Differential titin isoform expression in human skeletal muscle

Fry, Andrew C.; Staron, Robert S.; James, Calvin; Hikida, Robert S.; Hagerman, Fredrick C.

doi:10.1046/j.1365-201x.1997.00252.x

Cited by 19 publications

(13 citation statements)

References 32 publications

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“…These results suggest that jumping exercise did not change titin isoform expression. Fry et al (1997) partly support this suggestion showing that each studied subject expressed the same titin isoforms in VL, GA, and SOL, and both a 16-week aerobic rowing and a 6-week sprint cycling training protocols did not appear to affect titin isoform composition. Toursel et al (2002) showed, however, that changes in passive tension could occur without changes in titin isoform expression in single fibers in unloaded rat SOL muscles.…”

Section: Discussionsupporting

confidence: 67%

Effects of power training on muscle structure and neuromuscular performance

Kyröläinen

Avela

McBride

et al. 2005

Scandinavian Med Sci Sports

144

103

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The present study examines changes in muscle structure and neuromuscular performance induced by 15 weeks of power training with explosive muscle actions. Twenty‐three subjects, including 10 controls, volunteered for the study. Muscle biopsies were obtained from the gastrocnemius muscle before and after the training period, while maximal voluntary isometric contractions (MVC) and drop jump tests were performed once every fifth week. No statistically significant improvements in MVC of the knee extensor (KE) and plantarflexor muscles were observed during the training period. However, the maximal rate of force development (RFD) of KE increased from 18 836±4282 to 25 443±8897 N (P<0.05) during the first 10 weeks of training. In addition, vertical jump height (vertical rise of the center of body mass) in the drop jump test increased significantly (P<0.01). Simultaneously, explosive force production of KE muscles measured as knee moment and power increased significantly; however, there was no significant change (P>0.05) in muscle activity (electromyography) of KE. The mean percentage for myosin heavy chain and titin isoforms, muscle fiber‐type distributions and areas were unchanged. The enhanced performance in jumping as a result of power training can be explained, in part, by some modification in the joint control strategy and/or increased RFD capabilities of the KE.

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Section: Discussionsupporting

confidence: 67%

Effects of power training on muscle structure and neuromuscular performance

Kyröläinen

Avela

McBride

et al. 2005

Scandinavian Med Sci Sports

144

103

View full text Add to dashboard Cite

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“…The question that arises from both this investigation and the study by Fry et al (1997) is to the true nature of these bands. Titin analysis through gel electrophoresis often results in two protein bands (Tatsumi and Hattori 1995).…”

Section: Discussionmentioning

confidence: 98%

“…1 Gel electrophoresis of human skeletal muscle using a 2% polyacrylamide gel reinforced with agarose for comparison of T1 and T2 relative quantities and relative mobilities between powerlifters, weightlifters, sprinters and nonathletes gation also reported that while some subjects expressed two titin protein bands others only expressed a single band. The study by Fry et al (1997) also examined preand post-titin band expression after an aerobic rowing and sprint cycling training protocol reporting no significant differences.…”

Section: Discussionmentioning

confidence: 99%

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Characteristics of titin in strength and power athletes

McBride¹,

Triplett-McBride²,

Davie

et al. 2003

Eur J Appl Physiol

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The purpose of this investigation was to identify characteristics of the muscle protein titin in different athletic populations with increased levels of strength and power relative to non-athletes. Subjects fell into one of four groups: (1) non-athletes (NA) ( n=5), (2) weightlifters (WL) (n=5), (3) powerlifters (PL) (n=5), (4) sprinters (S) (n=5). A one repetition maximum in the squat exercise was performed to assess strength. In addition, countermovement vertical jump trials were performed to assess power capabilities. Peak power (W(peak)) was calculated for the vertical jumps from force plate measurements. From gel electrophoresis analyses of muscle samples, titin-1 (T1) and titin-2 (T2) protein bands were identified, quantified and expressed relative to each other. In addition the relative mobility (R(f)) of T1 and T2 was determined as an estimate of molecular weight. The NA group [%T1=47.8 (5.1), %T2=52.2 (5.1), mean (SE)] had lower T1 and higher T2 percentages than WL [%T1=62.3 (6.6), %T2=37.7 (6.6)], PL [%T1=66.8 (5.0), %T2=33.2 (5.0)] and S [%T1=65.9 (4.9), %T2=34.1 (4.9)] groups (P< or =0.10, preliminary investigation into titin and exercise justifies more liberal alpha level). No significant differences were found in R(f) of T1 or T2 between the groups. This investigation has shown that there is a differential expression of titin protein bands in competitive athletes with increased levels of strength and power in comparison to untrained non-athletic individuals. Some relationships between titin characteristics and athletic performance were observed; however, no conclusions can be made based on these data as to the contribution of titin to strength or power capabilities.

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“…Although from a single gene, the alternative splicing of titin mRNA allows for varying sizes of different titin isoforms to be present within striated muscle (45). In human skeletal muscle, two titin isoforms have been reported (62), with no fiber type-or muscle-specific associations observed (28). In both isoforms, the I-band region of titin is comprised of the proximal and distal immunoglobulin (Ig) tandem domains, the N2A domain, and a PEVK segment.…”

Section: Longitudinal Force Transmissionmentioning

confidence: 99%

Effects of aging, exercise, and disease on force transfer in skeletal muscle

Hughes

Wallace

Baar

2015

American Journal of Physiology-Endocrinology and Metabolism

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Hughes DC, Wallace MA, Baar K. Effects of aging, exercise, and disease on force transfer in skeletal muscle. Am J Physiol Endocrinol Metab 309: E1-E10, 2015. First published May 12, 2015; doi:10.1152/ajpendo.00095.2015.-The loss of muscle strength and increased injury rate in aging skeletal muscle has previously been attributed to loss of muscle protein (cross-sectional area) and/or decreased neural activation. However, it is becoming clear that force transfer within and between fibers plays a significant role in this process as well. Force transfer involves a secondary matrix of proteins that align and transmit the force produced by the thick and thin filaments along muscle fibers and out to the extracellular matrix. These specialized networks of cytoskeletal proteins aid in passing force through the muscle and also serve to protect individual fibers from injury. This review discusses the cytoskeleton proteins that have been identified as playing a role in muscle force transmission, both longitudinally and laterally, and where possible highlights how disease, aging, and exercise influence the expression and function of these proteins. force transmission; dystrophin-glycoprotein complex; injury; aging ON AVERAGE, HUMANS LOSE AROUND 45% of their muscle mass between their mid-20s and 80s (47,70,71). This loss in muscle mass in the absence of disease is known as sarcopenia (60). The decline in muscle mass is accompanied by, but cannot fully explain, a rapid loss in muscle strength (64). The loss in muscle strength has previously been investigated from the perspectives of loss of muscle protein mass (cross-sectional area) and decreased neural activation. A third possibility, impaired force transfer, has received the least attention in relation to aging, exercise, and disease (66,90,102). However, recent advances in our understanding of this process suggest that force transfer plays an important role in muscle strength and injury prevention, and this fact is the focus of this review. Force TransferOver 60 years ago, Andrew Huxley and his students used electron microscopy to show that during muscle contraction the I-band (containing the thin filament) shortened whereas the A-band (containing the thick filament) remained a constant length (39). Their famous "sliding theory of muscle contraction" provided an image of a muscle shortening end to end as the A-bands drew closer together. Implied in this model is that force is transferred in a longitudinal manner as a result of sarcomere shortening. However, a deeper consideration of this model requires that there be a secondary matrix of proteins that are not visible to the electron microscope, proteins that transmit the force produced by the thick and thin filaments along the muscle fiber to the tendons. These specialized networks of cytoskeletal proteins transmit force through the muscle to the tendon and also serve to protect individual fibers from injury.An important structure in these networks is the "costamere", which connects the sarcolemma with the contractile appar...

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Differential titin isoform expression in human skeletal muscle

Cited by 19 publications

References 32 publications

Effects of power training on muscle structure and neuromuscular performance

Effects of power training on muscle structure and neuromuscular performance

Characteristics of titin in strength and power athletes

Effects of aging, exercise, and disease on force transfer in skeletal muscle

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