a very narrow range of non-lethal activation of HSP70 by NRT.
Subrizi et al. [28] 2015 On exposing ARPE-19 cells with hydrogen peroxide, IL-6 production was reduced in cells treated with recombinant human HSP70 (rhHSP70), and also improved cell viability. rhHSP70 was localized in lysosomes. Exogenously delivered HSP70 localizes in lysosomes and improves the viability of ARPE-19 on administration.
Yang et al. [36] 2013 Giving HSP70 exogenously, inhibited subretinal fibrosis in mice with Toll-like receptor (TLR)2/TLR4 and induced IL-10 but not in TLR2 and TLR4-deficient mice   Results suggest that exogenous HSP70 exhibits anti-inflammatory action by combining with TLR2/TLR4.
Ryhänen et al. [39] 2009 The study suggested that accumulation of lysosomes can be reversed. Also, it stated that autophagy aids in the clearance of deposits due to proteasomal inhibition.   After the failure of the proteasome-mediated pathway, autophagy is stimulated. It helps in clearing the toxic cellular material but excess stimulation can result in degradation of tissues.