TY - JOUR
T1 - Skeletal muscle adaptations with age, inactivity, and therapeutic exercise
AU - Thompson, La Dora V.
PY - 2002
Y1 - 2002
N2 - One of the remarkable features of skeletal muscle is its adaptability. Skeletal muscle adaptations are characterized by modifications of morphological, biochemical, and molecular variables that alter the functional attributes of specific skeletal muscle fiber types. Skeletal muscle adaptation is diverse and the magnitude of change is dependent on many factors, such as activity pattern, age, and muscle fiber type composition. The adaptation of skeletal muscle in the adult population is well described. In contrast, the adaptation of skeletal muscle in the older population is less documented, especially in the area of inactivity-induced alterations. Age-related changes in skeletal muscle may play a significant role in the magnitude of change with inactivity and influence the rehabilitation process for the older adult. A consistent feature of age and inactivity is limb muscle atrophy and the loss of peak force and power. Differences exist in the rate and mechanisms of muscle wasting and in the susceptibility of a given fiber type to atrophy. Most likely, the rapid muscle wasting might be in part due to a decrease in protein synthesis coupled with an increased degradation. Besides the quantitative change in muscle mass, age and inactivity induce important qualitative changes in the structure of key skeletal muscle proteins that are manifested in alterations in contractile properties. Therefore, the purpose of this clinical commentary is to identify the major effects of age and inactivity on skeletal muscle structure and function, and discuss potential therapeutic interventions. Special emphasis will be placed on how alterations in muscle structure affect function and on the cellular and molecular mechanisms of the age-related and inactivity-induced muscle changes.
AB - One of the remarkable features of skeletal muscle is its adaptability. Skeletal muscle adaptations are characterized by modifications of morphological, biochemical, and molecular variables that alter the functional attributes of specific skeletal muscle fiber types. Skeletal muscle adaptation is diverse and the magnitude of change is dependent on many factors, such as activity pattern, age, and muscle fiber type composition. The adaptation of skeletal muscle in the adult population is well described. In contrast, the adaptation of skeletal muscle in the older population is less documented, especially in the area of inactivity-induced alterations. Age-related changes in skeletal muscle may play a significant role in the magnitude of change with inactivity and influence the rehabilitation process for the older adult. A consistent feature of age and inactivity is limb muscle atrophy and the loss of peak force and power. Differences exist in the rate and mechanisms of muscle wasting and in the susceptibility of a given fiber type to atrophy. Most likely, the rapid muscle wasting might be in part due to a decrease in protein synthesis coupled with an increased degradation. Besides the quantitative change in muscle mass, age and inactivity induce important qualitative changes in the structure of key skeletal muscle proteins that are manifested in alterations in contractile properties. Therefore, the purpose of this clinical commentary is to identify the major effects of age and inactivity on skeletal muscle structure and function, and discuss potential therapeutic interventions. Special emphasis will be placed on how alterations in muscle structure affect function and on the cellular and molecular mechanisms of the age-related and inactivity-induced muscle changes.
KW - Contractile properties
KW - Fiber types
KW - Hindlimb unweighting
KW - Myosin heavy chain isoforms
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U2 - 10.2519/jospt.2002.32.2.44
DO - 10.2519/jospt.2002.32.2.44
M3 - Review article
C2 - 11838580
AN - SCOPUS:0036154825
VL - 32
SP - 44
EP - 57
JO - Journal of Orthopaedic and Sports Physical Therapy
JF - Journal of Orthopaedic and Sports Physical Therapy
SN - 0190-6011
IS - 2
ER -