Information on EC 2.3.1.6 - choline O-acetyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
2.3.1.6
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RECOMMENDED NAME
GeneOntology No.
choline O-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + choline = CoA + O-acetylcholine
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glycerophospholipid metabolism
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:choline O-acetyltransferase
Propanoyl-CoA can act, more slowly, in place of acetyl-CoA.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-78-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
nematode
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
var. ma-yuen
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
zebrafish mutant line, bajan, in which compromised motility and fatigue result from a point mutation in the gene coding choline acetyltransferase
Uniprot
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
colocalization of calbindin-D28k and calretinin with ChAT
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
snail
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
horseshoe crab
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Lepidoptera: Spingidae
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Manually annotated by BRENDA team
Musa domestica
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Oenanthe siolonifera
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Andrews
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Manually annotated by BRENDA team
Andrews
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Manually annotated by BRENDA team
cockroach
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
3 enzyme forms
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-
Manually annotated by BRENDA team
Red.
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Manually annotated by BRENDA team
Red.
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-
Manually annotated by BRENDA team
Wolf.
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Manually annotated by BRENDA team
Wolf.
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Manually annotated by BRENDA team
var. ansu
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Manually annotated by BRENDA team
bulb-mite
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Manually annotated by BRENDA team
Michx
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Manually annotated by BRENDA team
Michx
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Manually annotated by BRENDA team
Sasamorpha purpurascens
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Manually annotated by BRENDA team
locust
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Torpedo californica
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
ChAT/calretinin colocalization
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + carnitine
acetylcarnitine + CoA
show the reaction diagram
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
acetyl-CoA + choline
CoA + O-acetylcholine
show the reaction diagram
additional information
?
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-
pilocarpine-induced seizures produce alterations on choline acetyltransferase and acetylcholinesterase activities and deficit memory in rats, overview
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
acetyl-CoA + choline
CoA + O-acetylcholine
show the reaction diagram
additional information
?
-
-
pilocarpine-induced seizures produce alterations on choline acetyltransferase and acetylcholinesterase activities and deficit memory in rats, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-Bromoacetonyltrimethylammonium bromide
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3-Bromoacetonyltrimethylammonium ion
3-Chloro-4-stilbazole
3-Trimethylammoniomethylcatechol
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4-(1-Naphthylvinyl)pyridine
5,5'-dithiobis(2-nitrobenzoate)
Acetylaminocholine
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Acetylcholine
Acyloylcholine
amyloid beta peptide
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the aggregated form of A-beta 25-35 decreased significantly enzyme activity only in the aged striatum
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arachidonic acid
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bromo-acetylcholine
Bromoacetyl-S-CoA
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bromoacetylcholine
Catecholine
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CdCl2
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Chloroacetylcholine
Chlorocholine
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choline
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Choline mustard aziridinium salt
coenzyme A
CuSO4
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dexamethasone
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Diethylaminoethanol
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diethyldicarbonate
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domoic acid
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ethylenimine
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Flubenzimine
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i.e. N-[3-phenyl-4,5-bis[(trifluoromethyl)immino]-2-thiazolidinylidene]benzenamine
glutamate
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Hg2+
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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
HgCl2
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iodoacetamide
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iodoacetate
kainate
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N,N-Dimethylaminoethyl acrylate
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N,N-Dimethylaminoethyl bromoacetate
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N,N-Dimethylaminoethyl chloroacetate
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N-ethylmaleimide
N-Hexamethylene-4-(1-naphthylvinyl)pyridinium-6-trimethylammonium ion
N-Methyl-4-(1-naphthylvinyl)pyridine
nerve growth factor
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nerve growth factor, under specific development conditions, leads to a paradoxical down-regulation of the enzyme
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ocadaic acid
p-chloromercuribenzoate
phenylacetate
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phenylacetyl-CoA
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phenylbutyrate
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Phenylmethanesulfonylfluoride
pilocarpine
quisqualate
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Reactive blue 2
Styrylpyridinium salts
thioctic acid
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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
veratridine
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Zinc acetate
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[2-[3-(2-Ammonioethoxy)-benzoyl]ethyl]trimethylammonium bromide
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additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
C3d
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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
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choline
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extracellular choline increases acetylcholine contents in the cell
Creatinine-HCl
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Dihydrolipoic acid
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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
ethanolic extract of Allium tuberosum
Guanidine-HCl
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high-affinity choline transporter
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i.e. CHT1, plays a key role in acetylcholine synthesis and choline uptake, CHT1 inhibition also inhibits acetylcholine formation, overview
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kinesin-associated protein 3
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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
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LiCl
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lipoic acid
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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
Na2HPO4
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Na2SO4
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NaBr
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NGFI-A
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NGF activates transcriptional factors which influence the promotor region of the enzyme
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NGFI-C
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NGF activates transcriptional factors which influence the promotor region of the enzyme
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NH4Cl
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okadaic acid
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increases the activity of water-soluble and nonionically membrane-bound enzyme
pilocarpine
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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
sarin
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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
Sodium acetate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00201 - 5
acetyl-CoA
0.0004 - 2.7
Acetylcholine
4.8 - 100
carnitine
0.192 - 128
choline
0.00025 - 0.04
CoA
additional information
additional information
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15
3-trimethylammoniomethyl catechol
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25
Catecholine
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0.008
coenzyme A
0.0005
Hg2+
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pH 7.4, 37°C
0.00031
phenylacetyl-CoA
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0.8
thioctic acid
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025
Hg2+
Electrophorus electricus
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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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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purified enzyme, pH 7.4
142
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-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
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without NaCl in assay medium
7 - 8
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presence of NaCl
7.2
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additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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developing antenna during larvae development, enzyme detected in neurons, glia and epidermal cells
Manually annotated by BRENDA team
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pChAT+ nerve fibers are found exclusively in the trigeminal and solitary systems. The ventral portion of the principal sensory nucleus contains many pChAT+ fibers
Manually annotated by BRENDA team
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33% of activity membrane associated
Manually annotated by BRENDA team
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ChAT activity is higher in Ts65Dn mice at both 19 and 24 months of age compared to normogenic animals
Manually annotated by BRENDA team
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uvea
Manually annotated by BRENDA team
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lung, fetal lung fibroblasts, HFL-1
Manually annotated by BRENDA team
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impaired spatial working memory and altered choline acetyltransferase immunoreactivity and nicotinic receptor binding in rats exposed to intermittent hypoxia during sleep
Manually annotated by BRENDA team
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15% of activity membrane associated
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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strong pChAT signal in intrinsic primary afferent neurons, low immunoreactivity for cChAT
Manually annotated by BRENDA team
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non-neuronal cholinergic cell
Manually annotated by BRENDA team
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no significant differences of ChAT activity are measured at both 19 and 24 months of age between Ts65Dn mice and normogenic animals
Manually annotated by BRENDA team
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no significant differences of ChAT activity are measured at both 19 and 24 months of age between Ts65Dn mice and normogenic animals
Manually annotated by BRENDA team
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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
Manually annotated by BRENDA team
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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
Manually annotated by BRENDA team
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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
Manually annotated by BRENDA team
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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
Manually annotated by BRENDA team
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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
Manually annotated by BRENDA team
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pChAT occurs in most CGRP+ SP+ ganglion cells, such sparseness of pChAT+ fibers implies poor transportation of pChAT to axon branchlets
Manually annotated by BRENDA team
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dorsal motor nucleus of the vagus nerve, contains a peripheral-type pChAT, a splice variant that lacks exons 6-9 of the common-type ChAT, cChAT
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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ChAT transport in the microtubule, schematic overview
Manually annotated by BRENDA team
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associated with synaptic vesicles, can be displaced by treatment with urea or alkaline solutions
Manually annotated by BRENDA team
additional information
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immunofluorescent localization study, overview
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000 - 300000
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self-association to large aggregates, gel filtration, sedimentation equilibrium
49000
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pChAT
66800
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gel filtration
67000 - 69000
68000
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gel filtration
69000
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cChAT
71000
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gel filtration
76000
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pChAT with GFP as fusion protein
80000
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gel filtration
96000
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cChAT with GFP as fusion protein
106000
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largest aggregate, formation after ammonium sulfate fractionation, gel filtration
120000 - 125000
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peaks A, B1, gel filtration, gel electrophoresis
128000
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gel filtration
140000
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gradient polyacrylamide electrophoresis
200000
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peak B2, gel filtration, gel electrophoresis
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
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sitting drop vapor diffusion method
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vapor diffusion crystallization
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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increasing ionic strength increases susceptibility to thermal degradation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA stabilizes
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bovine serum albumin stabilizes
choline chloride stabilizes
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EDTA stabilizes
ethylene glycol stabilizes
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increasing ionic strength increases susceptibility to proteolysis and thermal degradation
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sucrose stabilizes
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
extremely sensitive to oxidation due to its cysteine-rich nature, oxidation causes formation of dimers and loss of activity
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660442
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, partially purified preparation, several months stable, less stable in purified state
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-20°C, several months
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4°C, 24 h, less than 10% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 isozymes
large scale
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overview procedures
placental acidic and basic form
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recombinant enzyme using His-tag
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recombinant proteins using His-tag or chitin-binding-domain
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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
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expressed as GFP fusion protein in HEK293 cells
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expressed in Escherichia coli B834
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expression in Escherichia coli
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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
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expression in Spodoptera frugiperda Sf9 cells; expression in Spodoptera frugiperda Sf9 cells using a baculovirus expression system
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expression of wild-type- and S440A mutant-enzyme in HEK293 cells
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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
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residues 18-617 of full length DNA expressed in Escherichia coli DH5alphaF’IQ
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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
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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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
interleukin-1beta induces the enzyme in HFL-1 cells
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Nelumbo nucifera semen extract improves memory in rats with scopolamine-induced amnesia through the induction of choline acetyltransferase expression
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pChAT expression is induced by neuronal damage
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scopolamine suppresses the enzyme in neurons
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H268L
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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
H268N
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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
H393L
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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
H393N
-
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
H426L
-
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
H426N
-
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
S440A
-
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
N514R
-
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
R452A
-
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
R453A
-
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
R458A
-
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
R463A
-
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
V459T/D460E/N461T
-
is described as ChAT-TET
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
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
diagnostics
-
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
medicine
pharmacology
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Nelumbo nucifera semen extract improves memory in rats with scopolamine-induced dementia through the induction of choline acetyltransferase expression and inhibition of acetylcholinesterase activity