title: Changes in rat muscle with compensatory overload occur in a sequential manner.
abstract: The present study was initiated to determine the time course of changes in the profile of selected skeletal muscle myofibril proteins during compensatory overload. Whole muscle isometric contractile properties were measured to assess the physiological consequences of the overload stimulus. Compensatory overload of plantaris muscle of rats was induced by surgical ablation of the synergistic soleus and gastrocnemius muscles. Myosin light chain (LC) and tropomyosin (TM) compositions of control (CP) and overloaded plantaris (OP) muscles were determined by electrophoresis and myofibrillar ATPase assays were performed to assess changes in contractile protein interactions. Within one week of overload decreases in the alpha:beta TM ratio and myofibrillar ATPase activity were observed. Following 30 days of overload, a transition in type II to type I fibres was associated with an increase in slow myosin LC1. Interestingly, after 77 days of overload, the TM subunit ratio returned to one resembling a fast twitch muscle. It is proposed that the early and transitory changes in the TM subunits of OP, as well as the rapid initial depression in maximum tetanic isometric force and myofibrillar ATPase activity may be explained as a result of muscle fibre degeneration-regeneration. We propose that alterations in protein expression induced by compensatory overload reflect both degenerative-regenerative change and increased neuromuscular activity.
authors.affiliation: Faculty of Kinesiology, University of Western Ontario, London, Canada.
authors.forename: P C
authors.initials: PC
authors.lastname: Macpherson
authors.forename: R E
authors.initials: RE
authors.lastname: Thayer
authors.forename: C
authors.initials: C
authors.lastname: Rodgers
authors.forename: A W
authors.initials: AW
authors.lastname: Taylor
authors.forename: E G
authors.initials: EG
authors.lastname: Noble
mesh_terms: D000222:Adaptation, Physiological; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D006651:Histocytochemistry; D007537:Isometric Contraction / Q000502:physiology; D008297:Male; D020894:Microfibrils / Q000201:enzymology / Q000378:metabolism; D009119:Muscle Contraction / Q000502:physiology; D018482:Muscle, Skeletal / Q000201:enzymology / Q000378:metabolism / Q000502:physiology*; D009218:Myosins / Q000378:metabolism; D009929:Organ Size / Q000502:physiology; D051381:Rats; D017207:Rats, Sprague-Dawley; D014335:Tropomyosin / Q000378:metabolism
chemical_list: D014335:Tropomyosin; D000251:Adenosine Triphosphatases; D009218:Myosins