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OCCASIONAL REVIEW |
1 Hospital S Biagio, Department of Pneumology, Alessandria, Italy
2 Department of Experimental Medicine, Human Physiology Unit, University of Pavia, Pavia, Italy
3 Department of Anatomy and Physiology, University of Padova, Padova, Italy
Correspondence to:
Correspondence to:
Dr B Polla
Hospital S Biagio, Department of Pneumology, Alessandria, Italy; bpolla{at}ospedale.al.it
Skeletal muscles are composed of fibres of different types, each type being identified by the isoform of myosin heavy chain which is expressed as slow 1, fast 2A, fast 2X, and fast 2B. Slow fibres are resistant to fatigue due to their highly oxidative metabolism whereas 2X and 2B fibres are easily fatiguable and fast 2A fibres exhibit intermediate fatigue resistance. Slow fibres and fast fibres are present in equal proportions in the adult human diaphragm while intercostal muscles contain a higher proportion of fast fibres. A small fibre size, abundance of capillaries, and a high aerobic oxidative enzyme activity are typical features of diaphragm fibres and give them the resistance to fatigue required by their continuous activity. Because of their fibre composition, intercostal muscles are less resistant to fatigue. The structural and functional characteristics of respiratory muscle fibres are not fixed, however, and can be modified in response to several physiological and pathological conditions such as training (adaptation to changes in respiratory load), adaptation to hypoxia, age related changes, and changes associated with respiratory diseases. The properties of respiratory muscle fibres can also be modified by pharmacological agents such as ß2 agonists and corticosteroids used for the treatment of respiratory diseases.
Keywords: respiratory muscles; myosin isoforms; diaphragm
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