A. Conjard et al., ENERGY-STATE AND MYOSIN HEAVY-CHAIN ISOFORMS IN SINGLE FIBERS OF NORMAL AND TRANSFORMING RABBIT MUSCLES, Pflugers Archiv, 436(6), 1998, pp. 962-969
Energy-rich phosphates, [ATP]/[ADP(free)] ratios, and the myosin heavy
chain (MHC) complement were determined in single fibres from normal r
abbit muscles, and in fibres isolated from tibialis anterior muscle un
dergoing fast-to-slow conversion by chronic low-frequency stimulation
(CLFS). In normal muscles, energy-rich phosphate contents and [ATP]/[A
DP(free)] ratios could thus be assigned to different MHC-based fibre t
ypes. Phosphocreatine (PCr) contents and [ATP]/[ADP(free)] ratios diff
ered markedly between fast- and slow-twitch fibres, as well as within
the fast fibre subtypes. Both magnitudes were approximately twofold hi
gher in the fastest (type IIB) fibres as compared to the slowest (type
I) fibres. According to PCr contents and [ATP]/[ADP(free)] ratios pur
e and hybrid fibres were aligned in an order similar to that determine
d by their contractile properties and myofibrillar ATPase activities.
CLFS for up to 30 days induced pronounced decreases in PCr and [ATP]/[
ADP(free)] which attained levels twofold lower than in normal slow-twi
tch fibres. In both normal and stimulated muscles, PCr and [ATP]/[ADP(
free)] ratios were correlated, indicating their equilibrium in the dif
ferent fibre types. The relationship detected between MHC isoform expr
ession and the [ATP]/[ADP(free)] ratio suggests that the drastic and p
ersistent depression of the cellular energy state may act as an import
ant signal initialing fast-to-slow transformation processes in muscle
fibres.