Mechanical properties and myosin heavy chain isoform composition of skinned skeletal muscle fibres from a human biopsy sample.
Experiments were conducted to investigate the mechanics of contraction of chemically skinned muscle fibre segments of a biopsied sample of single human quadriceps muscle. Subsequently, the isoforms of the myosin 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 terms of the kinetics of force responses following stepwise length changes (order of velocity: IIA > IIC > I). The differences in maximal shortening velocity and in the kinetics of Ca(2+)-dependent activation were of the same order, but much less pronounced. Type I fibres had significantly greater fibre diameters than type IIA fibres. No significant differences were found among different fibre types in terms of isometric tension, resting sarcomere length or the length change needed to discharge the elasticity of maximally Ca(2+)-activated fibres (V0 value). The distribution of shortening velocity and kinetics of stretch activation values suggest that two muscle fibre subtypes may exist in human type I fibres.
Hilber
K
K
Abteilung Tierphysiologie, Universität Salzburg, Austria.
Galler
S
S
D000328:Adult; D001706:Biopsy; D006652:Histological Techniques; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism*; D007537:Isometric Contraction; D008297:Male; D018485:Muscle Fibers, Skeletal / Q000378:metabolism* / Q000473:pathology / Q000502:physiology*; D018482:Muscle, Skeletal / Q000378:metabolism* / Q000473:pathology / Q000502:physiology*; D018995:Myosin Heavy Chains / Q000378:metabolism*
D007527:Isoenzymes; D018995:Myosin Heavy Chains