acetylcholinesteráza

Acetylcholinesterase, often abbreviated as AChE, is a critical enzyme found in many biological systems. Its primary role is to break down the neurotransmitter acetylcholine into choline and acetic acid. This hydrolysis is essential for the proper functioning of cholinergic synapses, the junctions where acetylcholine is used as a chemical messenger. By rapidly degrading acetylcholine, AChE ensures that nerve signals are transmitted efficiently and that the postsynaptic neuron is not continuously stimulated.

This enzyme is particularly abundant at neuromuscular junctions, where it terminates the signal from motor neurons to muscles, allowing for muscle relaxation after contraction. It is also present in the central nervous system, playing a role in synaptic transmission within the brain, and in various other tissues. The activity of acetylcholinesterase is crucial for maintaining the balance of the nervous system.

Due to its vital function, acetylcholinesterase is a target for various substances. Organophosphates, a class of chemicals found in some pesticides and nerve agents, inhibit AChE. This inhibition leads to an accumulation of acetylcholine, causing overstimulation of nerve and muscle cells, which can be severely toxic. Conversely, some medications, such as those used to treat Alzheimer's disease, work by inhibiting AChE to increase acetylcholine levels in the brain, thereby improving cognitive function. The study of acetylcholinesterase is therefore significant in both toxicology and pharmacology.