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First published online May 28, 2005
doi: 10.1242/10.1242/jcs.02368
Research Article |
1 Department of Pathology and Laboratory Medicine, St Paul's Hospital/Providence Health Care, University of British Columbia, 1081 Burrard Street, Vancouver, BC V6Z 1Y6, Canada
2 Department of Medicine, St Paul's Hospital/Providence Health Care, University of British Columbia, 1081 Burrard Street, Vancouver, BC V6Z 1Y6, Canada
3 James Hogg iCAPTURE Centre for Cardiovascular and Pulmonary Research, St Paul's Hospital/Providence Health Care, University of British Columbia, 1081 Burrard Street, Vancouver, BC V6Z 1Y6, Canada
* Author for correspondence (e-mail: cseow{at}mrl.ubc.ca)
Accepted 9 March 2005
Smooth muscle cells line the walls of hollow organs and control the organ dimension and mechanical function by generating force and changing length. Although significant progress has been made in our understanding of the molecular mechanism of actomyosin interaction that produces sliding of actin (thin) and myosin (thick) filaments in smooth muscle, the sarcomeric structure akin to that in striated muscle, which allows the sliding of contractile filaments to be translated into cell shortening has yet to be elucidated. Here we show evidence from porcine airway smooth muscle that supports a model of malleable sarcomeric structure composed of contractile units assembled in series and in parallel. The geometric organization of the basic building blocks (contractile units) within the assembly and the dimension of individual contractile units can be altered when the muscle cells adapt to different lengths. These structural alterations can account for the different length-force relationships of the muscle obtained at different adapted cell lengths. The structural malleability necessary for length adaptation precludes formation of a permanent filament lattice and explains the lack of aligned filament arrays in registers, which also explains why smooth muscle is `smooth'.
Key words: Isotonic shortening, Plasticity, Contraction mechanism, Length adaptation, Ultrastructure
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