mutations in the superoxide dismutase 1, sod1, gene cause familial amyotrophic lateral sclerosis and motor axons in SOD1G93A-Tg mice also show a reduction in ChAT transport from the pre-onset stage, microtubule-dependent release of acetylcholine is significantly impaired by misfolded SOD1 species, overview. Sequestration by misfolded SOD1 species results in inhibition of ChAT transport, which plays a role in amyotrophic lateral sclerosis, overview
in cigarette smokers and patients with chronic obstructive pulmonary disease, acetylcholine activation in lung fibroblasts causes increased cell proliferation involving muscarinic M1, M2, and M3 receptors, and ERK1/2 and NFkappaB pathways, overview
ChAT is the rate-limiting enzyme of generating acetylcholine, which is synthesized in cholinergic neuronal cell bodies. Insulin signaling may play an important part in the activities of cholinergic neurons
peripheral type of choline acetyltransferase-positive nerves participate in the sympathetic cholinergic innervation of eccrine sweat glands. The enzyme also plays a role in cutaneous sensory nerve endings
a mutant enzyme that incorporates four amino acid substitutions from wild type, shows a substantial increase in catalytic efficiency toward L-carnitine
kinetic data indicate that choline acetyltransferase operates by forming an acetylated enzyme as an intermediate in the reversible reaction between acetyl-CoA and choline
synthesis of the neurotransmitter acetylcholine that is essential for the development and neuronal activities of the cholinergic systems involved in many fundamental brain functions
formation of acetylcholine in cholinergic neurons largely depends on both the levels of choline being transported into the cells from the extracellular space and the activity of ChAT, kinetics of choline uptake in the SK-N-SH cells
choline taken up by OCTs or derived from the plasma membrane is also utilized for acetylcholine synthesis in both cholinergic neurons and nonneuronal cholinergic cells, such as lymphocytes
synthesis of the neurotransmitter acetylcholine that is essential for the development and neuronal activities of the cholinergic systems involved in many fundamental brain functions
formation of acetylcholine in cholinergic neurons largely depends on both the levels of choline being transported into the cells from the extracellular space and the activity of ChAT, kinetics of choline uptake in the SK-N-SH cells
choline taken up by OCTs or derived from the plasma membrane is also utilized for acetylcholine synthesis in both cholinergic neurons and nonneuronal cholinergic cells, such as lymphocytes
noncompetitive with respect to choline, IC50: 0.0004 mM, mixed type inhibition with respect to acetyl-CoA, IC50: 0.0025 mM, activity can be recovered using 2,3-dimercapto-propanol
it is proposed that dihydrolipoic acid serves an essential role in the regulation of the activity of the the enzyme and that the ratio of reduced to oxidized lipoic acid in the cell may play an important role in the regulation of the activity of the enzyme
a neural cell adhesion molecule ligand, 65-74% activation at 0.001 mM involving the fibroblast growth factor receptor, activation is inhibited by the FGFR inhibitor, SU5402
it is proposed that dihydrolipoic acid serves an essential role in the regulation of the activity of the the enzyme and that the ratio of reduced to oxidized lipoic acid in the cell may play an important role in the regulation of the activity of the enzyme
i.e. KAP3, is a kinesin-2 subunit responsible for binding to cargos including choline acetyltransferase. Sequestration by misfolded SOD1 species results in inhibition of ChAT transport
lipoic acid and pilocarpine together increase enzyme activity in the hippocampus of healthy and epileptic rats, lipoic acid alone does not alter hippocampal ChAT activity. Lipoic acid protects rats against pilocarpine-induced seizures and eliminates lethality, overview
lipoic acid and pilocarpine together increase enzyme activity in the hippocampus of healthy and epileptic rats, lipoic acid alone does not alter hippocampal ChAT activity. Lipoic acid protects rats against pilocarpine-induced seizures and eliminates lethality, overview
choline acetyltransferase activity is increased in cortex, brainstem and midbrain 6h after LD50 treatment, and the elevated enzyme activity persisted up to 20h after treatment
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0025
Hg2+
Electrophorus electricus;
-
noncompetitive with respect to choline, IC50: 0.0004 mM, mixed type inhibition with respect to acetyl-CoA, IC50: 0.0025 mM, activity can be recovered using 2,3-dimercapto-propanol
pChAT+ nerve fibers are found exclusively in the trigeminal and solitary systems. The ventral portion of the principal sensory nucleus contains many pChAT+ fibers
impaired spatial working memory and altered choline acetyltransferase immunoreactivity and nicotinic receptor binding in rats exposed to intermittent hypoxia during sleep
enzyme-containing neuronal cell bodies in only two regions, the cell islands of the optic lobe medulla and the cortical layer of the posterior olfactory lobule. Immunoreactive fibers and probable nerve terminals are found in the plexiform layer of the deep retina, within the stroma of the optic gland, and the neuropils of the optic lobe, peduncle lobe, and olfactory lobe
enzyme-containing neuronal cell bodies in only two regions, the cell islands of the optic lobe medulla and the cortical layer of the posterior olfactory lobule. Immunoreactive fibers and probable nerve terminals are found in the plexiform layer of the deep retina, within the stroma of the optic gland, and the neuropils of the optic lobe, peduncle lobe, and olfactory lobe
enzyme-containing neuronal cell bodies in only two regions, the cell islands of the optic lobe medulla and the cortical layer of the posterior olfactory lobule. Immunoreactive fibers and probable nerve terminals are found in the plexiform layer of the deep retina, within the stroma of the optic gland, and the neuropils of the optic lobe, peduncle lobe, and olfactory lobe
in both young adult and middle-aged animals, oestradiol treatment initiates immediately after ovariectomy significantly increased ChAT levels in the hippocampus but not in the prefrontal cortex compared to cholesterol control treatment. When oestradiol treatment is initiated 5 months after ovariectomy, it fails to significantly increase ChAT levels in the hippocampus, but does so in the prefrontal cortex
the ganglion neurons possess pChAT, but never cChAT, mRNA and protein. pChAT has enzyme activity enough to supply physiological concentrations of acetylcholine in the ganglion. pChAT contributes both to acetylcholine neurotransmission in physiologically identified cholinergic cells and to functions yet unknown in non-cholinergic neurons
colocalization of nitric oxide synthase and choline acetyltransferase. nNOS/ChAT-positive cells are detected in: the diencephalon (the preoptic and suprachiasmatic nuclei, the habenula, the dorsal thalamus, and the nucleus of the medial longitudinal fasciculus), the mesencephalon (the optic tectum, the mesencephalic portion of the trigeminal nucleus, the oculomotor and trochlear nuclei, and the Edinger-Westphal nucleus) and the rhombencephalon (the secondary gustatory nucleus, the nucleus isthmi, the lateral lemniscus nucleus, the cerebellum, the reticular formation, different nuclei of the octaval column, the motor zone of the vagal lobe, and the trigeminal, facial, abducens, glosso-pharyngeal, vagal, and hypobranchial motor nuclei). Double-labeled cells are also observed in the spinal motor column
ingestion of lower quantity and quality of dietary protein are likely to control the mRNA level and concentration of NGF, and cause a decline in the activity of choline acetyltransferase in the brains of young rats
exposure to enriched environment improves spatial learning performances and enhances cell density but not choline acetyltransferase activity in the hippocampus of ventral subicular-lesioned rats
in both young adult and middle-aged animals, oestradiol treatment initiates immediately after ovariectomy significantly increased ChAT levels in the hippocampus but not in the prefrontal cortex compared to cholesterol control treatment. When oestradiol treatment is initiated 5 months after ovariectomy, it fails to significantly increase ChAT levels in the hippocampus, but does so in the prefrontal cortex
Alzheimer’s disease/galanin+ cells display a significant upregulation in choline acetyltransferase mRNA expression compared to cognitive impairment and Alzheimer’s disease/galanin- cells. Galanin fiber hyperinnervation of cholinergic nucleus basalis neurons upregulates the expression of ChAT
ChAT+/NOS- neurons account for 48% of myenteric neurons and ChAT-/NOS+ neurons accounted for 43%. ChAT+/NOS+ neurons comprised 4% of the total number of neurons. ChAT-/NOS- neurons comprise 5% of all cells
in addition, to the somatomotor neurons and the intermediolateral column, throughout the spinal cord small ChATir cells are found in the central ventral gray but not in the dorsal gray
trigeminal neuron, the majority of pChAT-positive neurons has small to medium-sized cell bodies. More than 90% of substance P (SP)-positive trigeminal cells and about 80% of calcitonin gene-related peptide (CGRP)-positive cells exhibited pChAT-immunoreactivity. pChAT-positive cells form a larger population of neurons than SP-positive or CGRP-positive cells, but they are a different population from calbindin-D28k-positive neurons. pChAT-immunoreactivity is present in a subset of neurons positive for neuronal nitric oxide synthase. pChAT plays roles not only in nociception, but also in other sensory functions such as mechanoreception mediating tactile sensation
enzyme-containing neuronal cell bodies in only two regions, the cell islands of the optic lobe medulla and the cortical layer of the posterior olfactory lobule. Immunoreactive fibers and probable nerve terminals are found in the plexiform layer of the deep retina, within the stroma of the optic gland, and the neuropils of the optic lobe, peduncle lobe, and olfactory lobe
ChAT protein levels are significantly increased in the dark-reared retina compared to those of the control. Light deprivation increases the expression of ChAT, increasing the apparent density of cholinergic neurons in the developing turtle retina
in addition, to the somatomotor neurons and the intermediolateral column, throughout the spinal cord small ChATir cells are found in the central ventral gray but not in the dorsal gray
after axotomy pChAT immunoreactivity is apparent in some brainstem nuclei, such as the dorsal motor nucleus of the vagus nerve, the nucleus ambiguus, and the hypoglossal nucleus, but not in the brainstem neurons of normal rats
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNAs encoding splicing variants cChAT and pChAT, purified from the rat striatum and pterygopalatine ganglion, respectively, expression analysis. Recombinant expression in HEK-293 cells
expression in FR3T3 fibroblasts, SN6 cells and transgenic mice, a 3800-bp 5'flanking segment from the rat ChAT gene promotor directed cell type-specific expression of a reporter gene in cholinergic cells. A 2342-bp segment from the 5' flanking region of the ChAT gene behaves as an enhancer in cholinergic cells but as a repressor in noncholinergic cells in an orientation-independent manner
large-scale expression as His-tag or chitin-binding-domain fusion protein in Escherichia coli, His-tag fusion protein expresses in inclusion bodies at 37°C growth temperature and in soluble form at 20°C, chitin-binding-domain fusion protein expressed at 15°C but not at 37°C
stable expression of the enzyme in NIH-3T3 fibroblasts, expression of ChAT and high-affinity choline transporter CHT1 in NIH-3T3 cells giving NIH3T3ChAT 112-1 cells leading to increased binding of the CHT1 inhibitor hemicholinium-3 and greater choline uptake and acetylcholine synthesis compared to NIH3T3ChAT 103-1 cells, a CHT1-negative control cell line
two fragments of the hChAT gene are used for functional analysis carrying 944 bp (P1) and 4000 bp (P2) of the 5' flanking region in front of the chloramphenicol acetyltransferase (CAT) reporter gene. They are transfected in NG108-15, SN6 and COS-1 cells
the administration of 0.5% gamma-aminobutyric acid in the diet of ovariectomized female rats causes an increase in the activity of choline acetyltransferase in the brain
an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426
an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426
an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426
an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426
an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426
an active site histidine of the enzyme is believed to act as general acid/base catalyst, a comparison of the deduced amino acid sequence of the enzyme from Drosophila, pig, rat and Caenorhabditis elegans reveales three conserved histidines: His268, His393 and His426
the wild-type enzyme is distributed predominantly in cytoplasm (88%), with the remainder (12%) bound to cellular membranes, mutation S440A results in localization of the enzyme entirely in cytoplasm
is described as ChAT-R, the introduction of an Arg at position 514 in rat enzyme is predicted to provide the ionic charge required to interact with, and neutralize, the carboxyl group of carnitine
kinetic as well chemical modification studies have implicated the presence of an active site arginine in enzyme, whose function is to stabilize coenzyme binding, conserved arginines are converted to identify these residues
kinetic as well chemical modification studies have implicated the presence of an active site arginine in enzyme, whose function is to stabilize coenzyme binding, conserved arginines are converted to identify these residues
kinetic as well chemical modification studies have implicated the presence of an active site arginine in enzyme, whose function is to stabilize coenzyme binding, conserved arginines are converted to identify these residues
kinetic as well chemical modification studies have implicated the presence of an active site arginine in enzyme, whose function is to stabilize coenzyme binding, conserved arginines are converted to identify these residues
real-time multiplex PCR technique can be carried out in a single tube and can differentiate between the polymorphic sites of the ChAT gene associated with Alzheimer’s disease
ChAT is selected as a marker of cholinergicneurons. In the CA1 region of hippocampus of mice, several of the insulin signaling-related proteins are co-located with ChAT, and most double immunoreactive positive cells are pyramidal cells
Nelumbo nucifera semen extract improves memory in rats with scopolamine-induced dementia through the induction of choline acetyltransferase expression and inhibition of acetylcholinesterase activity
investigation of three ChAt gene polymorphisms in schizophrenia. Evidence for an influence of a 5' promoter polymorphism, rs1880676A/G, on susceptibility to the disorder among individuals of Basque origin. Evidence for a similar though less significant, influence for a second polymorphism of putative function, rs3810950
a severe case of congenital myasthenia gravis in a Chinese newborn is reported who presents with complete ptosis, severe hypotonia, dysphagia and respiratory insufficiency with recurrent apnea that requires mechanical ventilatory support since birth. The infant has heterozygous mutations in the choline acetyltransferase genes, p.T553N and p.S704P
promoting ChAT activity and acetylcholine release can lead to treatments for neurodegenerative diseases with cholinergic deficits, such as Alzheimer’s disease