Abstract:
:The axonal transport of the molecular forms of acetylcholinesterase was investigated in regenerating facial nerves of guinea-pig and rat. Four forms were separated by velocity sedimentation corresponding to 16S (A12), 10S (G4), 6S (G2) and 4S (G1) acetylcholinesterase. They displayed species-specific changes, which are in good accordance with those previously found in the neuronal perikarya. In the rat, axonal transport decreased for all forms. In the guinea-pig, however, the molecular forms showed differential changes. Whereas after transection, the nerve content of 10S acetylcholinesterase decreased, 16S activity was considerably increased. Anterograde transport of 16S acetylcholinesterase was found to be enhanced, whilst transport of the 10S from decreased. The two lighter forms showed only minor changes. Similar results were obtained for the guinea-pig sciatic nerve. Changes in the localization of acetylcholinesterase activity were investigated by electron microscopical cytochemistry. In the normal facial nerve of both species, activity was located intra-axonally in tubular membraneous structures and on the outer surface of the axonal membrane. In the regenerating facial nerve of the rat, intra-axonal as well as axolemmal activity decreased. Axonal sprouts at the end of the proximal nerve stump showed no activity. In the guinea-pig, however, activity of the axonal membrane increased. This was especially prominent on the surface of axonal sprouts. Strong activity was found also in the extracellular space between the sprouting axons and in the endoneurial space filled by collagen fibres. Biochemical analysis of this region revealed that the histochemical activity was mainly due to the A12 form. Thus it was concluded that, in the guinea-pig, axonal sprouts represent a target for axonally transported A12 acetylcholinesterase, which may also be secreted to extracellular sites.
journal_name
Neurosciencejournal_title
Neuroscienceauthors
Engel AK,Tetzlaff W,Kreutzberg GWdoi
10.1016/0306-4522(88)90365-xsubject
Has Abstractpub_date
1988-02-01 00:00:00pages
729-38issue
2eissn
0306-4522issn
1873-7544pii
0306-4522(88)90365-Xjournal_volume
24pub_type
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