Muscle Mechanics: Adaptations with Exercise-Training

Document Type

Article

Publication Date

1-1996

Publisher

Lippincott Williams and Wilkins

Source Publication

Exercise and Sport Sciences Reviews

Source ISSN

0091-6331

Abstract

Muscle mechanics can be defined as the basic functional properties of muscles that allows them to produce movements with a characteristic force, velocity, and power. Understanding these properties and how they adapt to programs of regular exercise is essential if we hope to optimize human performance, and delay the deterioration of performance associated with the aging process. Although the basic functional properties of limb skeletal muscle have been known for some time [26], a few of the important cellular and molecular mechanisms of contraction are still not fully elucidated [42, 72, 89, 107, 122]. In particular, the processes of excitation-contraction (E-C) coupling, whereby the depolarization of the surface (sarcolemma) and t-tubular membranes leads to the release of Ca2+ from the adjacent terminal cisternae region of the sarcoplasmic reticulum (SR), and the interaction of the contractile proteins actin and myosin with the subsequent generation of force and filament movement (cross-bridge kinetics) are two important muscle cell functions for which we currently lack a complete understanding. Nevertheless, in recent years, considerable progress has been made in these fields, and a complete understanding of these processes appears eminent [72, 107]. In this chapter, it is our intent to review the isometric and isotonic contractile properties of limb skeletal muscle and, to whatever extent possible, to discuss the underlying cellular mechanisms. A second objective is to provide a summary of the published data concerning how the mechanical properties of muscle adapt to various programs of regular exercise-training. We will not discuss muscle fatigue in any detail, as this topic has recent been reviewed [44].

Comments

Exercise and Sport Sciences Reviews, Vol. 24, No. 1 (1996): 427-473. Publisher link.

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