Myotubes originating from single fast and slow satellite cells display similar patterns of AChE expression.
Slow- and fast-contracting skeletal muscles of both rats and mice display significant differences in their patterns of acetylcholinesterase (AChE) expression. Although neural influences are known to account for a large proportion of these differences, intrinsic variations between fast and slow myogenic precursor cells have been implicated. In the present study, we have capitalized on the use of Immorto transgenic mice to obtain single myogenic precursor cells isolated from either slow or fast muscle fibers and determined whether these cells generated myotubes that produced distinct patterns of AChE expression as observed in vivo between slow and fast muscles. These two myotube populations displayed similar cell-associated and secreted AChE enzyme activity as well as comparable levels of AChE transcripts. Both myotube populations also expressed nearly identical molecular form profiles. By contrast, AChE activity and transcript levels were approximately two- and fivefold greater in fast skeletal muscles compared with slow ones. Together, these findings indicate that differences in AChE expression between fast and slow muscles are not due to inherent differences in myogenic precursor cells, thereby suggesting that other factors, such as innervation, play a predominant role in establishing the distinct patterns of AChE expression in these muscle types.
Boudreau-Larivière
C
C
Department of Cellular and Molecular Medicine, Faculty of Medicine, University of Ottawa, Ottawa, Ontario, Canada K1H 8M5.
Parry
D J
DJ
Jasmin
B J
BJ
D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D002478:Cells, Cultured; D005260:Female; D006614:Hindlimb; D051379:Mice; D008822:Mice, Transgenic; D018656:Muscle Fibers, Fast-Twitch / Q000201:enzymology*; D018657:Muscle Fibers, Slow-Twitch / Q000201:enzymology*; D018482:Muscle, Skeletal / Q000201:enzymology*; D051381:Rats; D017207:Rats, Sprague-Dawley
D000110:Acetylcholinesterase