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Am J Physiol Cell Physiol 284: C962-C968, 2003; doi:10.1152/ajpcell.00326.2002
0363-6143/03 $5.00
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Vol. 284, Issue 4, C962-C968, April 2003

Altered muscle force and stiffness of skeletal muscles in alpha -sarcoglycan-deficient mice

Nisha D. Patel, Suneal R. Jannapureddy, Willy Hwang, Imran Chaudhry, and Aladin M. Boriek

Department of Medicine, Baylor College of Medicine, Houston, Texas 77030

alpha -Sarcoglycan (ASG) is a transmembrane protein of the dystrophin-associated complex, and absence of ASG causes limb-girdle muscular dystrophy. We hypothesize that disruption of the sarcoglycan complex may alter muscle extensibility and disrupt the coupling between passive transverse and axial contractile elements in the diaphragm. We determined the length-tension relationships of the diaphragm of young ASG-deficient mice and their controls during uniaxial and biaxial loading. We also determined the isometric contractile properties of the diaphragm muscles from mutant and normal mice in the absence and presence of passive transverse stress. We found that the diaphragm muscles of the null mutants for the protein ASG show 1) significant decrease in muscle extensibility in the directions of the muscle fibers and transverse to fibers, 2) significant reductions in force-generating capacity, and 3) significant reductions in coupling between longitudinal and transverse properties. Thus these findings suggest that the sarcoglycan complex serves a mechanical function in the diaphragm by contributing to muscle passive stiffness and to the modulation of the contractile properties of the muscle.

diaphragm mechanics; force transmission; mechanics of breathing; respiratory muscle mechanics; transmembrane proteins


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