Actions on Insects and Other Invertebrates

Chadwick, L. E.

doi:10.1007/978-3-642-99875-1_16

Cited by 30 publications

(4 citation statements)

References 190 publications

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“…There does not exist any essential relationship between anticholinesterase and insecticidal activities (see CHADWICK 1963). Results of the experiments reported in this paper support findings (LOVELL 1963;and others) that an in vitro ChE inhibition assay by itself is not reliable as a screening system for insecticides.…”

Section: Discussionsupporting

confidence: 77%

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Anticholinesterase Activity (In the Mediterranean Fruit Fly) and Mouse Toxicity of Some New Organophosphorus Compounds

Tahori

Sternberg

Zahavy

1966

Entomologia Exp Applicata

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Section: Discussionsupporting

confidence: 77%

“…The insecticidal action of organophosphorus compounds is generally attributed to inhibition of cholinesterase (ChE) present at certain physiOlogically important sites and targets (O'BRIEN, 1960;CHADWICK, 1963). Some phosphonate esters are very potent inhibitors of ChE, for example sarin, isopropyl methyl phosphonofluoridate (ROEDER & KENNEDY 1955).…”

mentioning

confidence: 99%

Anticholinesterase Activity (In the Mediterranean Fruit Fly) and Mouse Toxicity of Some New Organophosphorus Compounds

Tahori

Sternberg

Zahavy

1966

Entomologia Exp Applicata

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“…However, ChE activity in the upper abdomen did not appear to result from AChE in the central nervous system. Chadwick et al reported that AChE is present in both the hemolymph and the nervous system, 27 and Zador et al reported the presence of soluble AChEs with different structures in addition to AChE in neurons. 28 The presence of abdominal AChE activity (confirmed via fMSI) was consistent with these reports, indicating the validity of ChE activity localization using this method.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Mass Spectrometric Enzyme Histochemistry Method Developed for Visualizing In Situ Cholinesterase Activity in Mus musculus and Drosophila melanogaster

2020

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Enzyme histochemistry facilitates enzyme activity visualization in situ; however, as it is a color-based method, molecular quantification is prohibitive. This study aimed to develop a semiquantitative, mass spectrometry imaging (MSI)-based enzyme histochemistry method to determine endogenous cholinesterase (ChE) activity. Using deuterium-labeled acetylcholine (ACh-d9) as a substrate to distinguish ACh-d9 and choline-d9 from endogenous acetylcholine and choline, respectively, the heterogeneous localization of de novo ChE activity was visualized using MSI, devoid of interferences from in situ factors. Furthermore, a tissue inhibitor assay involving two ChE inhibitors in the mouse brain revealed specific ChE inhibition in the corpus callosum. To the best of our knowledge, this study is the first to report a visualization method for total ChE activity in the ganglia and abdomen in Drosophila melanogaster, indicating its applicability among different animals. The present results provide novel insights into the applicability of enzyme histochemistry via MSI to the metabolism of low-molecular-weight organic compounds (i.e., “small molecules”) and semiquantitative capability, suggesting that MSI enzyme histochemistry may become a powerful tool for heterogeneous tissue studies.

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“…However, Ozaki (1974) cautions that these inhibitors have been shown to distinguish between esterase activities of vertebrates, but not invertebrates. Moreover, as has been pointed out by Augustinsson ( 1963), Chadwick ( 1963), andSilver ( 1974), invertebrate cholinesterases do not always fit into the vertebrate classification schemes, which are based on substrate and inhibitor specificity. In any case, these data suggest a pharmacological difference between the AChE of high and lower deuterostomes.…”

Section: Discussionmentioning

confidence: 98%

Acetylcholinesterase from the Skeletal Muscle of the Lamprey Petromyzon marinus Exists in Globular and Asymmetric Forms

Pezzementi

Reinheimer

Pezzementi

1987

Journal of Neurochemistry

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To obtain information about the evolution of acetylcholinesterase (AChE), we undertook a study of the enzyme from the skeletal muscle of the lamprey Petromyzon marinus, a primitive vertebrate. We found that the cholinesterase activity of lamprey muscle is due to AChE, not pseudocholinesterase; the enzyme was inhibited by 1,5-bis(4-allyldimethylammonium phenyl) pentane-3-one (BW284C51), but not by tetramonoisopropyl pyrophosphortetramide (iso-OMPA) or ethopropazine. Also, the enzyme had a high affinity for acetylthiocholine and was inhibited by high concentrations of substrate. A large fraction of the AChE was found to be glycoprotein, since it was precipitated by concanavalin A-agarose. Optimal extraction of AChE was obtained in a high-salt detergent-containing buffer; fractional amounts of enzyme were extracted in buffers lacking salt and/or detergent. These data suggest that globular and asymmetric forms of AChE are present. On sucrose gradients, enzyme that was extracted in high-salt detergent-containing buffer sedimented as a broad peak of activity corresponding to G4; additionally, there was usually a peak corresponding to A12. Sequential extraction of AChE in conjunction with velocity sedimentation resolved minor forms of AChE and revealed that the G1, G2, G4, A4, A8, and A12 forms of AChE could be obtained from the muscle. The identity of the forms was confirmed through high-salt precipitation and collagenase digestion. The asymmetric forms of AChE were precipitated in low ionic strength buffer, and their sedimentation coefficients were shifted to higher values by collagenase digestion.(ABSTRACT TRUNCATED AT 250 WORDS)

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Actions on Insects and Other Invertebrates

Cited by 30 publications

References 190 publications

Anticholinesterase Activity (In the Mediterranean Fruit Fly) and Mouse Toxicity of Some New Organophosphorus Compounds

Anticholinesterase Activity (In the Mediterranean Fruit Fly) and Mouse Toxicity of Some New Organophosphorus Compounds

Mass Spectrometric Enzyme Histochemistry Method Developed for Visualizing In Situ Cholinesterase Activity in Mus musculus and Drosophila melanogaster

Acetylcholinesterase from the Skeletal Muscle of the Lamprey Petromyzon marinus Exists in Globular and Asymmetric Forms

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