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Literatura académica sobre el tema "Neuropathy target esterase"

Autor: Grafiati

Publicado: 7 de julio de 2024

Última modificación: 22 de junio de 2025

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Artículos de revistas sobre el tema "Neuropathy target esterase"

GLYNN, Paul. "Neuropathy target esterase." Biochemical Journal 344, no. 3 (1999): 625–31. http://dx.doi.org/10.1042/bj3440625.

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Neuropathy target esterase (NTE) is an integral membrane protein present in all neurons and in some non-neural-cell types of vertebrates. Recent data indicate that NTE is involved in a cell-signalling pathway controlling interactions between neurons and accessory glial cells in the developing nervous system. NTE has serine esterase activity and efficiently catalyses the hydrolysis of phenyl valerate (PV) in vitro, but its physiological substrate is unknown. By sequence analysis NTE has been found to be related neither to the major serine esterase family, which includes acetylcholinesterase, nor to any other known serine hydrolases. NTE comprises at least two functional domains: an N-terminal putative regulatory domain and a C-terminal effector domain which contains the esterase activity and is, in part, conserved in proteins found in bacteria, yeast, nematodes and insects. NTE's effector domain contains three predicted transmembrane segments, and the active-site serine residue lies at the centre of one of these segments. The isolated recombinant domain shows PV hydrolase activity only when incorporated into phospholipid liposomes. NTE's esterase activity appears to be largely redundant in adult vertebrates, but organophosphates which react with NTE in vivo initiate unknown events which lead, after a delay of 1-3 weeks, to a neuropathy with degeneration of long axons. These neuropathic organophosphates leave a negatively charged group covalently attached to the active-site serine residue, and it is suggested that this may cause a toxic gain of function in NTE.

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GLYNN, Paul. "Neuropathy target esterase." Biochemical Journal 344, no. 3 (1999): 625. http://dx.doi.org/10.1042/0264-6021:3440625.

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Hou, Wei-Yuan, Ding-Xin Long, and Yi-Jun Wu. "Effect of Inhibition of Neuropathy Target Esterase in Mouse Nervous Tissues In Vitro on Phosphatidylcholine and Lysophosphatidylcholine Homeostasis." International Journal of Toxicology 28, no. 5 (2009): 417–24. http://dx.doi.org/10.1177/1091581809340704.

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Neuropathy target esterase has been shown to be a lysophospholipase in mouse. The authors investigate the effect of neuropathy target esterase inhibition in mouse nervous tissues in vitro on the homeostasis of phosphatidylcholine and lysophosphatidylcholine by treating the homogenates with tri-ortho-cresyl phosphate, paraoxon, paraoxon plus mipafox, and phenylmethylsulfonyl fluoride. The activity of neuropathy target esterase is significantly inhibited by phenylmethylsulfonyl fluoride and paraoxon plus mipafox but not by paraoxon alone. Tri-ortho-cresyl phosphate slightly but significantly inhibits neuropathy target esterase activity in brain. The levels of phosphatidylcholine and lysophosphatidylcholine in all 3 nervous tissues are not obviously altered after treatment with tri-ortho-cresyl phosphate, paraoxon, or paraoxon plus mipafox. However, phosphatidylcholine and lysophosphatidylcholine levels are clearly enhanced by phenylmethylsulfonyl fluoride. It is concluded that inhibition of neuropathy target esterase in mouse nervous tissues is not enough to disrupt the homeostasis of phosphatidylcholine and lysophosphatidylcholine and that the upregulation by phenylmethylsulfonyl fluoride may be the consequence of combined inhibition of neuropathy target esterase and other phospholipases.

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Glynn, Paul. "Axonal Degeneration and Neuropathy Target Esterase." Archives of Industrial Hygiene and Toxicology 58, no. 3 (2007): 355–58. http://dx.doi.org/10.2478/v10004-007-0029-z.

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Axonal Degeneration and Neuropathy Target EsteraseThis brief review summarises recent observations which suggest a possible mechanism for organophosphate-induced delayed neuropathy (OPIDN). Neuropathy target esterase (NTE) has been shown to deacylate endoplasmic reticulum (ER) membrane phosphatidylcholine (PtdCho). Raised levels of PtdCho are present in the brains of swiss cheese/NTE mutant Drosophila together with abnormal membrane structures, axonal and dendritic degeneration and neural cell loss. Similar vacuolated pathology is found in the brains of mice with brain-specific deletion of the NTE gene and, in old age, these mice show clinical and histopathological features of neuropathy resembling those in wild-type mice chronically dosed with tri-ortho-cresylphosphate. It is suggested that OPIDN results from the loss of NTE's phospholipase activity which in turn causes ER malfunction and perturbation of axonal transport and glial-axonal interactions.

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Lush, Michael, David Read, and Paul Glynn. "Molecular cloning of neuropathy target esterase." Toxicology Letters 88 (October 1996): 27. http://dx.doi.org/10.1016/s0378-4274(96)80098-1.

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Glynn, Paul. "Neurodegeneration involving neuropathy target esterase (NTE)." Toxicology Letters 164 (September 2006): S9. http://dx.doi.org/10.1016/j.toxlet.2006.06.023.

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Glynn, Paul. "Neuropathy target esterase and phospholipid deacylation." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1736, no. 2 (2005): 87–93. http://dx.doi.org/10.1016/j.bbalip.2005.08.002.

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Bertoncin, Daniela, Alessandra Russolo, Stefano Caroldi, and Marcello Lotti. "Neuropathy Target Esterase in Human Lymphocytes." Archives of Environmental Health: An International Journal 40, no. 3 (1985): 139–44. http://dx.doi.org/10.1080/00039896.1985.10545905.

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Thomas, Thomas C., András Székács, Bruce D. Hammock, Barry W. Wilson, and Mark G. McNamee. "Affinity chromatography of neuropathy target esterase." Chemico-Biological Interactions 87, no. 1-3 (1993): 347–60. http://dx.doi.org/10.1016/0009-2797(93)90063-5.

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Seifert, Josef. "A Tentative Mechanism of Solubilization of Neuropathy Target Esterase from Chicken Embryo Brain by Phospholipase A2." Scientific World JOURNAL 8 (2008): 346–49. http://dx.doi.org/10.1100/tsw.2008.51.

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The neuropathy target esterase is a membrane-bound enzyme linked to organophosphate-induced distal neuropathy. Here we report a tentative mechanism of its solubilization from chicken embryo brains by using phospholipase A2. The enzyme was released from brain membranes after degradation of their structural phospholipids initiated by phospholipase A2. L-α-lysophosphatidylcholine, tested as a representative product of phospholipid hydrolysis, was identified as a new efficient detergent for solubilization of the neuropathy target esterase.

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Tesis sobre el tema "Neuropathy target esterase"

Lush, Michael John. "Molecular cloning of neuropathy target esterase." Thesis, University of Leicester, 1998. http://hdl.handle.net/2381/29627.

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A single ingestion of certain organophosphorus esters (OPs) can cause a syndrome known as Organophosphate Induced Delayed Polyneuropathy (OPIDP), a paralysing neuropathy with degeneration of long axons, developing after a latent period of approximately one to three weeks. The primary target of these OPs has been shown to be a 155kDa neural protein designated Neuropathy Target Esterase (NTE), and the toxic effects apparently due to the covalent inhibition and subsequent secondary modification of this protein. Recently NTE has been purified to apparent homogeneity using a novel biotinylated OP and sufficient pure protein was produced for limited problem sequencing. The aim of this project was to clone NTE cDNA using peptide sequence data. Initially, these sequences were used to design degenerate oligonucleotide primers for amplifying sections of brain cDNA by polymerase chain reaction (PCR). These approaches were unsuccessful. Subsequently, a database searching with the peptide sequences identified a number of Expressed Sequence Tags (EST)s; these could be aligned to form an initial contig of 2.2kbp which encoded the 3' end of NTE cDNA. The 5' end of NTE cDNA, comprising a further 2.2kbp, was obtained by PCR-based technique. The final 4.4kbp contig encoded a 1327 residue polypeptide predicted to have a molecular mass of 146kDa and at least one transmembrane domain. A novel serine esterase domain of approximately 200 residues was present near the C-terminus. NTE is unrelated to any known serine hydrolases but homologous proteins are predicted to be present in diverse prokaryotic and eukaryotic organisms. The homologue in Drosophila is associated with the swisscheese phenotype, an age-dependent neurodegeneration of the brain. NTE was also mapped to chromosome 19p 13.3 between markers D19216 and the D19S413 (using the UniGene database) and an OMIM search reveals that this is near the locus of cerebellar ataxia (Cayman type).

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Rezaie-Moazen, Nima. "Characterisation of neuropathy target esterase in mammalian cells." Thesis, University of Leicester, 2005. http://hdl.handle.net/2381/30775.

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The present study found that NTE's catalytic activity is not regulated by cAMP. Purification of the R domain could not be achieved as the recombinant polypeptide is essentially insoluble and consequently, direct cAMP binding could not be attempted. The reduction of NTE activity in HeLa cells caused inhibition of GroPCho production without altering PtdCho levels. Conversely, the inducible overexpression of NTE in a stable HeLa cell line resulted in increased GroPCho production also without altering PtdCho levels. Treatment of HeLa cells with ether-linked lipids caused an apparent inhibition of PtdCho synthesis followed by a time- and concentration-dependent cytotoxicity that was not altered by the inducible overexpression of NTE. Several mouse tissues were screened and the highest NTE expression was found in kidney tubular epithelial cells. Tubular epithelial cells from NTE heterozygous (HZ) mutant mice demonstrated the same GroPCho and phospholipids levels as wild-type cells, despite a 40% lower NTE PV hydrolase activity. The NTE HZ cells had 65% the CDP-choline levels of wild-type cells suggesting a down-regulation of PtdCho synthesis. Greater reduction of NTE activity by treating wild-type tubular epithelial cells with mipafox resulted in a 90% reduction in GroPCho production also accompanied by a down-regulation of PtdCho synthesis. In conclusion, changes in NTE activity, in both cell types, are compensated by corresponding changes in PtdCho synthesis to maintain phospholipids homeostasis.

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Zaccheo, Oliver. "Analysis of the yeast homologue of neuropathy target esterase." Thesis, University of Leicester, 2003. http://hdl.handle.net/2381/30772.

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Neuropathy Target Esterase (NTE) is an essential protein implicated in mammalian neural development and was first identified as the target for those organophosphates (OPs) that cause a delayed neuropathy. NTE has esterase activity, allowing it to hydrolyse the artificial substrate phenyl valerate in vitro: this can be followed in a simple assay. OPs inhibit this activity by reacting with the essential active site serine of NTE. Recent evidence suggests the physiological substrate of NTE to be a lysophospholipid. Previous work has shown that a region of 489 amino acids towards the C-terminal of NTE forms a domain that is sufficient for catalysis. The N-terminal portion of NTE contains regions that show similarity to cAMP-binding domains. These may contribute a regulatory role but have yet to be proved functional. On the basis of sequence data, NTE belongs to a family of proteins whose members are found in organisms ranging from bacteria to man. The previously uncharacterised protein Yml059c of the baker's yeast Saccharomyces cerevisiae belongs to the NTE family of proteins, displaying 58% similarity and 38% identity to NTE over the catalytic domain (NTE residues 727-1216) and also possessing a putative cAMP-binding motif. This study has shown that YML059c is not essential for cell viability deletion or overexpression of YML059c failed to cause any obvious phenotype. Visualisation by green fluorescent protein tagging revealed the protein to be associated with an undetermined intracellular organelle. Experiments described here show that Yml059c possesses a similar biochemical activity to mammalian NTE. Like NTE, it was able to hydrolyse phenyl valerate in an organophosphate-sensitive manner and had lysophospholipase activity. The catalytic activity of Yml059c was also dependent upon a serine residue, in an equivalent location to that of NTE's active site. In addition, Yml059c appeared able to bind radioactively labelled cAMP, suggesting a possible mechanism whereby the catalytic activity of this family of proteins may indeed be regulated by cAMP. The tentative conclusion can be drawn that Yml059c performs a similar cellular role in yeast as NTE does in mammals.

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Atkins, Jane. "Biochemical characterisation of the catalytic domain of neuropathy target esterase." Thesis, University of Leicester, 2000. http://hdl.handle.net/2381/29643.

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Neuropathy target esterase (NTE) is an integral membrane protein found predominantly in neurones. Covalent modification of NTE's active site serine, by certain organophosphates (OPs), results in a neurodegenerative syndrome. NTE's physiological substrate is unknown and its catalytic activity does not seem to be vital in the adult animal. The enzyme domain of human NTE (residues 727-1216), called NEST, was expressed in E. coli and reacted with a carboxyl ester substrate and OP inhibitors the same as native NTE. During purification catalytic activity was lost, but was restored by reconstitution into the liposomes. Site-directed mutagenesis revealed that S966, D960 and D1086 were critical for catalysis. Mutation of two histidines, H860 and H885, also resulted in a loss of activity. Reacting NEST with [3H]diisopropylfluorophosphate, confirmed S966 as the active site serine and showed that an isopropyl group is transferred to an aspartate residue. Standard hydropathy analysis predicts no membrane-spanning helices in NEST; however, biochemical evidence indicated that NEST is an integral membrane protein. TMpred analysis, on the other hand, predicts three transmembrane helices (TM2-4), with S966 at the centre of TM4. For S966 to be located within the membrane, TM4 would need to line the lumen of an aqueous pore to allow access of water for catalysis. Patch clamp studies on NEST-containing giant liposomes indicated that NEST forms a pore in vitro, while other experiments demonstrated that NEST monomers are catalytically active: this raises the possibility that NEST forms a -barrel structure in the membrane.

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Meredith, C. "Biochemical studies on neuropathy target esterase and its role in the initiation of delayed neuropathy by some organophosphorus esters." Thesis, University of Cambridge, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.373779.

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Emerick, Guilherme Luz [UNESP]. "Avaliação de neurotoxicidade de formas enantioméricas de praguicidas organifosforados: estudos in vitro, in vivo e de neuroproteção." Universidade Estadual Paulista (UNESP), 2012. http://hdl.handle.net/11449/106391.

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Made available in DSpace on 2014-06-11T19:35:39Z (GMT). No. of bitstreams: 0 Previous issue date: 2012-03-02Bitstream added on 2014-06-13T20:07:10Z : No. of bitstreams: 1 emerick_gl_dr_arafcf.pdf: 6421431 bytes, checksum: 0afb014cdc72c52072c05813f940629d (MD5) Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Universidade Estadual Paulista (UNESP) Clinicamente, os sintomas da intoxicação por organofosforados (OPs) são divididos em quatro categorias: síndrome colinérgica, síndrome intermediária, transtornos neuropsiquiátricos crônicos induzidos por OPs e neuropatia retardada induzida por OPs (NRIOP). Há estudos que comprovam a ocorrência de casos de NRIOP em seres humanos após intoxicação por metamidofós, porém existe grande dificuldade de estudar esta neuropatia no modelo experimental (galinha), devido à forte crise colinérgica que ocorre após a inibição da acetilcolinesterase (AChE). Uma possível explicação para tal diferença de efeito entre a espécie humana e a galinha é o fato de que os OPs possuem centros assimétricos e, assim sendo, se apresentam sob formas enantioméricas que podem apresentar diferenças de inibição da AChE e da esterase susceptível à neuropatia (ESNp). Assim, o objetivo deste trabalho foi avaliar, em sangue de galinhas e de seres humanos, em cérebro de galinhas (in vitro e in vivo) e em células da linhagem SH-SY5Y de neuroblastoma humano, a neurotoxicidade de formas enantioméricas de compostos organofosforados utilizados como praguicidas, tendo o metamidofós como protótipo e utilizando a AChE, butirilcolinesterase (BChE), ESNp e a calpaína como biomarcadores. Inicialmente, foi feita a separação dos enantiômeros do metamidofós utilizando a técnica de cromatografia líquida de alta eficiência (CLAE) com emprego de fases estacionárias quirais de polissacarídeos, onde se obteve resolução de até 1,56 para os enantiômeros avaliados. A forma (+)-metamidofós apresentou maior toxicidade in vitro para a BChE em galinhas e para ESNp... Clinically, the symptoms of organophosphorus (OP) poisoning are divided into four categories: acute cholinergic syndrome, intermediate syndrome, chronic organophosphorus-induced neuropsychiatric disorders (COPIND) and organophosphorus-induced delayed neuropathy (OPIDN). There are studies that prove the occurrence of OPIDN in humans after methamidophos poisoning, but there is great difficulty in studying this neuropathy in the experimental model (hen), due to strong cholinergic crisis that occurs after inhibition of acetylcholinesterase (AChE). One possible explanation for this difference in effect between humans and hens is the fact that the OPs have asymmetric centers and therefore, are presented as enantiomeric forms that may exhibit differences in inhibition of AChE and neuropathy target esterase (NTE). Thus, the objective of this study was to evaluate, in the blood of hens and humans, in the brains of chickens (in vitro and in vivo) and in the SH-SY5Y human neuroblastoma cells, the neurotoxicity of enantiomeric forms of OPs used as pesticides, having methamidophos as the prototype and using AChE, butyrylcholinesterase (BChE), NTE and calpain as biomarkers. Initially, the complete separation of the methamidophos enantiomers was obtained applying the technique of high performance liquid chromatography (HPLC) and using polysaccharide chiral stationary phases. A maximum resolution of 1.56 was gotten for the enantiomers evaluated. The form (+)-methamidophos presented higher in vitro toxicity than that of the (-)-methamidophos for BChE of hens and NTE of hens and humans... (Complete abstract click electronic access below)

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Emerick, Guilherme Luz. "Avaliação de neurotoxicidade de formas enantioméricas de praguicidas organifosforados : estudos in vitro, in vivo e de neuroproteção /." Araraquara : [s.n.], 2012. http://hdl.handle.net/11449/106391.

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Orientador: Georgino Honorato de Oliveira Coorientador: Regina Vincenzi Oliveira Banca: Maria Palmira Daflon Gremião Banca: Antonio Cardozo dos Santos Banca: Rosângela Gonçalves Peccinini Banca: Silvana Aparecida Calafatti Resumo: Clinicamente, os sintomas da intoxicação por organofosforados (OPs) são divididos em quatro categorias: síndrome colinérgica, síndrome intermediária, transtornos neuropsiquiátricos crônicos induzidos por OPs e neuropatia retardada induzida por OPs (NRIOP). Há estudos que comprovam a ocorrência de casos de NRIOP em seres humanos após intoxicação por metamidofós, porém existe grande dificuldade de estudar esta neuropatia no modelo experimental (galinha), devido à forte crise colinérgica que ocorre após a inibição da acetilcolinesterase (AChE). Uma possível explicação para tal diferença de efeito entre a espécie humana e a galinha é o fato de que os OPs possuem centros assimétricos e, assim sendo, se apresentam sob formas enantioméricas que podem apresentar diferenças de inibição da AChE e da esterase susceptível à neuropatia (ESNp). Assim, o objetivo deste trabalho foi avaliar, em sangue de galinhas e de seres humanos, em cérebro de galinhas (in vitro e in vivo) e em células da linhagem SH-SY5Y de neuroblastoma humano, a neurotoxicidade de formas enantioméricas de compostos organofosforados utilizados como praguicidas, tendo o metamidofós como protótipo e utilizando a AChE, butirilcolinesterase (BChE), ESNp e a calpaína como biomarcadores. Inicialmente, foi feita a separação dos enantiômeros do metamidofós utilizando a técnica de cromatografia líquida de alta eficiência (CLAE) com emprego de fases estacionárias quirais de polissacarídeos, onde se obteve resolução de até 1,56 para os enantiômeros avaliados. A forma (+)-metamidofós apresentou maior toxicidade in vitro para a BChE em galinhas e para ESNp... (Resumo completo, clicar acesso eletrônico abaixo) Abstract: Clinically, the symptoms of organophosphorus (OP) poisoning are divided into four categories: acute cholinergic syndrome, intermediate syndrome, chronic organophosphorus-induced neuropsychiatric disorders (COPIND) and organophosphorus-induced delayed neuropathy (OPIDN). There are studies that prove the occurrence of OPIDN in humans after methamidophos poisoning, but there is great difficulty in studying this neuropathy in the experimental model (hen), due to strong cholinergic crisis that occurs after inhibition of acetylcholinesterase (AChE). One possible explanation for this difference in effect between humans and hens is the fact that the OPs have asymmetric centers and therefore, are presented as enantiomeric forms that may exhibit differences in inhibition of AChE and neuropathy target esterase (NTE). Thus, the objective of this study was to evaluate, in the blood of hens and humans, in the brains of chickens (in vitro and in vivo) and in the SH-SY5Y human neuroblastoma cells, the neurotoxicity of enantiomeric forms of OPs used as pesticides, having methamidophos as the prototype and using AChE, butyrylcholinesterase (BChE), NTE and calpain as biomarkers. Initially, the complete separation of the methamidophos enantiomers was obtained applying the technique of high performance liquid chromatography (HPLC) and using polysaccharide chiral stationary phases. A maximum resolution of 1.56 was gotten for the enantiomers evaluated. The form (+)-methamidophos presented higher in vitro toxicity than that of the (-)-methamidophos for BChE of hens and NTE of hens and humans... (Complete abstract click electronic access below) Doutor

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Mercé, Théo. "High-throughput zebrafish larval locomotion assays of neuronal and muscular functions : Application to organophosphorus toxicity and antid." Electronic Thesis or Diss., Bordeaux, 2024. http://www.theses.fr/2024BORD0011.

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La prévalence croissante des contaminants chimiques pose d'importants problèmes en matière de santé publique, nécessitant des méthodologies efficaces pour l'évaluation des risques toxicologiques. Un travail initial a été réalisé pour optimiser une nouvelle approche méthodologique (NAM) utilisant des éleuthéroembryons de poisson-zèbre, appelée electric field pulse motor response test (EFPMRT). La méthode vise à effectuer un criblage à haut débit des molécules chimiques induisant des défauts des capacités motrices et du contrôle postural. La robustesse, la reproductibilité, la productivité et la transférabilité de l'EFPMRT ont été améliorées en développant un nouvel outil logiciel, DanioTracker, effectuant l'analyse automatisée de points finaux liés au comportement locomoteur induit par la stimulation électrique. Ensuite, à l'aide d'une batterie de tests, la neurotoxicité induite par des composés organophosphorés (OP) et leurs métabolites a été évaluée. Les perturbations comportementales ont été évaluées en utilisant l'EFPMRT et un test neurocomportemental complémentaire dépendant des fonctions sensorielles, le visual motor response test (VMRT). La contribution de l'inhibition de l'acétylcholinestérase (AChE) et de la neuropathy target esterase (NTE) aux perturbations comportementales a été testée. Le chlorpyrifos, le parathion et le tri-ortho-crésyl-phosphate ont perturbé les fonctions intégratives de contrôle de la nage de manière quantitativement distincte et ont réduit les capacités neuromusculaires des éleuthéroembryons. Leurs métabolites respectifs, le chlorpyrifos-oxon, le paraoxon et le cresyl-saligénine-phosphate, ont intégralement inhibé l'AChE, induisant ainsi un syndrome cholinergique. Une étude comparative de l'efficacité d'un antidote réactivateur de l'AChE, le pralidoxime (2-PAM), pour atténuer certains effets toxiques, a été effectuée. L'antidote a induit une récupération face aux syndromes cholinergiques associés à l'exposition aux métabolites. De façon remarquable, le 2-PAM a également partiellement restauré les hyperactivités induites par les composés parents de manière vraisemblablement indépendante des activités AChE et NTE. Toutefois, il n'a pas restauré les dysfonctionnements neuromusculaires induits par le parathion ou le tri-ortho-crésyl-phosphate. Ceci suggère l’existence d’un ou plusieurs modes d'action (MOA) OP-spécifiques inconnus, associés aux composés parents mais pas aux métabolites correspondants, dont certains sont récupérables par le 2-PAM. Dans l'ensemble, ce travail offre une NAM robuste et transférable qui contribue à une stratégie d'évaluation globale des risques chimiques. Il révèle également des MOA alternatifs potentiels pour les OP sélectionnés, suggérant la nécessité de poursuivre les recherches sur les métabolites dans le cadre réglementaire, et contribue à la compréhension et à la prévention des troubles neurocomportementaux induits par les expositions environnementales seules ou en mixtures The growing prevalence of chemical contaminants poses major public health concerns, necessitating efficient methodologies for toxicological risk assessment. An initial work was carried out to optimize a new approach methodology (NAM) using zebrafish pre-feeding larvae, called the electric field pulse (EFP) motor response test (EFPMRT). The method aims to perform a high-throughput screening of chemicals inducing motor capabilities and postural control defects. The robustness, reproducibility, productivity, and transferability of EFPMRT were enhanced by developing a novel software tool, DanioTracker, performing the automated analysis of endpoints linked to EFP-induced locomotor behavior. Then, using a battery of tests, the neurotoxicity induced by organophosphorus (OPs) compounds and their metabolites was assessed. Behavioral disruptions were evaluated using EFPMRT and a complementary sensory-dependent neurobehavioral test, the visual motor response test (VMRT). Contributions of acetylcholinesterase (AChE) and neuropathy target esterase (NTE) inhibition to behavioral disruptions were tested. Chlorpyrifos, parathion and tri-ortho-cresyl-phosphate disturbed integrative swimming control functions in quantitatively distinct manners and decreased the neuromuscular capacities of pre-feeding larvae. Their respective metabolites chlorpyrifos-oxon, paraoxon and cresyl-saligenin-phosphate fully inhibited AChE, thus inducing a cholinergic syndrome. Comparative study of the antidotal efficacy of an AChE reactivator, pralidoxime, in mitigating some toxic effects was performed. The antidote induced a recovery of the cholinergic syndromes associated with metabolites exposure. Strikingly, pralidoxime (2-PAM) also partially restored hyperactivities induced by parent compounds apparently independently of the activities of AChE and NTE. However, it did not restore neuromuscular dysfunctions induced by parathion or tri-ortho-cresyl phosphate. This suggests the existence of one or more unknown OP-specific multiple modes of action (MOAs) associated with parent compound but not corresponding metabolites, of which some are restorable by 2-PAM. Overall, this work offers a robust, transferable NAM that contributes to a comprehensive chemical risk assessment strategy. It also uncovers potential alternative MOA for selected OPs, suggesting the need for further research on metabolites within regulatory frameworks, and contributes to understanding and preventing neurobehavioral disorders induced by environmental exposures alone or in mixtures

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Libros sobre el tema "Neuropathy target esterase"

Ehrich, Marion. Relationship of neuropathy target esterase inhibition to neuropathology and ataxia in hens given organophosphorus esters. Environmental Protection Agency], 1993.

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Capítulos de libros sobre el tema "Neuropathy target esterase"

Wu, Yi-Jun, and Ping-An Chang. "Molecular Toxicology of Neuropathy Target Esterase." In Anticholinesterase Pesticides. John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9780470640500.ch9.

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Lush, Michael, David Read, and Paul Glynn. "Molecular Cloning of Neuropathy Target Esterase." In Archives of Toxicology. Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-60682-3_39.

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Lotti, Marcello. "Neuropathy Target Esterase in Blood Lymphocytes." In Biological Monitoring for Pesticide Exposure. American Chemical Society, 1988. http://dx.doi.org/10.1021/bk-1988-0382.ch009.

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Glynn, Paul. "Neuropathy Target Esterase (NTE): Molecular Characterisation and Cellular Localisation." In Archives of Toxicology. Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-60682-3_30.

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Mackay, C. E., B. D. Hammock, and B. W. Wilson. "Identification of a 155 kDa Fraction that Possesses Neuropathy Target Esterase Activity." In Enzymes of the Cholinesterase Family. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4899-1051-6_74.

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Johnson, Martin K., and Paul Glynn. "Neuropathy Target Esterase." In Handbook of Pesticide Toxicology. Elsevier, 2001. http://dx.doi.org/10.1016/b978-012426260-7.50050-1.

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Wijeyesakere, Sanjeeva J., and Rudy J. Richardson. "Neuropathy Target Esterase." In Hayes' Handbook of Pesticide Toxicology. Elsevier, 2010. http://dx.doi.org/10.1016/b978-0-12-374367-1.00067-7.

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"NTE (neuropathy target esterase)." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics. Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_11590.

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Srivastava, Devesh, Neeraj Kohli, Rudy J., Robert M., and Ilsoon Lee. "Neuropathy Target Esterase Biosensor." In Intelligent and Biosensors. InTech, 2010. http://dx.doi.org/10.5772/7156.

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Johnson, Martin K. "Molecular events in delayed neuropathy: experimental aspects of neuropathy target esterase." In Clinical and Experimental Toxicology of Organophosphates and Carbamates. Elsevier, 1992. http://dx.doi.org/10.1016/b978-0-7506-0271-6.50016-4.

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