Jll. Rivero et al., FIBER SIZE AND METABOLIC PROPERTIES OF MYOSIN HEAVY CHAIN-BASED FIBERTYPES IN RAT SKELETAL-MUSCLE, Journal of muscle research and cell motility, 19(7), 1998, pp. 733-742
Cross-sectional area (CSA), succinate dehydrogenase (SDH), and a-glyce
rophosphate dehydrogenase (GPD) activities were measured in single fib
res of adult rat medial gastrocnemius muscle (deep region) using quant
itative histochemical procedures. The same fibres were identified in s
erial sections stained by immunohistochemistry with monoclonal antibod
ies specific for selected myosin heavy chain (MyHC) isoforms. The valu
es of CSA, SDH and GPD activities formed a continuum, but significant
differences in mean values were observed among fibre types of presumed
homogeneous MyHC content. Type IIA fibres were the smallest, type IIB
fibres were the largest, and type I and IIX fibres were intermediate.
Type IIA fibres had the highest SDH activity, followed in rank order
by type IIX, type I and type IIB. The average GPD activity was ranked
according to fibre type such that IIB > IIX > IIA > I. Hybrid fibres c
o-expressing two MyHC isoforms generally showed intermediate mean CSA,
SDH and GPD values lying between their respective pure MyHC fibre typ
es. Across all fibres, there was an inverse relationship between SDH a
ctivity and CSA and between GPD and SDH activities, and a positive cor
relation between GPD and CSA. Moreover, a significant interdependence
between CSA, SDH activity, GPD activity and MyHC content existed on a
fibre-to-fibre basis, suggesting that the MyHC isoform expressed in a
fibre is associated with differences in size, oxidative and glycolytic
capabilities of muscle fibres. In fact, most of the fibres could be d
iscriminated into discrete groups with the same MyHC content when thei
r CSA, SDH and GPD values were considered together. (C) Kluwer Academi
c Publishers.