Rabbit Anti-HSP60 monoclonal antibody, clone TU59-15

Toxic effects of continuous low dose application of the antifouling biocide chlorine on marine benthic organisms were monitored using transplanted green mussels (Perna viridis) and a suite of biomarkers. Caged mussels were deployed in chlorinated and non-chlorinated sections of the cooling system of an operating electric power plant. Biomarkers indicative of general stress, oxidative stress (superoxide dismutase and catalase), and DNA integrity, along with expression of stress proteins, were studied to assess the effects. Deterioration in condition index with corresponding increase in DNA strand breaks was indicative of chlorine stress. Superoxide dismutase enzyme did not show any particular trend, but catalase activity was high during the initial days of exposure at the chlorinated site; later, it became almost equal to that at the control site. Similarly, expressions of stress proteins (HSP60, HSP70, HSP22, GSTS1, and CYP4) showed bell-shaped pattern during the period of study. Positive correlation among the endpoints indicated the utility of the multimarker approach to monitor the effects of continuous low dose chlorination on mussels.

The activity of specific tyrosine protein kinases is known to be associated with the production of oncogenes. A specific inhibitor of tyrosine protein kinases can be effective not only as an antitumor agent but also as a tool for studying the physiological role of tyrosine phosphorylation. Among similar inhibitors, the flavonoid genistein was shown to have the most specific effect. This agent almost completely inhibited phosphorylation of tyrosine residues, while the activity of serine and threonine protein kinases was slightly suppressed. At the same time, another flavonoid quercetin inhibited activities of tyrosine kinase and other protein kinases with equal efficacy. The aim of the work was to study the effect of genistein on phosphorylation of maize mitochondrial proteins at the tyrosine residues for the assessment of signal cascades associated with tyrosine protein kinases. It was first revealed that tyrosine phosphorylation occurred in the maize mitochondrial heat shock protein 60 (HSP60) and the protein of 90 kDa. Phosphorylation of the 90-kDa protein is observed only during the treatment of isolated mitochondria with genistein. The study of the activity of mitochondrial respiratory complex V showed a significant decrease in the hydrolytic activity of the mitochondrial ATPase after exposure to genistein. The activating effect of this agent on mitochondrial protein kinases can be explained by changes in the redox state of mitochondria due to inhibition of mitochondrial ATPase by genistein.