Effects of altered loading states on muscle plasticity: what have we learned from rodents?

This paper summarizes the key findings concerning the adaptive properties of rodent muscle in response to altered loading states. When the mechanical stress on the muscle is chronically increased, the muscle adapts by hypertrophying its fibers. This response is regulated by processes resulting in contractile protein expression reflecting slower phenotypes, thereby enabling the muscle to better support load-hearing activity. In contrast, reducing the load-bearing activity induces an opposite response whereby muscles used for both antigravity function and locomotion atrophy while transforming some of the slow fibers into faster contractile phenotypes. Accompanying the atrophy is both a reduced power generating and activity sustaining capability. These adaptive processes are regulated by both transcriptional and translational processes. Available evidence further suggests that the interaction of heavy resistance activity and hormonal/growth factors (insulin-like growth factor, growth hormone, glucocorticoids, etc.) are critical in the maintenance of muscle mass and function. Also resistance training, in contrast to other activities such as endurance running, provides a more economical form of stress because less mechanical activity is required to maintain muscle homeostasis in the context of chronic states of weightlessness.

[1]  V J Caiozzo,et al.  Microgravity-induced transformations of myosin isoforms and contractile properties of skeletal muscle. , 1996, Journal of applied physiology.

[2]  V J Caiozzo,et al.  Influence of mechanical loading on myosin heavy-chain protein and mRNA isoform expression. , 1996, Journal of applied physiology.

[3]  V. Mukku,et al.  Stimulation of myofibrillar protein synthesis in hindlimb suspended rats by resistance exercise and growth hormone. , 1995, Life sciences.

[4]  F. Haddad,et al.  Pressure-induced regulation of myosin expression in rodent heart. , 1995, Journal of applied physiology.

[5]  S. Swoap,et al.  Interaction of thyroid hormone and functional overload on skeletal muscle isomyosin expression , 1994 .

[6]  C. Reggiani,et al.  Myosin isoforms in mammalian skeletal muscle. , 1994, Journal of applied physiology.

[7]  K M Baldwin,et al.  Effect of spaceflight on skeletal muscle: mechanical properties and myosin isoform content of a slow muscle. , 1994, Journal of applied physiology.

[8]  M. Lango,et al.  Induction of Myocardial Insulin‐Like Growth Factor‐I Gene Expression in Left Ventricular Hypertrophy , 1994, Circulation.

[9]  D. Desplanches,et al.  Effects of adrenalectomy or RU-486 on rat muscle fibers during hindlimb suspension. , 1993, Journal of applied physiology.

[10]  F. Haddad,et al.  Myosin heavy chain expression in rodent skeletal muscle: effects of exposure to zero gravity. , 1993, Journal of applied physiology.

[11]  K M Baldwin,et al.  Substrate oxidation capacity in rodent skeletal muscle: effects of exposure to zero gravity. , 1993, Journal of applied physiology.

[12]  K M Baldwin,et al.  Activity-induced regulation of myosin isoform distribution: comparison of two contractile activity programs. , 1993, Journal of applied physiology.

[13]  S. Kandarian,et al.  Regulation of skeletal muscle dihydropyridine receptor gene expression by biomechanical unloading. , 1992, Journal of applied physiology.

[14]  K M Baldwin,et al.  Effects of zero gravity on myofibril content and isomyosin distribution in rodent skeletal muscle , 1990, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[15]  R. Herrick,et al.  Time course adaptations in rat skeletal muscle isomyosins during compensatory growth and regression. , 1987, Journal of applied physiology.

[16]  R. Herrick,et al.  Subunit composition of rodent isomyosins and their distribution in hindlimb skeletal muscles. , 1987, Journal of applied physiology.

[17]  K M Baldwin,et al.  Activity influences on soleus muscle myosin during rodent hindlimb suspension. , 1987, Journal of applied physiology.

[18]  V. Edgerton,et al.  Biochemical and physiological changes in overloaded rat fast- and slow-twitch ankle extensors. , 1985, Journal of applied physiology.

[19]  E. Noble,et al.  Protein synthesis in compensatory hypertrophy of rat plantaris. , 1984, Canadian journal of physiology and pharmacology.

[20]  R. Roy,et al.  Biochemical properties of overloaded fast-twitch skeletal muscle. , 1982, Journal of applied physiology: respiratory, environmental and exercise physiology.

[21]  R. Herrick,et al.  Effect of functional overload on substrate oxidation capacity of skeletal muscle. , 1981, Journal of applied physiology: respiratory, environmental and exercise physiology.

[22]  W. Cheadle,et al.  Effect of functional overload on enzyme levels in different types of skeletal muscle. , 1977, Journal of applied physiology: respiratory, environmental and exercise physiology.

[23]  F. Booth,et al.  Atrophy of the soleus muscle by hindlimb unweighting. , 1990, Journal of applied physiology.