Variation in expression of calcium-handling proteins is associated with inter-individual differences in mechanical performance of rat (Rattus norvegicus) skeletal muscle.

An important constraint on locomotor performance is the trade-off between sprint and endurance performance. One intuitive explanation for this trade-off is that an individual muscle cannot excel at generating both maximal force/power and high fatigue resistance. The underlying reasons for this muscle trade-oft are poorly defined. The aim of this study was to test the hypothesis that inter-individual variation in muscle mechanics is associated with inter-individual differences in metabolic capacities and expression of calcium-handling proteins. Lateral gastrocnemius muscles were isolated from 20 rats (Rattus norvegicus) and analysed to determine metabolic capacity, sarco/endoplasmic reticulum calcium ATPase (SERCA)1 protein concentration, total SERCA activity, and mRNA concentrations of SERCA1, SERCA2, troponin I and ryanodine receptors. Isometric studies of lateral gastrocnemius muscles at 300C showed that muscles with higher sprint performance had lower fatigue resistance. More rapid muscle contraction was correlated with higher lactate dehydrogenase activity and increased expression of ryanodine receptor 1. More rapid muscle relaxation was correlated with increased expression of troponin I type 2 (fast) isoform and decreased expression of SERCA2 (slow) isoform. Treating muscles with dantrolene confirmed that ryanodine receptor activity is important in determining tetanus force and muscle contraction rates, but has no effect on fatigue resistance. Thapsigargin treatment revealed that SERCA activity determines fatigue resistance but does not affect maximal muscle force or contraction rates. We conclude that the opposing roles of SERCA activity and expression of ryanodine receptors in determining fatigue resistance and force production, respectively, at least partly explain differences in sprint and endurance performance in isolated rat gastrocnemius muscle. [ABSTRACT FROM AUTHOR]