Cellular Distribution of 16s Acetylcholinesterase

Fernández, Hugo L.; Duell, Myron J.; Festoff, Barry W.

doi:10.1111/j.1471-4159.1979.tb00387.x

Cited by 58 publications

(26 citation statements)

References 23 publications

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“…These forms approximately accounted for 2%, 70%, 16%, and 12% of total AChE activity, respectively. These results are consistent with those of a previous study showing small amounts of 16s-AChE in crude extracts of rat nervous tissue including whole spinal cord (LI-LG segments), ventral motor roots (Ls-L~ spinal roots), and hypoglossal, phrenic, and sciatic nerves (Fernandez et al, 1979a).…”

Section: Ache From Obturator Neruesupporting

confidence: 94%

“…The lower limit of 16s-AChE detectability has been defined in an earlier study in which different amounts of the 1 6 s enzyme, isolated from gracilis endplate regions, were subjected to a second centrifugation in sucrose gradients. The results indicated that small but reproducible 16s peaks could be resolved above a baseline of approximately 0.05 mU (Fernandez et al, 1979a).…”

Section: Ache From Bloodmentioning

confidence: 93%

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Neurotrophic control of 16S acetylcholinesterase at the vertebrate neuromuscular junction

1979

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Endplate 16S acetylcholinesterase (16S-AChE) from rat anterior gracilis muscle was assessed, 6 hr to 10 days after denervation, by velocity sedimentation analysis on linear sucrose gradients. The innervating obturator nerve was transected either close (1--2 mm, short stump) or far (35--40 mm, long stump) from the muscle. In both instances, the activity of 16S-AChE gradually decreased and reached approximately the same level (10%--20% of control) by 6 days after denervation. However, enzymatic decay started considerably earlier in short stump (12--24 hr) as compared to long stump (4--5 days preparations, i.e., the time of onset of 16S-AChE loss depended on the length of nerve that remained attached to the muscle. Whether this result extended to other AChE molecular forms (10S, 4S) in muscle endplates could not be determined because, in contrast to 16S-AChE, these forms were also detected in red blood cells (4S) and plasma (10S). Only small amounts of 16S-AChE were found in intact obturator nerves (1/100 of that in gracilis endplate regions). Thus a faster depletion of enzyme from shorter nerve stumps after axotomy could not entirely account for the substantial effect of nerve stump length on 16S-AChE. Since muscle contraction ceases immediately following nerve transection, regardless of nerve stump length, the results can be ascribed to the lack of some neural influence other than nerve-evoked muscle activity. The present findings are consistent with the view that maintenance of 16SAChE at neuromuscular junctions primarily depends on regulatory substances which are conveyed by axonal transport and released from nerve terminals.

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Section: Ache From Obturator Neruesupporting

confidence: 94%

Section: Ache From Bloodmentioning

confidence: 93%

Neurotrophic control of 16S acetylcholinesterase at the vertebrate neuromuscular junction

1979

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“…Previous work has shown AChE expression in motor neurons to be present along the axon (Massoulie and Bon, 1982;Rotundo and Carbonetto, 1987). In addition, asymmetric forms of the enzyme, present in synapses, have also been found in the motoneuron (Di Giamberardino and Couraud, 1978;Fernandez et al, 1979;Torres et al, 1983). Skeletal muscle myotubes in culture will secrete the asymmetric forms of AChE after differentiation (Inestrosa et al, 1982).…”

Section: Origin Of Acetylcholinesterase In the Neuromuscular Junctionmentioning

confidence: 99%

Acetylcholinesterase Expression in Muscle Is Specifically Controlled by a Promoter-Selective Enhancesome in the First Intron

Camp¹,

Jaco²,

Zhang³

et al. 2008

J. Neurosci.

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Mammalian acetylcholinesterase (AChE) gene expression is exquisitely regulated in target tissues and cells during differentiation. An intron located between the first and second exons governs a ϳ100-fold increase in AChE expression during myoblast to myotube differentiation in C2C12 cells. Regulation is confined to 255 bp of evolutionarily conserved sequence containing functional transcription factor consensus motifs that indirectly interact with the endogenous promoter. To examine control in vivo, this region was deleted by homologous recombination. The knock-out mouse is virtually devoid of AChE activity and its encoding mRNA in skeletal muscle, yet activities in brain and spinal cord innervating skeletal muscle are unaltered. The transcription factors MyoD and myocyte enhancer factor-2 appear to be responsible for muscle regulation. Selective control of AChE expression by this region is also found in hematopoietic lineages. Expression patterns in muscle and CNS neurons establish that virtually all AChE activity at the mammalian neuromuscular junction arises from skeletal muscle rather than from biosynthesis in the motoneuron cell body and axoplasmic transport.

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“…As in peripheral nerves of several birds or mammals (Skau and Brimijoin, 1978;Brimijoin, 1979;Fernandez et al, 1980;Vitadello et al, 1983;Couraud et al, 1983), not only the globular G I , G,, and G, forms of AChE but also the asymmetric A,, forms are detected in F and S rabbit nerves. It is worth noting that both nerves contain the same proportion of the AI2, a form that was shown to be almost exclusively confined to motor axons (Fernandez et al, 1979;Couraud, 1982). For that reason, we think that the differences observed in the molecular form distribution of F and S nerves, especially in their G , + G , and G, contents, do not result from different proportions of motor or sensory axons (see Landon and Hall, 1976), but are rather related to intrinsic differences among motor axons.…”

Section: Discussionmentioning

confidence: 99%

Retrograde Effect of Muscle on Forms of Acetylcholinesterase in Peripheral Nerves

Bacou

Vigneron

Couraud

1985

Journal of Neurochemistry

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In the peripheral nerves of birds and mammals, acetylcholinesterase (AChE) exists in four main molecular forms (G1, G2, G4, and A12). The two heaviest forms (G4 and A12) are carried by rapid axoplasmic transport, whereas the two lightest forms (G1 and G2) are probably much more slowly transported. Here we report that nerves innervating fast-twitch (F nerves) and slow-twitch (S nerves) muscles of the rabbit differ both in their AChE molecular form patterns and in their anterograde and retrograde axonal transport parameters. Since we had previously shown a selective regulation of this enzyme in fast and slow parts of rabbit semimembranosus muscle, we wondered whether the differences observed in the nerve could be affected by the twitch properties of muscle. The results reported here show that in F nerves that reinnervate slow-twitch muscles, both the AChE molecular form patterns and axonal transport parameters turn into those of the S nerve. These data suggest the existence of a retrograde specific effect exerted by the muscles on their respective motoneurons.

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Cellular Distribution of 16s Acetylcholinesterase

Cited by 58 publications

References 23 publications

Neurotrophic control of 16S acetylcholinesterase at the vertebrate neuromuscular junction

Neurotrophic control of 16S acetylcholinesterase at the vertebrate neuromuscular junction

Acetylcholinesterase Expression in Muscle Is Specifically Controlled by a Promoter-Selective Enhancesome in the First Intron

Retrograde Effect of Muscle on Forms of Acetylcholinesterase in Peripheral Nerves

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