Force-dependent and force-independent heat production in single slow- and fast-twitch muscle fibres from Xenopus laevis.
1. The origin of labile heat production, i.e. a heat component which rapidly decays after the onset of stimulation, and of stable (maintenance) heat production was investigated in intact single fast-twitch (type 1) and slow-twitch (type 3) iliofibularis muscle fibres from Xenopus laevis, at 20 degrees C, by varying stimulation frequency and by varying sarcomere length and the concentration of 2,3-butanedione 2-monoxime (BDM) added. 2. The labile heat produced consisted of a force-independent and a force-dependent part. The average parvalbumin (PA) content found in type 1 fibre bundles (0.84 +/- 0.08 mM; mean +/- S.E.M.; n = 5) and in type 3 fibre bundles (0.12 +/- 0.02 mM; n = 5) indicates that the force-independent labile heat is explained by Ca(2+)-Mg2+ exchange on PA, and amounts to a molar enthalpy change of -78 kJ (molPA)-1. 3. Force-dependent labile heat during fused contractions was similar to the calculated heat production resulting from the formation of force-generating cross-bridges, assuming an enthalpy change associated with cross-bridge formation of -30 kJ mol-1. 4. Activation heat, i.e. the part of the total stable heat that is not related to the contractile apparatus, and of which the calcium sequestration by the sarcoplasmic reticulum is the most important contributor, determined by varying sarcomere length or BDM concentration, was identical. For fused contractions the fraction activation heat of the stable maintenance rate of heat production was 34 +/- 4% (mean +/- S.E.M.; n = 13) in type 1 fibres, and 52 +/- 4% (n = 15) in type 3 fibres. In unfused contractions this was 48 +/- 5% (n = 13) in type 1 fibres, and 35 +/- 2% (n = 11) in type 3 fibres. 5. From the force-dependent stable rate of heat production the economy of cross-bridge cycling, expressed as the force-time integral for a single myosin head per ATP molecule hydrolysed, was calculated. It followed that cross-bridge interaction in type 3 fibres is more economical than in type 1 fibres, and that fused contractions are more economical than unfused contractions.
Buschman
H P
HP
Laboratory for Physiology, Vrije Universiteit, Amsterdam, The Netherlands. buschman@mit.edu
van der Laarse
W J
WJ
Stienen
G J
GJ
Elzinga
G
G
D000818:Animals; D001833:Body Temperature Regulation / Q000502:physiology*; D004558:Electric Stimulation; D004734:Energy Metabolism / Q000502:physiology; D005260:Female; D066298:In Vitro Techniques; D007537:Isometric Contraction / Q000502:physiology; D009119:Muscle Contraction / Q000502:physiology; D018656:Muscle Fibers, Fast-Twitch / Q000502:physiology* / Q000648:ultrastructure; D018657:Muscle Fibers, Slow-Twitch / Q000502:physiology* / Q000648:ultrastructure; D018482:Muscle, Skeletal / Q000166:cytology / Q000502:physiology* / Q000648:ultrastructure; D010320:Parvalbumins / Q000378:metabolism; D012518:Sarcomeres / Q000648:ultrastructure; D013816:Thermodynamics; D014982:Xenopus laevis
D010320:Parvalbumins