Acetylcholinesterase of mangrove oyster Crassostrea rhizophorae: A highly thermostable enzyme with promising features for estuarine biomonitoring

Souza, Paula Rayane de; Souza, Kelma Sirleide de; Assis, Caio Rodrigo Dias; Araújo, Marlyete Chagas de; Silva, Kaline Catiely Campos; Silva, Juliett de Fátima Xavier da; Ferreira, Andreia Cybelle Marques; Silva, Valdir Luna da; Adam, Mônica Lúcia; Carvalho, Luiz Bezerra de; Bezerra, Ranilson de Souza

doi:10.1016/j.aquatox.2018.02.008

Cited by 16 publications

(7 citation statements)

References 62 publications

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“…Fluorinated pesticides can induce pathologies due to inhibition of enzymes like AChE, resulting in cholinergic hyperstimulation caused by accumulation of acetylcholine in the synaptic cleft. De Souza et al (2018) exposed oyster viscera to 0.001-10 mM of DFB and to 0.00025-2.5 mM of novaluron to assess the endogenous AChE activity determining IC20 values of 0.091 mM for novaluron and 1.35 mM for DBF. However, Ki values could not be calculated because of the weak inhibition potentials.…”

Section: Studies Ex Vivo and In Vitro On Fluorinated Organic Compoundsmentioning

confidence: 99%

“…A recent work described use of oyster (Crassostrea rhizophorae) gills and viscera extracts, to assess endogenous AChE activity, as a specific biomarker for toxicity caused by chlorinated organophosphorus pesticides (de Souza et al, 2018). The authors evaluated catalytic efficiency of the extracts in vitro for hydrolysis of acetylcholine, obtaining KM values of 1.32±0.20 mM and 0.43±0.12 mM in gills and viscera, respectively.…”

Section: Studies Ex Vivo and In Vitro On Chlorinated Organic Compoundsmentioning

confidence: 99%

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Enzymatic assays for the assessment of toxic effects of halogenated organic contaminants in water and food. A review

Artabe

Cunha-Silva

Barranco

2020

Food and Chemical Toxicology

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Halogenated organic compounds are a particular group of contaminants consisting of a large number of substances, and of great concern due to their persistence in the environment, potential for bioaccumulation and toxicity. Some of these compounds have been classified as persistent organic pollutants (POPs) under The Stockholm Convention and many toxicity assessments have been conducted on them previously. In this work we provide an overview of enzymatic assays used in these studies to establish toxic effects and dose-response relationships. Studies in vivo and in vitro have been considered with a particular emphasis on the impact of halogenated compounds on the activity of relevant enzymes to the humans and the environment. Most information available in the literature focuses on chlorinated compounds, but brominated and fluorinated molecules are also the target of increasing numbers of studies. The enzymes identified can be classified as enzymes: i) the activities of which are affected by the presence of halogenated organic compounds, and ii) those involved in their metabolisation/detoxification resulting in increased activities. In both cases the halogen substituent seems to have an important role in the effects observed. Finally, the use of these enzymes in biosensing tools for monitoring of halogenated compounds is described.

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Section: Studies Ex Vivo and In Vitro On Fluorinated Organic Compoundsmentioning

confidence: 99%

Section: Studies Ex Vivo and In Vitro On Chlorinated Organic Compoundsmentioning

confidence: 99%

Enzymatic assays for the assessment of toxic effects of halogenated organic contaminants in water and food. A review

Artabe

Cunha-Silva

Barranco

2020

Food and Chemical Toxicology

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“…Extracts from tissues of marine animals such as the eyes of shrimp and oyster gills can be used satisfactorily as models to simulate the biological environment concerning AChE inhibition, given the enzyme abundance in these organs. ,, Figure shows a comparison of the IC 50 values for the inhibition of commercial AChE and AChE extracts from the Crassostrea rhizophorae species. The IC 50 values of the system containing the AChE of Litopenaeus vannamei were 6.41 and 3.54 μM for inhibition with lapatinib and pazopanib, respectively.…”

Section: Resultsmentioning

confidence: 99%

“…vannamei, and gills of mangrove oysters, species C. rhizophorae, following the literature . 20 mg of tissue/mL was homogenized in Tris–HCl buffer at 0.5 mol L –1 (pH 8) and centrifuged at 10,000 g at 277 K for 10 min.…”

Section: Methodsmentioning

confidence: 99%

“…AChE extracts were obtained from the eyes of shrimps, species L. vannamei, and gills of mangrove oysters, species C. rhizophorae, following the literature. 27 20 mg of tissue/mL was homogenized in Tris−HCl buffer at 0.5 mol L −1 (pH 8) and centrifuged at 10,000g at 277 K for 10 min. The extracts were obtained from the supernatant separated by centrifugation and stored under refrigeration at 253 K until analysis.…”

Section: Methodsmentioning

confidence: 99%

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Binding Mechanism between Acetylcholinesterase and Drugs Pazopanib and Lapatinib: Biochemical and Biophysical Studies

Menezes

Assis

Cintra

et al. 2021

ACS Chem. Neurosci.

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Tyrosine kinase inhibitors (TKIs) are antitumor compounds that prevent the phosphorylation of proteins in a biological environment. However, the multitarget performance of TKIs promotes them as possible candidates for drug repositioning. In this work, interaction and inhibition studies through spectroscopic and computational techniques to evaluate the binding effectiveness of lapatinib and pazopanib TKIs to acetylcholinesterase (AChE) are reported. The results indicated potent inhibition at the μM level. The types of inhibition were identified, with pazopanib acting through non-competitive inhibition and lapatinib through acompetitive inhibition. The fluorescence suppression studies indicate a static mechanism for lapatinib−AChE and pazopanib−AChE systems, with a binding constant in the order of 10 5 M −1 . The obtained thermodynamic parameters reveal interactions driven by van der Waals forces and hydrogen bonds in the lapatinib−AChE system (ΔH°and ΔS°< 0). In contrast, the pazopanib−AChE system shows positive ΔH°and ΔS°, characteristic of hydrophobic interactions. The Foster resonance energy transfer study supports the fluorescence studies performed. The 3D fluorescence studies suggest changes in the microenvironment of the tryptophan and tyrosine residues of the protein in contact with lapatinib and pazopanib. The results suggest effective inhibition and moderate interaction of the drugs with AChE, making them interesting for conducting more in-depth repositioning studies as AChE inhibitors.

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Investigation of the effects of some pesticides on carbonic anhydrase isoenzymes

Baltacı

Çıkrıkçı

Gençer

2023

J of Molecular Recognition

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The aim of this study was to investigate the inhibitory effects of some pesticides known to have harmful effects on human health on carbonic anhydrase isoenzymes. Therefore, carbonic anhydrase isoenzymes (hCA I and II) were purified from human erythrocytes. The isoenzymes were purified from human erythrocytes by using an affinity column that has the chemical structure of Sepharose‐4B‐4‐(6‐amino‐hexyloxy)‐benzenesulfonamide. The purity of the isoenzymes was checked by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDSPAGE). It was determined that the pesticides used in this study inhibit hCA I and hCA II isoenzymes at different levels in vitro. It was determined that the strongest inhibitor for the hCA I enzyme was Carbofuran (IC50:6.52 μM; Ki: 3.58 μM) and the weakest one was 1‐Naphtol (IC50:16.55 μM; Ki: 14.4 μM) among these pesticides. It was also found that the strongest inhibitor for the hCA II enzyme was coumatetralil (IC50:5.06 μM; Ki: 1.62 μM) and the weakest one was Dimethachlor (IC50 14.6 μM; Ki: 8.44 μM).

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Acetylcholinesterase of mangrove oyster Crassostrea rhizophorae: A highly thermostable enzyme with promising features for estuarine biomonitoring

Cited by 16 publications

References 62 publications

Enzymatic assays for the assessment of toxic effects of halogenated organic contaminants in water and food. A review

Enzymatic assays for the assessment of toxic effects of halogenated organic contaminants in water and food. A review

Binding Mechanism between Acetylcholinesterase and Drugs Pazopanib and Lapatinib: Biochemical and Biophysical Studies

Investigation of the effects of some pesticides on carbonic anhydrase isoenzymes

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