Ca2+ activation properties of myofibrillar ATPase from fatigued rat plantaris.
1. Muscle fatigue following long-duration rhythmic activity is often characterized by reduced force following a single impulse and at low-frequencies of stimulation. 2. Although this response is generally attributed to an alteration in excitation-contraction coupling, the possibility that the responsiveness of myofibrillar proteins to a given Ca2+ signal is altered has never been ruled out. 3. In this study, rat plantaris muscles were subjected to an in situ regimen of contractions (100 Hz, lasting 100 msec, once every 750 msec, for 1 hr), and allowed to recover for 15 min. 4. Twitch, 100 Hz, and 200 Hz forces were reduced by 79%, 49% and 17% respectively, at this time. 5. In myofibrils isolated from these muscles, maximum activity of Ca2+ activated myofibrillar ATPase, Ca2+ sensitivity (pCa 50), and co-operatively (Hill n), were not different from non-fatigued muscles. 6. It appears, therefore, that the Ca2+ activation properties of myofibrillar ATPase do not contribute to this pattern of fatigue.
Département d'Education Physique, Université de Montréal, Quebec, Canada.
R A
RA
Turcotte
H
H
Oueslati
P F
PF
Gardiner
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000378:metabolism*; D004789:Enzyme Activation; D005260:Female; D009119:Muscle Contraction; D009132:Muscles / Q000201:enzymology* / Q000503:physiopathology; D009210:Myofibrils / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains
D000251:Adenosine Triphosphatases; D002118:Calcium