25 Specific and Non-Specific Adaptations to Rowing and Cycle Ergometer Training

Vordun, H.; Dudley, Gary A.; Fry, A.; Gilders, Roger M.; Hagerman, Fredrick C.; Hurray, T.; Ploutz, L. L.; Staron, Robert S.

doi:10.1249/00005768-199405001-00026

Cited by 1 publication

(4 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In general, it appears that the passive force-producing properties of titin may be modulated by a number of possible mechanisms and may eventually in¯uence gross physical performances. Comparisons of previously published performance data for these subjects (Allemeier et al 1994, Verdun et al 1994, however, indicate no between-group differences for muscular strength, muscular endurance or aerobic capacity. Similarly, muscle performance differences have not been previously observed between titin isoforms in individuals with muscular dystrophy (Horowits et al 1990).…”

Section: Variablementioning

confidence: 57%

“…the same muscle at two different times. Identical titin isoform expression was also evident among different muscles (vastus lateralis, medial head of the gastrocnemius, soleus), even though these muscles exhibit different ®bre type pro®les (Verdun et al 1994, Vandenborne et al 1995; see also Table 2). This is contrary to reports of ®bre type-speci®c and muscle-speci®c titin isoforms in animals (Akster et al 1989, Horowits 1992, where fast-twitch ®bres exhibit titin isoforms with greater stiffness characteristics than slow-twitch ®bres.…”

Section: Discussionmentioning

confidence: 94%

“…Fifteen healthy males (X SE; age 25X4 AE 2X9 years, height 177X7 AE 1X8 cm, weight 76X5AE 2X2 kg, % fat 12X0 AE 1X1%) volunteered to participate in a series of three separate investigations (Allemeier et al 1994, Verdun et al 1994, Vandenborne et al 1995. All subjects signed informed consent statements approved by the Ohio University Institutional Review Board.…”

Section: Subjects and Biopsiesmentioning

confidence: 99%

“…Single percutaneous muscle biopsies (80±160 mg) (Bergstro Èm 1962) were extracted from the right soleus n 15 and the lateral head of the right gastrocnemius n 15 (Vandenborne et al 1995), and two biopsies (pre and post) were extracted on separate occasions from both the right n 5 and left n 14 vastus lateralis muscles (Allemeier et al 1994, Verdun et al 1994. The pre-and post-biopsies taken from the left vastus lateralis muscles were separated by a 16 week aerobic rowing training protocol (Verdun et al 1994), while the right vastus lateralis samples were separated by a 6 week sprint cycling training protocol (Allemeier et al 1994). Not all subjects participated in all three investigations, explaining the unequal biopsy numbers.…”

Section: Subjects and Biopsiesmentioning

confidence: 99%

See 3 more Smart Citations

Differential titin isoform expression in human skeletal muscle

Fry

Staron

James

et al. 1997

Acta Physiologica Scandinavica

View full text Add to dashboard Cite

Mammalian skeletal muscle expresses at least two isoforms of the cytoskeletal protein titin (connectin; MW approximately 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 (mean +/- 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.

show abstract

Section: Variablementioning

confidence: 57%