Age- and Gender-Related Differences in Maximum Shortening Velocity of Skeletal Muscle Fibers

Krivickas, Lisa S.; Suh, Dongwon; Wilkins, John T.; Hughes, Virginia; Roubenoff, Ronenn; Frontera, Walter R.

doi:10.1097/00002060-200106000-00012

Cited by 128 publications

(109 citation statements)

References 33 publications

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“…The heightened susceptibility to damage observed here, coupled with an impaired ability to recover from injury or adapt to repeated exercise reported by others (Dedrick and Clarkson 1990;McBride et al 1995;Brooks and Faulkner 1990;Rader and Faulkner 2006;Lavender and Nosaka 2006b;Cutlip et al 2006) could be a contributor to the reduced lower limb muscle strength of elderly adults. Because contraction-induced damage impairs excitation-contraction coupling and cross-bridge function (Balnave and Allen 1995;Warren et al 1994), a heightened susceptibility to injury could initiate the age-related deterioration in muscle fiber activation and contractility (Delbono et al 1995;Wang et al 2002;Larsson et al 1997;Thompson and Brown 1999;Lowe et al 2001;Frontera et al 2000;Hook et al 2001;Krivickas et al 2001). Consistent with our results, studies conducted on skinned fibers from EDL muscles of young and old laboratory rodents have identified age-related deficits at the level of the force-producing or force-transmitting components of the cell (Lynch et al 2008;Brooks and Faulkner 1996).…”

Section: Discussionsupporting

confidence: 87%

“…Cross-bridge kinetics are altered with aging (Larsson et al 1997;Thompson and Brown 1999;Lowe et al 2001;Frontera et al 2000;Hook et al 2001;Krivickas et al 2001) but whether these changes are directly responsible for an age-related increase in damage is unknown. Alternatively, desmin, titin, myosin light chain 2, tropomyosin, and α-actinin covary (either in concentration or isoform expression) with fiber MHC isoform content (Prado et al 2005;Chopard et al 2001;Schiaffino and Reggiani 1996) and have all been implicated in contraction-induced muscle injury (Meyer et al 2010;Lieber et al 1996;Koh and Escobedo 2004;Zhang et al 2008;Lehti et al 2007;Belcastro 1993;Childers and McDonald 2004).…”

Section: Discussionmentioning

confidence: 99%

“…The latter includes fiber loss and atrophy (Larsson et al 1979;Sato et al 1984;Lexell et al 1988), impairments in the excitation-contraction process (Delbono et al 1995;Wang et al 2002), and perturbations to actomyosin cross-bridge function (Larsson et al 1997; Thompson and Brown 1999;Lowe et al 2001;Frontera et al 2000;Hook et al 2001;Krivickas et al 2001). These factors are specific to the mode of muscle contraction, impacting force during isometric and shortening contractions but having much less effect on force during lengthening or eccentric, muscular activity (Porter et al 1997;Poulin et al 1992;Phillips et al 1991;Ochala et al 2006;Hortobagyi et al 1995).…”

Section: Introductionmentioning

confidence: 99%

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Eccentric contraction-induced injury to type I, IIa, and IIa/IIx muscle fibers of elderly adults

Choi

Lim

Nibaldi

et al. 2011

AGE

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Muscles of old laboratory rodents experience exaggerated force losses after eccentric contractile activity. We extended this line of inquiry to humans and investigated the influence of fiber myosin heavy chain (MHC) isoform content on the injury process. Skinned muscle fiber segments, prepared from vastus lateralis biopsies of elderly men and women (78± 2 years, N=8), were subjected to a standardized eccentric contraction (strain, 0.25 fiber length; velocity, 0.50 unloaded shortening velocity). Injury was assessed by evaluating pre-and post-eccentric peak Ca 2+ -activated force per fiber cross-sectional area (F max ). Over 90% of the variability in post-eccentric F max could be explained by a multiple linear regression model consisting of an MHC-independent slope, where injury was directly related to pre-eccentric F max , and MHC-dependent y-intercepts, where the susceptibility to injury could be described as type IIa/IIx fibers>type IIa fibers>type I fibers. We previously reported that fiber type susceptibility to the same standardized eccentric protocol was type IIa/IIx>type IIa=type I for vastus lateralis fibers of 25-year-old adults (Choi and Widrick, Am J Physiol Cell Physiol 299:C1409-C1417, 2010). Modeling combined data sets revealed significant age by fiber type interactions, with posteccentric F max deficits greater for type IIa and type IIa/ IIx fibers from elderly vs. young subjects at constant pre-eccentric F max . We conclude that the resistance of the myofilament lattice to mechanical strain has deteriorated for type IIa and type IIa/IIx, but not for type I, vastus lateralis fibers of elderly adults.

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Section: Discussionsupporting

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Eccentric contraction-induced injury to type I, IIa, and IIa/IIx muscle fibers of elderly adults

Choi

Lim

Nibaldi

et al. 2011

AGE

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“…Similarly, in the present study we found that IIX fibers did not have age-related contractile decrements. Fiber segments studied from human quadriceps muscle biopsies show consistent slowing of V 0 with age (D'Antona et al, 2003;Krivickas et al, 2001;Larsson et al, 1997). Despite some discrepancies, overall there is a consensus that, at the cellular level, muscle shortening velocity is slowed with aging.…”

Section: Discussionmentioning

confidence: 96%

“…At the cellular level, maximal unloaded shortening velocity (V 0 ) is slower in muscle fibers from aged individuals relative to fibers from younger individuals (D'Antona et al, 2003;Degens et al, 1998;Krivickas et al, 2001;Larsson et al, 1997;Li and Larsson, 1996;Thompson, 1999;Thompson and Brown, 1999). It is well known that shortening velocity is directly related to, and dependent upon, Ca 2+ -activated myosin ATPase activity (Barany, 1967;Reiser et al, 1985).…”

Section: Introductionmentioning

confidence: 99%

Myofibrillar myosin ATPase activity in hindlimb muscles from young and aged rats

Lowe

Husom

Ferrington

et al. 2004

Mechanisms of Ageing and Development

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We tested the hypothesis that Ca 2+ -activated myosin ATPase activity is lower in muscles of aged rats relative to muscles of young rats, independent of changes in myosin isoform expression. Myofibrils were prepared from permeabilized fibers of soleus, plantaris, and semimembranosus muscles of young (8-12 months) and aged (32-38 months) F344 × BN rats and assayed for resting myosin ATPase, Ca 2+ -activated myosin ATPase, and myosin heavy chain (MHC) and myosin light chain (MLC) isoform compositions. Resting myosin ATPases were not affected by age in any muscle (P ≥ 0.42). Ca 2+ -activated myosin ATPases of soleus and plantaris myofibrils were not affected by age (P ≥ 0.31) but were 16% lower in semimembranosus myofibrils from aged rats (0.448 ± 0.019 μmol P i /min/mg) compared to young rats (0.533 ± 0.031 μmol P i /min/mg; P = 0.03). Correspondingly, maximal unloaded shortening velocity of single semimembranosus fibers from aged rats was slow (4.6 ± 0.2 fiber lengths/s) compared with fibers from young rats (5.8 ± 0.3 fiber lengths/s; P < 0.01). No age-related changes in MHC or regulatory MLC isoforms were detected in any muscle (P ≥ 0.08) but changes in the essential MLC occurred in plantaris and semimembranosus muscles. The data indicate that Ca 2+ -activated myosin ATPase activity is reduced with age in semimembranosus muscle, independent of age-related changes in MHC isoform expression, and is one mechanism contributing to age-related slowing of contraction in that muscle.

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Sex differences in skeletal muscle fiber types: A meta‐analysis

Nuzzo

2023

Clinical Anatomy

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Biopsies have been acquired from living men and women to determine proportions of Type I (slow‐twitch) and II (fast‐twitch) skeletal muscle fibers since the 1970s. Sex differences have been assumed but the literature has not been submitted to meta‐analysis. Here, the aim was to generate effect sizes of sex differences in muscle fiber cross‐sectional areas, distribution percentages, and area percentages. Data from 2875 men and 2452 women, who participated in 110 studies, were analyzed. Myofibrillar adenosine triphosphatase histochemistry was used in 71.8% of studies to classify fibers as Type I, II, IIA, and/or IIX; immunohistochemistry, immunofluorescence, or sodium dodecyl sulfate‐polyacrylamide gel electrophoresis were used in 35.4% of studies to similarly classify myosin heavy chain (MHC) isoform content. Most studies involved biopsies from vastus lateralis (79.1%) in healthy individuals (92.7%) between 18 and 59 years old (80.9%). Men exhibited greater cross‐sectional areas for all fiber types (g = 0.40–1.68); greater distribution percentages for Type II, MHC II, IIA, IIX fibers (g = 0.26–0.34); greater area percentages for Type II, IIA, MHC IIA, IIX fibers (g = 0.39–0.93); greater Type II/I and Type IIA/I fiber area ratios (g = 0.63, 0.94). Women exhibited greater Type I and MHC I distribution percentages (g = −0.13, −0.44); greater Type I and MHC I area percentages (g = −0.53, −0.69); greater Type I/II fiber area ratios (g = −1.24). These data, which represent the largest repository of comparative muscle fiber type data from living men and women, can inform discussions about biological sex and its impact on pathologies and sports performance (e.g., explaining sex differences in muscle strength and muscle endurance).

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Age- and Gender-Related Differences in Maximum Shortening Velocity of Skeletal Muscle Fibers

Abstract: Both age and gender affect Vo. Age- and gender-related differences in Vo may partially explain the impairments in muscle function that occur with aging and the greater impairment in muscle function observed in OW compared with that observed in OM.

Cited by 128 publications

References 33 publications

Eccentric contraction-induced injury to type I, IIa, and IIa/IIx muscle fibers of elderly adults

Eccentric contraction-induced injury to type I, IIa, and IIa/IIx muscle fibers of elderly adults

Myofibrillar myosin ATPase activity in hindlimb muscles from young and aged rats

Sex differences in skeletal muscle fiber types: A meta‐analysis

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