Abstract
IN vertebrate skeletal muscle acetylcholinesterase (AChE, EC 3.1.1.7) is usually considered to be involved in the termination of impulse transmission by hydrolysis of acetylcholine1. AChE is often accompanied by a second enzyme2, pseudocholinesterase (ψ/ChE, EC 3.1.1.8), which differs from AChE in substrate specificity and in susceptibility to anticholinesterases3,4. No role comparable with that of AChE in synaptic transmission is known for ψChE, despite its abundance at some sites and its occurrence (as shown histochemically) with ψChE in various muscle endplates1,5. It has been suggested that ψChE is a precursor of AChE in the superior cervical ganglion6,7. Moreover, in ganglia and skeletal muscle of rats, forms of 0ChE have been demonstrated8 homologous with forms of ψChE observed previously9–11. Elevated levels of AChE have been demonstrated in aqueous extracts of fast-twitch muscles of dystrophic as compared with normal chickens12,13; ψChE levels increased similarly13, and also in such extracts of denervated muscles of normal chickens14. We show here that the total amounts and forms of AChE change in parallel with those of ψChE during development of skeletal muscles of both normal and dystrophic chickens, as well as on denervation of normal muscle. Our data strongly indicate that in these tissues the two enzymes are controlled by a common regulatory mechanism.
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SILMAN, I., GIAMBERARDINO, L., LYLES, J. et al. Parallel regulation of acetylcholinesterase and pseudocholinesterase in normal, denervated and dystrophic chicken skeletal muscle. Nature 280, 160–162 (1979). https://doi.org/10.1038/280160a0
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DOI: https://doi.org/10.1038/280160a0
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