Acetylcholinesterase (AChE) hydrolyzes the neurotransmitter, acetylcholine at neuromuscular junctions and brain cholinergic synapses, and thus terminates signal transmission. It is also found on the red blood cell membranes, where it constitutes the Yt blood group antigen. AChE exists in multiple molecular forms which possess similar catalytic properties, but differ in their oligomeric assembly and mode of cell attachment to the cell surface. The T form, also known as the asymmetric form, is soluble and is present in synapses. The H form is also known as the globular form and is present on the outer surfaces of cell membranes. The R form is not known to be a functional species. AChE globular form subunits are GPI-anchored to cell membranes and asymmetric subunits are anchored to basal lamina components by a collagen tail. The catalytic sununits of AChE are oligomers composed of disulfide-linked homodimers. The loss of AChE from cholinergic and noncholinergic neurons in the brain is seen in patients with Alzheimer′s disease. However, AChE activity is increased around amyloid plaques, which may be due to a disturbance in calcium homeostasis involving the opening of L-type voltage-dependent calcium channels.
Skeletal muscle tissues, striatum
IHC, ICC/IF, WB
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