Influence of human muscle length on energy transduction studied by 31P-NMR.
Muscle contractions at lengths below the optimum for force development were previously found to cause less fatigue than contractions at the optimum length (Lo). Decreased fatigability was suggested to arise from fewer cross-bridge interactions in shortened sarcomeres. In the present study, this suggestion was tested by monitoring energy use of human ankle dorsiflexor muscles during and after contractions at Lo and shortened lengths (Ls) with phosphorus nuclear magnetic resonance spectroscopy. The nuclear magnetic resonance spectra indicated similar rates of ATP use during contractions at Lo and Ls. Phosphocreatine, at an initial concentration of 37 mM, was reduced to an equivalent extent by 2 min of ischemic exercise at Lo (to 2.3 mM) and Ls (to 4.7 mM). Changes in pH (indicating glycolytic ATP production) were also equivalent at Lo and Ls. Exercise caused pH to fall from an initial level of 7.07 to 6.5 at Lo and to 6.53 at Ls. In relation to previous experiments performed under similar conditions on human ankle dorsiflexor muscles, the present experiments suggest that in shortened muscle the decreased force found in this and previous studies and the decreased fatigability that was previously found may not be simply due to fewer cross-bridge interactions in shortened sarcomeres. Examination of the relationships between developed force and levels of metabolites suggests that changes of force during fatigue and recovery correlate better with intracellular [Pi] and H2PO4- than with [H+].
Baker
A J
AJ
Magnetic Resonance Unit, Veterans Affairs Medical Center, San Francisco, California.
Carson
P J
PJ
Green
A T
AT
Miller
R G
RG
Weiner
M W
MW
D000255:Adenosine Triphosphate / Q000378:metabolism; D000328:Adult; D004734:Energy Metabolism / Q000502:physiology*; D005221:Fatigue / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D009119:Muscle Contraction / Q000502:physiology; D009132:Muscles / Q000033:anatomy & histology / Q000378:metabolism / Q000502:physiology*; D010710:Phosphates / Q000378:metabolism; D010725:Phosphocreatine / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology
D010710:Phosphates; D010725:Phosphocreatine; D000255:Adenosine Triphosphate