A study of sister chromatid exchange in patients with dental amalgam restorations.

Study Background: Dental amalgam is still widely used as a restorative material in developing countries due to its low cost and ease of manipulation. The health risks associated with the components of this restorative material has always been a matter of concern. Our study was designed to address this question regarding dental amalgam. Objective: To study sister chromatid exchange (SCE) as an indicator of systemic genotoxicity, due to the exposure from the components of amalgam restorations during its placement and chronic use. Materials and Methods: Systemic genotoxicity in subjects exposed to amalgam during its placement (Group II; n = 5) and subjects with chronic exposure to amalgam (Group III; n = 5) were compared with controls (Group I; n = 5) by SCE assay in cultured peripheral blood lymphocytes. Result: Subjects exposed to amalgam during its placement and subjects having chronic exposure to amalgam showed an increase in the frequency of SCE, but the change was not statistically significant (P = 0.84, P = 0.123 respectively). Conclusion: Systemic genotoxicity was not observed due to the components of amalgam restorations released during its placement and chronic use. The findings of this study can be considered as preliminary information on the systemic toxicity due to the components of amalgam restorations.

Structural and functional analysis of cathepsin S of Heterodera spp: A promising candidate for its control.

Cysteine proteinases are required for a wide range of physiological processes in all living organisms. In parasitic nematodes, they are particularly crucial for the digestion of host tissues and evasion of host immune responses. Therefore, in general, these are identified as primary targets for the control of parasitic nematodes. Herein, cathepsin S-like cysteine proteinase of Heterodera avenae (Hacp-s) has been cloned and analysed for the first time. The predicted protein is 298 amino acids long and showed significant similarity with cathepsin S of Heterodera glycines (Hgcp-s). The sequence of cathepsin S contains a signal peptide of 30 amino acids which suggests its role in extracellular functions. Multiple sequence alignment revealed the presence of ERFNIN motif and conserved catalytic residues. Three dimensional structure (3D) of Hgcp-s was modelled using homology modelling. In order to illustrate the plausible mode of interaction of cathepsin S (Hgcp-s), docking analysis was performed with E-64 cysteine proteinase inhibitor. Docking studies revealed the hydrogen bonding of E-64 with Gln153, His299 and Gly203 as well as close interaction with catalytic residues Cys159 and Asn320. Expression analysis of Hacp-s using qRT-PCR showed high expression of cathepsin S in pre parasitic J2s and female stages suggesting its significant role in both pre-parasitic and parasitic stages of the nematode life cycle.