Muscular dystrophy alters the processing of light acetylcholinesterase but not butyrylcholinesterase forms in liver ofLama2dy mice

García‐Ayllón, María‐Salud; Campoy, Francisco J.; Vidal, Cecilio J.

doi:10.1002/1097-4547(20001001)62:1<134::aid-jnr14>3.0.co;2-t

Cited by 18 publications

(5 citation statements)

References 48 publications

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“…2B), the almost complete absence of PRiMA mRNA from the liver and the presence in the organ of AChE-T and BuChE mRNAs ( Fig. 3) certainly explain the lack in liver of the PRiMA-linked (amphiphilic) G 4 A AChE T and G 4 A BuChE components and the secretion to blood serum of the PRiMA-devoid (hydrophilic) G 4 H AChE T and G 4 H BuChE species (33,51,56,57).…”

Section: Buche Transcripts Prevail Over Ache Transcripts In the Mousementioning

confidence: 88%

“…Although reports on the down-expression of AChE in cirrhosis (17) and hepatic carcinoma (11) have increased attention toward hepatic AChE, clinicians should be aware of the fact that BuChE prevails over AChE in the mammalian liver, both at the levels of activity (33) and mRNA, as demonstrated by the ;45,000 copies of BuChE mRNA vs. ;250 copies of AChE mRNA, which were determined in the mouse liver (Fig. 3).…”

Section: Buche Transcripts Prevail Over Ache Transcripts In the Mousementioning

confidence: 91%

“…This research was addressed to ascertain whether GPI-bound AChE H localizes to rafts in tissues other than muscle, and whether the targeting of AChE to rafts has a functional role. For this, we took advantage of the abundance of GPI-bound AChE H in mouse liver (33). Conversely, existence of E1e-AChE mRNA that encodes N-AChE variants prompted us to examine their occurrence and translation in the liver and eventual raft recruitment.…”

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confidence: 99%

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Lipid rafts of mouse liver contain nonextended and extended acetylcholinesterase variants along with M3 muscarinic receptors

Montenegro

Cabezas-Herrera²,

Campoy

et al. 2016

FASEB j.

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The observation of acetylcholinesterase (AChE) type H (AChE), which is the predominant AChE variant in visceral organs and immune cells, in lipid rafts of muscle supports functional reasons for the raft targeting of glypiated AChE The search for these reasons revealed that liver AChE activity is mostly confined to rafts and that the liver is able to make N-extended AChE variants and target them to rafts. These results prompted us to test whether AChE and muscarinic receptors existed in the same raft. Isolation of flotillin-2-rich raft fractions by their buoyancy in sucrose gradients, followed by immunoadsorption and matrix-assisted laser desorption ionization-time of flight-mass spectrometry application, gave the following results: 1) most hepatic AChE activity emanates from AChE-H mRNA, and its product, glypiated AChE, accumulates in rafts; 2) N-extended N-AChE readthrough variant, nonglypiated N-AChE, and N-AChE tailed variant were all identified in liver rafts; and 3) M3 AChRs were observed in rafts, and coprecipitation of raft-confined N-AChE and M3 receptors by using anti-M3 antibodies showed that enzyme and receptor reside in the same raft unit. A raft domain that harbors tightly packed muscarinic receptor and AChE may represent a molecular device that, by means of which, the intensity and duration of cholinergic inputs are regulated.-Montenegro, M. F., Cabezas-Herrera, J., Campoy, F. J., Muñoz-Delgado, E., Vidal, C. J. Lipid rafts of mouse liver contain nonextended and extended acetylcholinesterase variants along with M3 muscarinic receptors.

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Section: Buche Transcripts Prevail Over Ache Transcripts In the Mousementioning

confidence: 88%

Section: Buche Transcripts Prevail Over Ache Transcripts In the Mousementioning

confidence: 91%

mentioning

confidence: 99%

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Lipid rafts of mouse liver contain nonextended and extended acetylcholinesterase variants along with M3 muscarinic receptors

Montenegro

Cabezas-Herrera²,

Campoy

et al. 2016

FASEB j.

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“…Increased concentration of AChE lowers ACh level, leading to reduction or absence of its antiinflammatory activity (Das 2012). Additionally, various studies examine a possible role of hepatic AChE on inhibition of circulating ACh, maintenance of cellular signal transduction and stimulation of different types of apoptosis (Gómez et al 2000;Silman and Sussman 2005;Gralewicz 2006;García-Ayllón et al 2012;Zhang and Greenberg 2012). Besides, methionine deprivation stimulates synthesis and release of tumor necrosis factor α (TNFα) and other cytokines, which also contributes to inflammation (McClain et al 2002).…”

Section: Discussionmentioning

confidence: 99%

Methionine-choline deprivation alters liver and brain acetylcholinesterase activity in C57BL6 mice

Vučević

Cerović²,

Mladenović³

et al. 2016

gpb

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Choline and methionine are precursors of acetylcholine, whose hydrolysis is catalyzed by acetylcholinesterase (AChE). Considering the possibility of their common deficiency, we investigated the influence of methionine-choline deprivation on AChE activity in liver and various brain regions (hypothalamus, hippocampus, cerebral cortex and striatum) in mice fed with methionine-choline deficient (MCD) diet. Male C57BL/6 mice (n = 28) were randomly and equally divided into following groups: control group fed with standard diet for 6 weeks (C) and groups fed with MCD diet for 2 weeks (MCD2), 4 weeks (MCD4) and for 6 weeks (MCD6). After the diet, mice were sacrificied and AChE activity in liver and brain was determined spectrophotometrically. Hepatic AChE activity was higher in MCD2, MCD4 and MCD6 compared to control (p < 0.01), with most prominent increase in MCD6. AChE activity in hypothalamus was higher in MCD4 and MCD6 vs. control (p < 0.05 and p < 0.01, respectively), as well as in MCD6 compared to MCD4 (p < 0.01). In hippocampus, increase in AChE activity was shown in MCD6 compared to control (p < 0.01). In cortex and striatum, increase in AChE activity was noted in MCD6 compared to control (p < 0.05). Our findings indicate the increase of hepatic and brain AChE activity in mice caused by methionine-choline deprivation.

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“…El hígado es el principal órgano productor de la enzima butirilcolinesterasa. Este órgano posee la capacidad de sintetizar dos tipos de reservorios de la enzima, uno de la actividad propia del órgano y la segunda, que se depositará en el plasma (Gómez et al, 2000). También, se ha detectado en el estómago, el riñón, pulmón, músculo, cerebro, entre otros tejidos (López et al, 2018).…”

Section: Generalidades De Las Colinesterasasunclassified

Efecto neuroprotector de nicotinamida vía sistema colinérgico en un modelo de obesidad en rata

Cruz

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Excessive intake of saturated fats and simple sugars is associated with learning and memory impairment. This type of diet can produce different physiological changes, such as low-grade systemic inflammation and oxidative stress. The high production of pro-inflammatory cytokines and reactive oxygen species can enter the central nervous system and affect neural homeostasis. In this context, acetylcholine, the main parasympathetic neurotransmitter and inflammation regulator could be affected.Acetylcholine concentrations in organs and tissues depends on its hydrolysis through the activities of acetylcholinesterase and butyrylcholinesterase (AChE and BChE, respectively). Changes in the diet increase their cholinesterases activity by hydrolyzing ACh, contributing to the inflammation process and affecting the synapse, which favors cognitive impairment. The use of vitamins as adjuvants to treat inflammatory diseases is frequent nowadays. Nicotinamide (NAM) is a vitamin that exerts antioxidant and antiinflammatory effects. In this study we evaluated cholinergic activity associated with the antioxidant and anti-inflammatory effect of NAM in a model of diet-induced cognitive deficit. Thirty male Sprague Dawley rats were distributed in 5 groups and subjected to the following treatments: 1) CON (Control); 2) Hypercaloric diet (HC, 18% fat and 40% sucrose); 3) HC-NAM 5 mM; 4) HC-NAM 10 mM; 5) HC-NAM 15 mM for 13 weeks with ad libitum food and water. AChE and BuChE activities, GSH concentrations, thiobarbituric acid reactive substances (TBARS) and pro-inflammatory cytokines were evaluated; as well as memory and spatial learning. The results showed that the hypercaloric diet increased plasma triacylglycerols, interleukin (IL) -6, TBARS and decreased IL-10 levels, it also increased liver and hippocampal TBARS levels, and

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Muscular dystrophy alters the processing of light acetylcholinesterase but not butyrylcholinesterase forms in liver ofLama2dy mice

Cited by 18 publications

References 48 publications

Lipid rafts of mouse liver contain nonextended and extended acetylcholinesterase variants along with M3 muscarinic receptors

Lipid rafts of mouse liver contain nonextended and extended acetylcholinesterase variants along with M3 muscarinic receptors

Methionine-choline deprivation alters liver and brain acetylcholinesterase activity in C57BL6 mice

Efecto neuroprotector de nicotinamida vía sistema colinérgico en un modelo de obesidad en rata

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