Bivalve Esterases as Biomarker: Identification and Characterization in European Cockles (Cerastoderma edule)

Nilin, Jeamylle; Monteiro, Marta S.; Domingues, Inês; Loureiro, Susana; Costa-Lotufo, Letı́cia V.; Soares, Amadeu M.V.M.

doi:10.1007/s00128-012-0521-2

Cited by 16 publications

(4 citation statements)

References 25 publications

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“…Cholinesterases, in particular, AChE, have been found in tissues from our test species, C. edule (Guinot et al, 2012;Nilin et al, 2012). This enzyme is inhibited by several neurotoxicants.…”

Section: Oxidative Stressmentioning

confidence: 72%

Assessment of carbamazepine acute toxicity in the cockle Cerastoderma edule through chemical, physiological and biochemical tools

et al. 2022

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The cockle Cerastoderma edule was exposed to four concentrations (5, 10, 20 and 70 μg L-1) of carbamazepine (CBZ). This anticonvulsant was found to alter the mussel behavior of by reducing its clearance rate (CR). Analysis of CBZ accumulation in tissues of C. edule was carried out using HPLC-UV after 48 or 96 hours of exposure. In addition, an overproduction of H2O2 by the bivalves was detected following exposure to CBZ but nitrite levels remained unchanged. Moreover, superoxide dismutase and catalase activities showed a significant increase in relation to their contact with CBZ. The activity of the biotransformation enzyme gluthatione-S-transferase did not change during exposure. Malondialdehyde (MDA) levels indicating cellular damage, increased when bivalves were exposed to 20 and 70 μg l-1 of carbamazepine for 96 h CBZ. The results also indicate that acetylcholinesterase activity (AChE) was inhibited in all CBZ concentrations during the 48 h exposure period. However, during the 96 h exposure period, AChE was only inhibited at the highest concentration. Further studies are needed now for more exploration of the toxicity of CBZ since it could be bioaccumulable throughout the food web and may affect non-target organisms.

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Section: Oxidative Stressmentioning

confidence: 72%

Assessment of carbamazepine acute toxicity in the cockle Cerastoderma edule through chemical, physiological and biochemical tools

et al. 2022

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“…Enzyme activity was determined at room temperature 25°C by the Ellman method [18], and using thioacetate (PSA) for measuring CbE enzyme activity or by using thiocholine (e.g., AcTChI, BuTChI, or PrTChI substrate) for measuring ChE enzyme activities [19]. Subsequent combination of thioacetate or thiocholine derivatives with DTNB forms the yellow anion 5-thio-2-nitrobenzoic acid (TNB), which absorbs strongly at 410 nm [20].…”

Section: Methodsmentioning

confidence: 99%

A Method for Fast Assessment of OP/CB Exposure in the Japanese Quail (Coturnix coturnix japonica) Using Combined Esterases Enzyme Activity as Biomarkers

Abass

2014

Enzyme Research

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The aims of this study were to investigate the presence of different esterase activities in plasma and liver for Japanese quail and to combine determination of both carboxylesterase and cholinesterase as biochemical biomarker in order to identify the effects of carbamate and organophosphate compounds exposure. Carboxylesterase exhibits larger sensitivity to carbamate and organophosphate compounds than to cholinesterase and is present at higher levels. This permitted nature and distribution of carboxylesterase or cholinesterase to be measured. One predominant toxicological form of enzyme level constant in its patterns of motivation and inhibition with cholinesterase was identified in plasma with an apparent Michaelis constant for butyrylthiocholine iodide of 0.394 mM. Carboxylesterase activity in liver was considered by its preferential hydrolysis of the S-phenyl thioacetate. A concentration dependent decrease of carboxylesterase and cholinesterase has demonstrated during in vitro incubation of malathion, parathion, and trichlorfon in the range 0.125–2 mM, while with methomyl was in the range 0.25–4 mM. When quail (n = 15) was exposed orally for 48 h to concentrations of carbamate or organophosphate compounds of 3–200 mg/kg, the percentage inhibition of cholinesterase was in each case larger than that of carboxylesterase and reached statistical significance (P < 0.05) at lower concentrations.

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“…Esterase enzyme activity was determined at room temperature 25°C by the Ellman method [22], using thioacetate (PSA substrate) for measuring CbE activity or by using thiocholine (AcTChI substrate) for measuring ChE activity [2, 23]. Subsequent combination of thioacetate or thiocholine derivatives with DTNB forms the yellow anion 5-thio-2-nitrobenzoic acid, which absorbs strongly at 410 nm [24].…”

Section: Methodsmentioning

confidence: 99%

Experimental Measurements for the Effect of Dilution Procedure in Blood Esterases as Animals Biomarker for Exposure to OP Compounds

Abass

2014

BioMed Research International

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Organophosphate compounds can bind to carboxylesterase, which may lower the concentration of organophosphate pesticides at the target site enzyme, cholinesterase. It is unclear from the literature whether it is the carboxylesterase affinity for the organophosphate and/or the number of carboxylesterase molecules that is the dominant factor in determining the protective potential of carboxylesterase. The fundamental dilutions and kinetic effects of esterase enzyme are still poorly understood. This study aims to confirm and extend our current knowledge about the effects of dilutions on esterases activities in the blood for birds with respect to protecting the enzyme from organophosphate inhibition. There was significantly higher esterases activities in dilution 1 : 10 in the all blood samples from quail, duck, and chick compared to other dilutions (1 : 5, 1 : 15, 1 : 20, and 1 : 25) in all cases. Furthermore, our results also pointed to the importance of estimating different dilutions effects prior to using in birds as biomarker tools of environmental exposure. Concentration-inhibition curves were determined for the inhibitor in the presence of dilutions 1 : 5, 1 : 10, plus 1 : 15 (to stimulate carboxylesterase). Point estimates (concentrations calculated to produce 20, 50, and 80% inhibition) were compared across conditions and served as a measure of esterase-mediated detoxification. Results with well-known inhibitors (malathion) were in agreement with the literature, serving to support the use of this assay. Among the thiol-esters dilution 1 : 5 was observed to have the highest specificity constant (k cat/K m), and the K m and k cat values were 176 μM and 16,765 s−1, respectively, for S-phenyl thioacetate ester, while detected in dilution 1 : 15 was the lowest specificity constant (k cat/K m), and the K m and k cat values were 943 μM and 1154 s−1, respectively, for acetylthiocholine iodide ester.

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Bivalve Esterases as Biomarker: Identification and Characterization in European Cockles (Cerastoderma edule)

Cited by 16 publications

References 25 publications

Assessment of carbamazepine acute toxicity in the cockle Cerastoderma edule through chemical, physiological and biochemical tools

Assessment of carbamazepine acute toxicity in the cockle Cerastoderma edule through chemical, physiological and biochemical tools

A Method for Fast Assessment of OP/CB Exposure in the Japanese Quail (Coturnix coturnix japonica) Using Combined Esterases Enzyme Activity as Biomarkers

Experimental Measurements for the Effect of Dilution Procedure in Blood Esterases as Animals Biomarker for Exposure to OP Compounds

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