Acetylcholinesterase Inhibition as a Relevant Biomarker in Environmental Biomonitoring: New Insights and Perspectives pp. 87-116
Authors: (M.G. Lionetto, R. Caricato, A. Calisi, T. Schettino, Dept. of Biological and Environmental Sciences and Technologies, University of Salento, Lecce, Italy)
Abstract: Acetylcholinesterase (AChE) is a key enzyme in the nervous system, terminating nerve impulses by catalyzing the hydrolysis of neurotransmitter acetylcholine. AChE is the target site of inhibition by organophosphorus and carbamate pesticides. In particular, organophosphorous pesticides inhibit the enzyme activity by covalently phosphorylating the serine residue within the active site group. They irreversibly inhibit AChE, resulting in excessive accumulation of acetylcholine, leading to the hyperactivities and consequently paralysis of the neural and muscle system. Therefore, monitoring of AChE inhibition is widely used as a biomarker of organophosphorous and carbamate exposure either in aquatic or terrestrial environments. Recently, new insights are emerging in the use of AChE as biomarker in environmental biomonitoring. A number of important contaminants other than carbamate and organophosphorus pesticides have recently been shown to have anticholinesterase properties, including heavy metals, detergents, hydrocarbons, and herbicides. It is also worth noting that not only different compounds may reach levels of significance in terms of anticholinesterase effect, but, moreover, combinations of different chemical classes were shown to be highly synergistic in their ability to inhibit AChE activity.
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