EC Number   |
General Information |
Reference |
|---|
   2.3.1.6 | malfunction |
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 |
705317 |
| 2.3.1.6 | malfunction |
loss of enzyme activity is associated with dementia with Lewy bodies |
736675 |
| 2.3.1.6 | malfunction |
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 |
703962 |
| 2.3.1.6 | malfunction |
the reduction in levels of O-acetylcholine is one of the most significant physiological symptoms of Alzheimer's disease |
735984 |
| 2.3.1.6 | physiological function |
acetylcholine, synthesized by ChAT, and muscarinic M1, M2, and M3 receptors are involved in fibroblast proliferation |
705317 |
| 2.3.1.6 | physiological function |
acute exposure to amyloid Abeta1-42 results in increased association of ChAT with chromatin and formation of ChAT aggregates in nuclei. Abeta1-42 -exposure increases ChAT association with gene promoters and introns. The Abeta1-42 -induced ChAT aggregates colocalize with special AT-rich binding protein 1 (SATB1), which anchors DNA to scaffolding/matrix attachment regions (S/MARs). Both ChAT and SATB proteins associate with synapse and cell stress genes. After Abeta1-42 -exposure, both SATB1 and ChAT are enriched at the same S/MAR on the APP gene, with ChAT expression attenuating an increase in an isoform-specific APP mRNA transcript |
758362 |
| 2.3.1.6 | physiological function |
both soluble amyloid Abeta40 and Abeta42 enhance the catalytic efficiency of ChAT byabout 21% and 26% at physiological concentration ranges found in cerebrospinal fluid. Activation of ChAT by Abeta is highly specific. Abeta42 exhibits an EC50 of activation at 10fold lower concentrations compared to Abeta40. The activation is persistent even in the presence of a physiological Abeta40/42 mixture ratio, expected in human cerebrospinal fluid |
756803 |
| 2.3.1.6 | physiological function |
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 |
702958 |
| 2.3.1.6 | physiological function |
choline acetyltransferase is robustly induced in both CD4+ and CD8+ T cells during lymphocytic choriomeningitis virus infection in an IL-21-dependent manner. Deletion of ChAT within the T cell compartment in mice ablates vasodilation in response to infection, impairs the migration of antiviral T cells into infected tissues, and ultimately compromises the control of chronic lymphocytic choriomeningitis virus clone 13 infection |
758467 |
| 2.3.1.6 | physiological function |
direct interaction between the kinesin-2 motor and ChAT for brief duration induces the episodic flow towards synapse, and synaptic activity is essential for this interaction. Blocking the acetylcholine synthesis through the HC3 treatment, and activation of the post synaptic neurons through the inhibition of actylcholine receptors by BTX, respectively, reduce the axonal entry and disrupt the episodic nature of ChAT transport within a short time |
758440 |
