Histochemical and biochemical changes in human skeletal muscle with age in sedentary males, age 22–65 years

Larsson, Lars; Sjödin, B.; Karlsson, Jan

doi:10.1111/j.1748-1716.1978.tb06187.x

Cited by 422 publications

(270 citation statements)

References 24 publications

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“…In agreement with many other studies,34, 35, 36 we found that the type II fibres were 18% smaller in muscles from the older participants than from the younger participants, while no such atrophy was observed for type I fibres. However, the similar average size of all fibres pooled in the old and the young participants and the greater variation in type I fibre size in the older participants suggest that the atrophy of type II fibres was accompanied by a concomitant (compensatory) hypertrophy, although not significant, of some type I fibres.…”

Section: Discussionsupporting

confidence: 93%

Coupling between skeletal muscle fiber size and capillarization is maintained during healthy aging

Barnouin

McPhee

Butler-Browne

et al. 2017

J cachexia sarcopenia muscle

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BackgroundAs muscle capillarization is related to the oxidative capacity of the muscle and the size of muscle fibres, capillary rarefaction may contribute to sarcopenia and functional impairment in older adults. Therefore, it is important to assess how ageing affects muscle capillarization and the interrelationship between fibre capillary supply with the oxidative capacity and size of the fibres.MethodsMuscle biopsies from healthy recreationally active young (22 years; 14 men and 5 women) and older (74 years; 22 men and 6 women) people were assessed for muscle capillarization and the distribution of capillaries with the method of capillary domains. Oxidative capacity of muscle fibres was assessed with quantitative histochemistry for succinate dehydrogenase (SDH) activity.ResultsThere was no significant age‐related reduction in muscle fibre oxidative capacity. Despite 18% type II fibre atrophy (P = 0.019) and 23% fewer capillaries per fibre (P < 0.002) in the old people, there was no significant difference in capillary distribution between young and old people, irrespective of sex. The capillary supply to a fibre was primarily determined by fibre size and only to a small extent by oxidative capacity, irrespective of age and sex. Based on SDH, the maximal oxygen consumption supported by a capillary did not differ significantly between young and old people.ConclusionsThe similar quantitative and qualitative distribution of capillaries within muscle from healthy recreationally active older people and young adults indicates that the age‐related capillary rarefaction, which does occur, nevertheless maintains the coupling between skeletal muscle fibre size and capillarization during healthy ageing.

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Section: Discussionsupporting

confidence: 93%

Coupling between skeletal muscle fiber size and capillarization is maintained during healthy aging

Barnouin

McPhee

Butler-Browne

et al. 2017

J cachexia sarcopenia muscle

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“…Preferential atrophy and loss of fast‐twitch fibers increase the ratio of slow‐twitch fibers to total fibers in aging muscle (Deschenes, Gaertner, & O'Reilly, 2013; Larsson, Sjödin, & Karlsson, 1978). We performed slow myosin heavy chain (sMHC) staining on cross sections of soleus muscle and found that the percentage of sMHC+ fibers/total fibers increased in wild‐type mice from 10 to 20 months of age.…”

Section: Resultsmentioning

confidence: 99%

Myeloid cell‐derived tumor necrosis factor‐alpha promotes sarcopenia and regulates muscle cell fusion with aging muscle fibers

et al. 2018

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Sarcopenia is age‐related muscle wasting that lacks effective therapeutic interventions. We found that systemic ablation of tumor necrosis factor‐α (TNF‐α) prevented sarcopenia and prevented age‐related change in muscle fiber phenotype. Furthermore, TNF‐α ablation reduced the number of satellite cells in aging muscle and promoted muscle cell fusion in vivo and in vitro. Because CD68+ macrophages are important sources of TNF‐α and the number of CD68+ macrophages increases in aging muscle, we tested whether macrophage‐derived TNF‐α affects myogenesis. Media conditioned by TNF‐α‐null macrophages increased muscle cell fusion in vitro, compared to media conditioned by wild‐type macrophages. In addition, transplantation of bone marrow cells from wild‐type mice into TNF‐α‐null recipients increased satellite cell numbers and reduced numbers of centrally nucleated myofibers, indicating that myeloid cell‐secreted TNF‐α reduces muscle cell fusion. Transplanting bone marrow cells from wild‐type mice into TNF‐α‐null recipients also increased sarcopenia, although transplantation did not restore the age‐related change in muscle fiber phenotype. Collectively, we show that myeloid cell‐derived TNF‐α contributes to muscle aging by affecting sarcopenia and muscle cell fusion with aging muscle fibers. Our findings also show that TNF‐α that is intrinsic to muscle and TNF‐α secreted by immune cells work together to influence muscle aging.

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“…Analyses from human muscle biopsy samples have consistently demonstrated that type II fibers are more susceptible to aging-related atrophy when compared to type I fibers [3,50]. Doherty [51] reported that the loss of type II fiber area was 20-50%, whereas type I area loss was much less (1-25%).…”

Section: Type II Muscle Fibers and Agingmentioning

confidence: 99%

“…Although this phenomenon is well documented in animal and human studies, the underlying mechanisms leading to sarcopenia remain to be fully elucidated. The contributing mechanism(s) leading to sarcopenia are multi-factorial and may include: denervation and reinnervation of motor units, especially within skeletal muscles composed of a high degree of type II muscle fibers [1][2][3]; an alteration in the hormonal milieu in which anabolic hormone concentrations progressively decline [4,5]; elevated concentrations of inflammatory mediators that are not only associated with disease states, but also occur in healthy older adults [6][7][8][9][10][11][12][13]; and myonuclear loss through apoptotic mechanisms [14][15][16][17][18][19].…”

Section: Introductionmentioning

confidence: 99%

Death receptor-associated pro-apoptotic signaling in aged skeletal muscle

2006

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Tumor necrosis factor-alpha (TNF-α) is elevated in the serum as a result of aging and it promotes pro-apoptotic signaling upon binding to the type I TNF receptor. It is not known if activation of this apoptotic pathway contributes to the well-documented age-associated decline in muscle mass (i.e. sarcopenia). We tested the hypothesis that skeletal muscles from aged rodents would exhibit elevations in markers involved in the extrinsic apoptotic pathway when compared to muscles from young adult rodents, thereby contributing to an increased incidence of nuclear apoptosis in these muscles. The plantaris (fast) and soleus (slow) muscles were studied in young adult (5-7 mo, n = 8) and aged (33 mo, n = 8) Fischer 344 × Brown Norway rats. Muscles from aged rats were significantly smaller while exhibiting a greater incidence of apoptosis. Furthermore, muscles from aged rats had higher type I TNF receptor and Fas associated death domain protein (FADD) mRNA, protein contents for FADD, BCL-2 Interacting Domain (Bid), FLICE-inhibitory protein (FLIP), and enzymatic activities of caspase-8 and caspase-3 than muscles from young adult rats. Significant correlations were observed in the plantaris muscle between caspase activity and muscle weight and the apoptotic index, while similar relationships were not found in the soleus. These data demonstrate that pro-apoptotic signaling downstream of the TNF receptor is active in aged muscles. Furthermore, our data extend the previous demonstration that type II fibers are preferentially affected by aging and support the hypothesis that type II fiber containing skeletal muscles may be more susceptible to muscle mass loses via the extrinsic apoptotic pathway.

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Histochemical and biochemical changes in human skeletal muscle with age in sedentary males, age 22–65 years

Cited by 422 publications

References 24 publications

Coupling between skeletal muscle fiber size and capillarization is maintained during healthy aging

Coupling between skeletal muscle fiber size and capillarization is maintained during healthy aging

Myeloid cell‐derived tumor necrosis factor‐alpha promotes sarcopenia and regulates muscle cell fusion with aging muscle fibers

Death receptor-associated pro-apoptotic signaling in aged skeletal muscle

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