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Molecular forms of acetylcholinesterase in the rat extensor digitorum longus and soleus muscles regenerating from notexin-induced necrosis.
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- Author(s): Kiss G;Kiss G; Zádor E; Szalay J; Somogyi J; Vér A
- Source:
Journal of muscle research and cell motility [J Muscle Res Cell Motil] 2004; Vol. 25 (7), pp. 509-14. Date of Electronic Publication: 2005 Feb 09.
- Publication Type:
Journal Article; Research Support, Non-U.S. Gov't
- Language:
English
- Additional Information
- Source:
Publisher: Springer Netherlands Country of Publication: Netherlands NLM ID: 8006298 Publication Model: Print-Electronic Cited Medium: Print ISSN: 0142-4319 (Print) Linking ISSN: 01424319 NLM ISO Abbreviation: J Muscle Res Cell Motil Subsets: MEDLINE
- Publication Information:
Publication: Dordrecht : Springer Netherlands
Original Publication: [London] Chapman and Hall.
- Subject Terms:
- Abstract:
The activity of acetylcholinesterase molecular forms were examined after separation on sucrose gradients during notexin-induced necrosis and the following regeneration in rat extensor digitorum longus (EDL) and soleus (SOL) muscles. All forms dropped rapidly in both muscles in the first few days after single notexin injection. After a delay small globular forms (G1+G2) started to regenerate from day 7 and larger forms (G4 and A12) from day 10 in EDL. The A8 form which cannot be detected in normal EDL was present between day 7 and day 28. In SOL the recovery of AChE forms begun already on day 3. The small globular forms displayed a more rapid increase between day 3 and day 7 then the other forms. In SOL we observed a temporary overshooting peak at day 7 in the activity of all molecular forms. Both muscles recovered their normal AChE pattern by that time when muscle fibres regained their normal diameter (day 28). Most of the events of regeneration of AChE forms resembled those of normal myogenesis.
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- Accession Number:
0 (Elapid Venoms)
0 (Isoenzymes)
37223-96-4 (notexin)
EC 3.1.1.7 (Acetylcholinesterase)
- Publication Date:
Date Created: 20050216 Date Completed: 20050712 Latest Revision: 20181113
- Publication Date:
20240829
- Accession Number:
10.1007/s10974-004-2928-9
- Accession Number:
15711881
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