2008, Number 2
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Rev Educ Bioquimica 2008; 27 (2)
Enzimas polifuncionales: El caso de la acetilcolinesterasa
Sánchez-Chávez G, Salceda R
Language: Spanish
References: 17
Page: 44-51
PDF size: 204.11 Kb.
ABSTRACT
Acetylcholinesterase (AChE) is the enzyme that ends
the neurotransmitter effect of the acetylcholine and
together with butyrylcholinesterase (BChE) belong to a
group of enzymes known as cholinesterases (ChEs),
which are synthesized from a single gene for each one.
Three variants of AChE are originated from alternative
splicing at 3' end of the transcrits and post-translational
modifications. The AChE-R is expressed as monomers
in stress and neuropathological conditions; the AChE-E
are amphiphilic dimers that are present in erythrocytes
and the AChE-T is localized mainly in synapses, and
can be expressed as asymmetric and globular forms.
Additional to its classical cholinergic function, AChE
participates in developmental processes and contains a
domain that is present in cell adhesion proteins as the
glutactin, neurotactin, gliotactin and neuroligins.
Changes in their levels or properties are present in
different neuropathologies as the Alzheimer, Parkinson
and miastenia gravis.
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