Noncholinergic functions of cholinesterases

Balasubramanian, A.S.; Bhanumathy, Cunnigaiper D.

doi:10.1096/fasebj.7.14.8224608

Cited by 71 publications

(39 citation statements)

References 1 publication

(2 reference statements)

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“…For instance, AChE can noncatalytically promote axon and dendritic outgrowth [McKeon et al, 1989;Jones et al, 1995], most likely by modulating neurite-substrate adhesion [Sternfeld et al, 1998]. AChE can also contribute to migration, cellular differentiation, synaptogenesis and survival [Bon et al, 1987;Small, 1990;Kuchler et al, 1991;Balasubramanian and Bhanumathy, 1993;Layer et al, 1993;Massoulie et al, 1993;Schlagger et al, 1993;Feng and Carlson, 1994;Geula et al, 1995;Hutchins et al, 1995;Coleman and Taylor, 1996;, roles which have been proposed for the AChE transiently expressed in GABAergic cortical and other developing neurons [Hallinger et al, 1986;Geula et al, 1995].…”

Section: Discussionmentioning

confidence: 99%

Prenatal Availability of Choline Alters the Development of Acetylcholinesterase in the Rat Hippocampus

Cermák¹,

Blusztajn²,

Meck

et al. 1999

Dev Neurosci

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Choline (Ch) supplementation during embryonic days (ED) 12–17 enhances spatial and temporal memory in adult and aged rats, whereas prenatal Ch deficiency impairs attention performance and accelerates age-related declines in temporal processing. To characterize the neurochemical and neuroanatomical mechanisms that may mediate these behavioral effects in rats, we studied the development [postnatal days (PD) 1, 3, 7, 17, 27, 35, 90, and 26 months postnatally] of acetylcholinesterase (AChE) activity in hippocampus, neocortex and striatum as a function of prenatal Ch availability. We further measured the density of AChE-positive laminae (PD27 and PD90) and interneurons (PD20) in the hippocampus as a function of prenatal Ch availability. During ED11-ED17 pregnant Sprague-Dawley rats received a Ch-deficient, control or Ch-supplemented diet (average Ch intake 0, 1.3 and 4.6 mmol/kg/day, respectively). Prenatal Ch deficiency increased hippocampal AChE activity as compared to control animals in both males and females from the 2nd to 5th week postnatally. Moreover, prenatal Ch supplementation reduced hippocampal AChE activity as compared to control animals over the same developmental period. There was no effect of prenatal Ch status on either cortical or striatal AChE activity at any age measured, and by PD90 the effect of Ch on hippocampal AChE was no longer observed. In order to localize the early changes in hippocampal AChE activity anatomically, frozen coronal brain sections (PD20, PD27, PD90) were stained histochemically for AChE. Consistent with biochemical results, the AChE staining intensity was reduced in PD27 hippocampal laminae in the Ch-supplemented group and increased in the Ch-deficient group compared to control animals. There was no effect of the diet on hippocampal AChE staining intensity on PD90. In addition, the prenatal Ch availability was found to alter the size and density of AChE-positive PD20 interneurons. These results show that prenatal Ch availability has long-term consequences on the development of the hippocampal cholinergic system.

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Section: Discussionmentioning

confidence: 99%

Prenatal Availability of Choline Alters the Development of Acetylcholinesterase in the Rat Hippocampus

Cermák¹,

Blusztajn²,

Meck

et al. 1999

Dev Neurosci

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“…Its low pH optimum (about pH 5) is reminiscent of a previously described subform AAA-2, which was also detected in the rat brain [54]. The deacetylating properties of other AAAs turned out to represent side activities of acetylcholinesterase [6,29,91,92], butyrylcholinesterase [6] or even human serum albumin [83]. It has remained uncertain to what extent non-specific AAAs of vertebrate origin are capable of deacetylating melatonin at all.…”

Section: Melatonin Deacetylationmentioning

confidence: 96%

Melatonin Metabolism in the Central Nervous System

Hardeland¹

2010

112

110

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Abstract:The metabolism of melatonin in the central nervous system is of interest for several reasons. Melatonin enters the brain either via the pineal recess or by uptake from the blood. It has been assumed to be also formed in some brain areas. Neuroprotection by melatonin has been demonstrated in numerous model systems, and various attempts have been undertaken to counteract neurodegeneration by melatonin treatment. Several concurrent pathways lead to different products. Cytochrome P 450 subforms have been demonstrated in the brain. They either demethylate melatonin to Nacetylserotonin, or produce 6-hydroxymelatonin, which is mostly sulfated already in the CNS. Melatonin is deacetylated, at least in pineal gland and retina, to 5-methoxytryptamine. N 1 -acetyl-N 2 -formyl-5-methoxykynuramine is formed by pyrrole-ring cleavage, by myeloperoxidase, indoleamine 2,3-dioxygenase and various non-enzymatic oxidants. Its product, N 1 -acetyl-5-methoxykynuramine, is of interest as a scavenger of reactive oxygen and nitrogen species, mitochondrial modulator, downregulator of cyclooxygenase-2, inhibitor of cyclooxygenase, neuronal and inducible NO synthases. Contrary to other nitrosated aromates, the nitrosated kynuramine metabolite, 3-acetamidomethyl-6-methoxycinnolinone, does not re-donate NO. Various other products are formed from melatonin and its metabolites by interaction with reactive oxygen and nitrogen species. The relative contribution of the various pathways to melatonin catabolism seems to be influenced by microglia activation, oxidative stress and brain levels of melatonin, which may be strongly changed in experiments on neuroprotection. Many of the melatonin metabolites, which may appear in elevated concentrations after melatonin administration, possess biological or pharmacological properties, including N-acetylserotonin, 5-methoxytryptamine and some of its derivatives, and especially the 5-methoxylated kynuramines.

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“…In this respect, it is relevant that AChE also possesses activities besides its pivotal role in the hydrolysis of acetylcholine. 57 Since activation of proteases, especially the caspase cascade, has been shown to be a vital step in the execution of apoptosis, we believe it will be interesting to further investigate how caspases and acetylcholinesterase are related in regulating apoptosis. We believe that further identification of the targets of acetylcholinesterase in apoptotic cells may provide important information for understanding the mechanisms of apoptosis.…”

Section: Of Ache Was Detected By Cytochemical Staining At 0 H (A) 2 mentioning

confidence: 99%

Induction of acetylcholinesterase expression during apoptosis in various cell types

et al. 2002

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Acetylcholinesterase (AChE) plays a key role in terminating neurotransmission at cholinergic synapses. AChE is also found in tissues devoid of cholinergic responses, indicating potential functions beyond neurotransmission. It has been suggested that AChE may participate in development, differentiation, and pathogenic processes such as Alzheimer's disease and tumorigenesis. We examined AChE expression in a number of cell lines upon induction of apoptosis by various stimuli. AChE is induced in all apoptotic cells examined as determined by cytochemical staining, immunological analysis, affinity chromatography purification, and molecular cloning. The AChE protein was found in the cytoplasm at the initiation of apoptosis and then in the nucleus or apoptotic bodies upon commitment to cell death. Sequence analysis revealed that AChE expressed in apoptotic cells is identical to the synapse type AChE. Pharmacological inhibitors of AChE prevented apoptosis. Furthermore, blocking the expression of AChE with antisense inhibited apoptosis. Therefore, our studies demonstrate that AChE is potentially a marker and a regulator of apoptosis.

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Noncholinergic functions of cholinesterases

Cited by 71 publications

References 1 publication

Prenatal Availability of Choline Alters the Development of Acetylcholinesterase in the Rat Hippocampus

Prenatal Availability of Choline Alters the Development of Acetylcholinesterase in the Rat Hippocampus

Melatonin Metabolism in the Central Nervous System

Induction of acetylcholinesterase expression during apoptosis in various cell types

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