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  • Title: Acetylcholinesterase inhibition in estuarine fish and invertebrates as an indicator of organophosphorus insecticide exposure and effects.
    Author: Fulton MH, Key PB.
    Journal: Environ Toxicol Chem; 2001 Jan; 20(1):37-45. PubMed ID: 11351414.
    Abstract:
    The majority of insecticides currently in use are organophosphorus, carbamate, and synthetic pyrethroid compounds. Organophosphorus insecticides (OPs) produce toxicity by inhibiting the cholinesterase enzymes in the nervous system. Monitoring of acetylcholinesterase (AChE) inhibition has been widely used in terrestrial and freshwater aquatic systems as an indicator of OP exposure and effects. This review describes the use of AChE inhibition as a biomarker in the estuarine environment, discusses the relationship between AChE inhibition and other manifestations of OP toxicity, and highlights areas where additional research is needed. A variety of studies with estuarine fish have suggested that brain AChE inhibition levels of > 70% are associated with mortality in most species. Selected species, however, appear capable of tolerating much higher levels (> 90%) of brain inhibition. Sublethal effects on stamina have been reported for some estuarine fish in association with brain AChE inhibition levels as low as 50%. Most studies suggest, however, that these effects are observed only when brain AChE inhibition is at near-lethal levels. A number of field studies have successfully used AChE inhibition in fish as a biomarker in the estuarine environment. The use of AChE inhibition as a biomarker in estuarine invertebrates has been less well studied. Although AChE inhibition has been measured in the tissues of a variety of invertebrate species following OP exposure, the relationship between AChE inhibition and lethality is less distinct. Additional work is needed in both fish and invertebrates to better explain species-specific differences in the relationship between AChE inhibition and mortality and to investigate other physiological perturbations associated with AChE inhibition.
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