Characteristics of cholinesterase of the earthworm Eisenia foetida

Andersen, Reidar; Aune, Trond Erik Vee; Barstad, J. A. B.

doi:10.1016/0306-4492(78)90115-6

Cited by 14 publications

(12 citation statements)

References 32 publications

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“…80) Indeed, a half-aging time (AT50)-defined as the time elapsed since in vitro ChE inhibition at which 2-PAM reactivated the 50% of normal activity-of 22 and 14 h was estimated for ChE activity of L. terrestris and E. fetida, respectively. 80) This observation was previously documented by Andersen et al, 37) who found that the AT50 of E. fetida ChE activity previously inhibited with paraoxon (5ϫ10 Ϫ6 M) was 12 h using 5ϫ10 Ϫ5 M 2-PAM. These in vitro results were reproduced in an in vivo trial with the species L. terrestris exposed for 48 h to chlorpyrifos-spiked soils.…”

Section: Need For Complementary Methods Of Pesticide Exposuresupporting

confidence: 67%

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Environmental applications of earthworm esterases in the agroecosystem

Sánchez-Hernández

2010

J. Pestic. Sci.

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Chemical control of pests is still necessary in agriculture, despite the growing efforts to introduce biocontrolbased strategies. Many studies have evidenced the harm of pesticide side-effects on natural populations of pest enemies and other non-target organisms. Moreover, pesticide-contaminated soils can act as a secondary pollution source causing contamination in environmental compartments of critical concern to public health (water resource). These environmental risks need to be assessed and monitored for decision-making related to the post-authorization management of pesticides. Under these considerations, earthworm esterases can be a suitable tool for these regulatory and environmental purposes. Herein, it is suggested the use of earthworm esterases as biomarkers to be included in a field toxicity test. Furthermore, the potential role of gut carboxylesterases (CEs) in the modulation of pesticide toxicity is discussed in view of their contribution to the natural tolerance of earthworms to pesticides, and consequently the appropriate selection of earthworm species for regulatory toxicity testing. Finally, it is postulated that CE secretion into the earthworm gut could be an environmental friendly methodology in the enzymatic bioremediation of pesticide-contaminated soils.

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Section: Need For Complementary Methods Of Pesticide Exposuresupporting

confidence: 67%

“…35) These two ChEs in E. fetida was later corroborated by Scaps et al, 36) although Andersen et al 37) reported the presence of a ChE activity solely in this earthworm species. Esterase characterization has also been performed with other earthworm species.…”

Section: The Pastsupporting

confidence: 49%

Environmental applications of earthworm esterases in the agroecosystem

Sánchez-Hernández

2010

J. Pestic. Sci.

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“…21) As with other organisms, earthworm AChE inhibition has been one of the most studied biomarkers of pesticide exposure in the past. [22][23][24] Some laboratory studies have shown that the measurement of AChE inhibition in earthworms is a sensitive biomarker to assess exposure to OPs and CBs (Table 1). Similarly, CbE activity has been explored in earthworms exposed to pesticides.…”

Section: Need For Field Studiesmentioning

confidence: 99%

Earthworm biomarkers of pesticide contamination: Current status and perspectives

Rodríguez-Castellanos

Sánchez-Hernández²

2007

J. Pestic. Sci.

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Earthworms are standard test organisms in soil toxicity testing. They have been broadly used to assess environmental impact from heavy metal pollution; however, the knowledge on toxic effects from pesticides upon these organisms is still very limited. One of the ecotoxicological approaches to assess pollutant bioavailability and sublethal effects is the use of molecular and biochemical biomarkers. This review focuses on five issues that need further investigation: 1) field validation of earthworm biomarkers of pesticide exposure (e.g., cholinesterases) as well as testing and development in earthworms of those biomarkers of pesticide exposure currently used in other organisms (e.g., carboxylesterases), 2) the impact of environmental and biological interfering factors upon biomarker responses, 3) the development of biomarker-based approaches to assess long-term pesticide exposure, and 4) the need to develop biomarkers of behavioural and reproductive disruption with direct implications at individual and population levels.

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“…However, the moderate differences among V,,,, values for the various choline esters suggest that this enzyme form does not effectively discriminate differently sized substrates, likely owing to a lack of steric restriction of the active site. On the other hand, the lack of a marked preference for one of the thiocholine esters is a common feature of several cholinesterases from Invertebrata such as Sipunculus nudus (Talesa et al, 1993), the annelids Hirudo medicinalis (Principato et al, 1983 ;Talesa et al, 1995 a) and Eisenia foetida (Andersen et al, 1978;Stenersen, 1980) or from the crustacean Palinurus vulgaris (Talesa et al, 1992b) and the mollusc Murex brandaris (Talesa et al, 1990(Talesa et al, , 1994. The V~~~~~nnx(BISCho)/V,nax(AcSC,,o) ratio (0.6) for a cholinesterase is very similar to that for Drosophila head acetylcholinesterase and intermediate to those of inammaliaii acetylcholinesterases and butyrylcholinesterases (Gnagey et al, 1987).…”

Section: B Vncmentioning

confidence: 99%

Acetylcholinesterase in Dendrobaena veneta (Oligochaeta: Opisthopora) is Present with Forms Sensitive and Insensitive to Phosphatidylinositol Phospholipase C

Talesa

Romani

Rosi

et al. 1996

European Journal of Biochemistry

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Three distinct acetylcholinesterases were detected in the annelid oligochaete Dendrobuenu veneta.Two enzymes (a, p), copurified from a Triton-X-l 00-soluble extract of whole animals by affinity (edrophonium-Sepharose) chromatography, were separately eluted from a Sephadex G-200 column. Gel-filtration chromatography, sedimentation analysis and SDS/PAGE showed the a and p forms to be a globular dimer (1 10 kDa, 7.0 S) and a hydrophilic monomer (58 kDa, 5.0 S) respectively, both weakly linked to the cell membrane. The third form ( y ) , also purified to homogeneity by slower filtration through an edrophonium-Sepharose matrix, proved to be an amphiphilic globular dimer ( 1 33 kDa, 7.0 S) with a phosphatidylinositol anchor giving cell membrane insertion, detergent (Triton X-100, Brij 96) interaction and self-aggregation. The a acetylcholinesterase showed a fairly low substrate specificity : the p form hydrolyzed propionylthiocholine at the highest rate and was inactive on butyrylthiocholine ; the y acetylcholinesterase, showing a marked active-site specificity with differently sized substrates, was likely functional in cholinergic synapses. Studies with inhibitors showed incomplete inhibition of all three acetylcholinesterase by 1 mM eserine and different sensitivity for edrophonium or procainamide. The a and p forms, sensitive to 1,5-bis(4-allyldimethylammoniumphenyl)-pentan-3-one dibromide, were unaffected by tetra(monoisopropy1)-pyrophosphortetramide, while both these agents inhibited the y enzyme. All three forms showed excess-substrate inhibition by acetylthiocholine. Enzyme activity was histochemically localized in the nerve ring and its minor branches. Monomeric acetylcholinesterase (p) is likely the only form present in the ganglionic glial framework.

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Characteristics of cholinesterase of the earthworm Eisenia foetida

Cited by 14 publications

References 32 publications

Environmental applications of earthworm esterases in the agroecosystem

Environmental applications of earthworm esterases in the agroecosystem

Earthworm biomarkers of pesticide contamination: Current status and perspectives

Acetylcholinesterase in Dendrobaena veneta (Oligochaeta: Opisthopora) is Present with Forms Sensitive and Insensitive to Phosphatidylinositol Phospholipase C

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