| Abstract: | Mammalian skeletal muscle expresses at least two isoforms of the cytoskeletal protein titin (connectin; MW ≈ 3000 kDa). These isoforms are associated with different passive force curves, and thus may affect physical performance. To study the distribution of titin and its possible influence on performance in humans, muscle biopsies were obtained from 15 males (X ± SE; age = 25.4 ± 2.9 years, height = 177.7 ± 1.8 cm, weight = 76.5 ± 2.2 kg). Two biopsies were obtained on separate occasions from both the right and left vastus lateralis, and one biopsy each from the lateral head of the right gastrocnemius and the right soleus, with all biopsies handled identically. Fibre type analyses were performed via mATPase histochemistry. Expression of titin and myosin heavy chain isoforms were determined by SDS-PAGE. Titin bands in the resulting gels were highly repeatable and were verified by migration patterns, as well as Western blot analysis. Two groups of subjects were identified: group 1 (n=10) expressed only one titin isoform (titin-1) in all biopsies, and group 2 (n=5) expressed two titin isoforms (titin-1 and titin-2) in all biopsies. No significant differences (P> 0.05) between groups were observed for percentage fibre types, percentage fibre type areas, fibre type cross-sectional areas, and percentage myosin heavy chain expression when comparing individual muscles, sampling times or bilateral comparisons. This is the first report of differential titin isoform expression in healthy, mature human skeletal muscle, but it is not clear why this occurs or what influence this may have on performance. |
