Cholinesterase activity in Gammarus pulex (Crustacea Amphipoda): Characterization and effects of chlorpyrifos

Xuereb, Benoît; Noury, Patrice; Felten, Vincent; Garric, Jeanne; Geffard, Olivier

doi:10.1016/j.tox.2007.04.010

Cited by 67 publications

(37 citation statements)

References 60 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…However, On the contrary, this OP increased AChE activity in S. inaequivalvis after 15 days of exposure 346 to 0.3 nM (Romani et al, 2005), which comforts our results on V. piscinalis; however, the 347 biological explanation remains unknown. IC 50 of chlorpyrifos for AChE was 9.71 nM in P. 348 antipodarum at 96 h, which was ten times higher that for G. pulex in the same experimental 349 conditions (Xuereb et al, 2007 control. However, a high mortality was observed in N. diversicolor contaminated with 361 parathion and malathion when 55% of AChE inhibition occurred (Scaps et al, 1997).…”

mentioning

confidence: 86%

“…However, a high mortality was observed in N. diversicolor contaminated with 361 parathion and malathion when 55% of AChE inhibition occurred (Scaps et al, 1997). A high 362 mortality and 70% of AChE inhibition also occurred in G. pulex exposed to chlorpyrifos 363 (Xuereb et al, 2007). More research is needed to clarify the relationships between OP 364 exposure, AChE inhibition and mortality.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Cholinesterase activities as potential biomarkers: Characterization in two freshwater snails, Potamopyrgus antipodarum (Mollusca, Hydrobiidae, Smith 1889) and Valvata piscinalis (Mollusca, Valvatidae, Müller 1774)

et al. 2008

Self Cite

View full text Add to dashboard Cite

mentioning

confidence: 86%

mentioning

confidence: 99%

Cholinesterase activities as potential biomarkers: Characterization in two freshwater snails, Potamopyrgus antipodarum (Mollusca, Hydrobiidae, Smith 1889) and Valvata piscinalis (Mollusca, Valvatidae, Müller 1774)

et al. 2008

Self Cite

View full text Add to dashboard Cite

“…External factors such as food supply, ambient temperature, and water quality can also alter in vivo activity of the enzyme (Hill, 1989;Phillips et al, 2002;Xuereb et al, 2007;Garabrant et al, 2009). These factors impair determination of the "normal" activity of ChE and thus hinder identification of "abnormal" activity, including that caused by anticholinesterases.…”

Section: Introductionmentioning

confidence: 99%

Developing antibodies from cholinesterase derived from prokaryotic expression and testing their feasibility for detecting immunogen content in Daphnia magna

Liu

Yuan

2016

J. Zhejiang Univ. Sci. B

View full text Add to dashboard Cite

Abstract:To yield cholinesterase (ChE) from prokaryotic expression, the ChE gene that belongs to Daphnia magna was amplified by reverse transcription-polymerase chain reaction (RT-PCR) using forward primer 5'-CCCYGGNGCSAT GATGTG-3' and reverse primer 5'-GYAAGTTRGCCCAATATCT-3'. To express the gene, one sequence of the amplified DNA, which was able to encode a putative protein containing two conserved carboxylesterase domains, was connected to the prokaryotic expression vector PET-29a(+). The recombinant vector was transformed into Escherichia coil BL21 (DE3). Protein expression was induced by isopropy-D-thiogalactoside. The expressed ChE was used as an immunogen to immunize BALB/c mice. The obtained antibodies were tested for their specificity towards crude enzymes from species such as Alona milleri, Macrobrachium nipponense, Bombyx mori, Chironomus kiiensis, Apis mellifera, Eisenia foetida, Brachydanio rerio, and Xenopus laevis. Results indicated that the antibodies had specificity suitable for detecting ChE in Daphnia magna. A type of indirect and non-competitive enzyme-linked immunosorbent assay (IN-ELISA) was used to test the immunoreactive content of ChE (ChE-IR) in Daphina magna. The detection limit of the IN-ELISA was found to be 14.5 ng/ml at an antiserum dilution of 1:22 000. Results from tests on Daphnia magna exposed to sublethal concentrations of triazophos indicated a maximal induction of 57.2% in terms of ChE-IR on the second day after the animals were exposed to a concentration of 2.10 μg/L triazophos. Testing on animals acclimatized to a temperature of 16 °C indicated that ChE-IR was induced by 16.9% compared with the ChE-IR content detected at 21 °C, and the rate of induction was 25.6% at 10 °C. The IN-ELISA was also used to test the stability of ChE-IR in collected samples. Repeated freezing and thawing had no influence on the outcome of the test. All these results suggest that the polyclonal antibodies developed against the recombinant ChE are as efficient as those developed against the native ChE in detecting ChE content in Daphnia magna.

show abstract

“…However, AChE is selectively inhibited by 1,5-bis (4-allyldimethyl-ammoniumphenyl)-pentan-3-one dibromide (BW284c51) but not by tetraisopropylpyrophosphoramide (iso-OMPA). BChE is selectively inhibited by iso-OMPA (Massoulié et al 1993;Key & Fulton 2002;García-de la Parra et al 2006;Xuereb et al 2007). Inhibition of AChE by toxicants causes an accumulation of ACh at cholinergic synapses resulting in hyperactivation of postsynaptic cholinergic receptors.…”

Section: Introductionmentioning

confidence: 99%

“…Chlorpyrifos exerts its toxicity by inhibiting ChE activity (Xuereb et al 2007). In addition to its neurotoxicity, chlorpyrifos induces oxidative stress in an organism either by generating reactive oxygen species (ROS) or interfering with the antioxidant defense mechanism (Kavitha & Venkateswara Rao 2008).…”

Section: Introductionmentioning

confidence: 99%

Enzymatic responses of the riceland prawn, Macrobrachium lanchesteri, to chlorpyrifos exposure

2012

View full text Add to dashboard Cite

Cholinesterase (ChE) was characterized in whole bodies of adult riceland prawns, Macrobrachium lanchesteri, based on substrate preference and inhibitor sensitivity. M. lanchesteri ChE activity was mainly attributable to acetylcholinesterase (AChE) since it preferentially hydrolyzed an AChE-specific substrate, acetylthiocholine iodide, over s-butyrylthiocholine iodide and was sensitive to 1,5-bis-(4-allyldimethyl-ammoniumphenyl)-pentan-3-one dibromide, a specific inhibitor for AChE. The effect of chlorpyrifos exposure on M. lanchesteri were also investigated. The 24, 48, 72 and 96 h LC50 values for chlorpyrifos were 3.37, 2.76, 2.58 and 2.53 µg L −1 , respectively. Based on these values, adult M. lanchesteri were exposed to 0.5, 1.5, 2.5 and 3.5 µg chlorpyrifos L −1 for 24, 48, 72 and 96 h. Chlorpyrifos appeared to induce drastic enzymatic responses in M. lanchesteri. AChE activity was inhibited after 24 h of exposure in a dose-and time-dependent manner. The levels of lipid peroxidation increased significantly after 24 h of exposure. However, the activities of the antioxidant enzyme, catalase, and the detoxification enzyme, glutathione S-transferase, were reduced. In conclusion, M. lanchesteri is sensitive to chlorpyrifos and can serve as a bioindicator species for freshwater environmental assessment.

show abstract

Cholinesterase activity in Gammarus pulex (Crustacea Amphipoda): Characterization and effects of chlorpyrifos

Cited by 67 publications

References 60 publications

Cholinesterase activities as potential biomarkers: Characterization in two freshwater snails, Potamopyrgus antipodarum (Mollusca, Hydrobiidae, Smith 1889) and Valvata piscinalis (Mollusca, Valvatidae, Müller 1774)

Cholinesterase activities as potential biomarkers: Characterization in two freshwater snails, Potamopyrgus antipodarum (Mollusca, Hydrobiidae, Smith 1889) and Valvata piscinalis (Mollusca, Valvatidae, Müller 1774)

Developing antibodies from cholinesterase derived from prokaryotic expression and testing their feasibility for detecting immunogen content in Daphnia magna

Enzymatic responses of the riceland prawn, Macrobrachium lanchesteri, to chlorpyrifos exposure

Contact Info

Product

Resources

About