K. Hilber et S. Galler, MECHANICAL-PROPERTIES AND MYOSIN HEAVY-CHAIN ISOFORM COMPOSITION OF SKINNED SKELETAL-MUSCLE FIBERS FROM A HUMAN BIOPSY SAMPLE, Pflugers Archiv, 434(5), 1997, pp. 551-558
Experiments were conducted to investigate the mechanics of contraction
of chemically skinned muscle fibre segments of a biopsied sample of s
ingle human quadriceps muscle. Subsequently, the isoforms of the myosi
n heavy chain (MHC) were analysed by sodium dodecyl sulphate (SDS) gel
electrophoresis. Of the 41 fibres, 26 contained MHCI (type I), 11 of
the fibres contained MHCIIa (type IIA), and 4 of the fibres contained
both MHCI and MHCIIa (of which MHCIIa was always slightly predominant
(type IIC)). Distinct differences between fibre types were found in te
rms of the kinetics of force responses following stepwise length chang
es (order of velocity: IIA > IIC > I). The differences in maximal shor
tening velocity and in the kinetics of Ca2+-dependent activation were
of the same order, but much less pronounced. Type I fibres had signifi
cantly greater fibre diameters than type IIA fibres. No significant di
fferences were found among different fibre types in terms of isometric
tension, resting sarcomere length or the length change needed to disc
harge the elasticity of maximally Ca2+-activated fibres (y(o) value).
The distribution of shortening velocity and kinetics of stretch activa
tion values suggest that two muscle fibre subtypes may exist in human
type I fibres.