Synergistic Effects of Toxic Elements on Heat Shock Proteins

Abstract

Heat shock proteins show remarkable variations in their expression levels under a variety of toxic conditions. A research span expanded over five decades has revealed their molecular characterization, gene regulation, expression patterns, vast similarity in diverse groups, and broad range of functional capabilities. Their functions include protection and tolerance against cytotoxic conditions through their molecular chaperoning activity, maintaining cytoskeleton stability, and assisting in cell signaling. However, their role as biomarkers for monitoring the environmental risk assessment is controversial due to a number of conflicting, validating, and nonvalidating reports. The current knowledge regarding the interpretation of HSPs expression levels has been discussed in the present review. The candidature of heat shock proteins as biomarkers of toxicity is thus far unreliable due to synergistic effects of toxicants and other environmental factors. The adoption of heat shock proteins as “suit of biomarkers in a set of organisms” requires further investigation.

Effect of Selenium Deficiency on Nitric Oxide and Heat Shock Proteins in Chicken Erythrocytes

“…Hsp27 is involved in cell migration, the architecture of the cytoskeleton, and cell growth [46]. Hsps, particularly Hsp60 and Hsp70, were proposed as biomarkers of exposure to heavy metals and various environmental factors [47]. Liu et al reported that the expression levels of Hsps were induced in the liver of Se-deficient chickens [22].…”

Change in redox state and heat shock protein expression in an Indian major carp <i>Cirrhinus cirrhosus</i> exposed to zinc and lead

“…HSP90 were generally used as biomarkers against metals and organic compounds' stress in marine diatom Ditylum brightwellii. Exposure to different types and doses of copper and nickel compounds was monitored, revealing stimulation of HSP90 gene expression; however the pattern of such stimulation varied (Mahmood et al, 2014).…”

HSP70-Ran-RCC1 transport system during cadmium-induced apoptosis in porcine kidney LLC-PK₁ cells

“…A variety of cellular stresses induce the nucleocytoplasmic redistribution of various functional proteins and perturbation of conventional nucleocytoplasmic transport pathways (Kose and Imamoto, 2014). HSP70 plays a protective role in cadmium cytotoxicity (Levinson et al, 1980;Mahmood et al, 2014). In this study, HSP70-Ran-RCC1 transport system was induced by cadmium exposure.…”

“…Protooncogenes such as c-myc might not be involved in cadmium-induced apoptosis of porcine kidney LLC-PK 1 cells (Ishido et al, 1998), and it has been reported that HSP70 would protect against cadmium cytotoxicity (Levinson et al, 1980;Mahmood et al, 2014). Here, we investigated the effect of cadmium on the HSP70-Ran-RCC1 transport system in porcine kidney LLC-PK 1 cells.…”