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Am J Physiol Cell Physiol (April 3, 2002). doi:10.1152/ajpcell.00529.2001
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Articles in PresS, published online ahead of print April 3, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00529.2001
Submitted on November 6, 2001
Accepted on March 27, 2002

The dystrophin-glycoprotein complex and Ras and Rho GTPases signaling are altered in muscle atrophy

Priya Sethu Chockalingam1, Rushina Cholera2, Shilpa A. Oak1, Yi Zheng1, Harry W. Jarrett1*, and Donald B. Thomason2

1 Molecular Science, University Tennessee Health Science Center, Memphis, TN, USA
2 Physiology, University Tennessee Health Science Center, Memphis, TN, USA

* To whom correspondence should be addressed. E-mail: hjarrett{at}utmem.edu.

The dystrophin-glycoprotein complex (DGC) is a sarcolemmal complex whose defects cause muscular dystrophies. The normal function of this complex is not clear. We have proposed that this is a signal transduction complex, signaling normal interactions with matrix laminin and the response is normal growth and homeostasis. If so, the complex and its signaling should be altered in other physiological states such as atrophy. The amount of some of the dystrophin-glycoprotein complex proteins, including dystrophin, ß-dystroglycan, and {alpha}-sarcoglycan, is reduced significantly in rat skeletal muscle atrophy induced by tenotomy. Furthermore, H-Ras, RhoA, and Cdc42 decrease in expression levels and activities in muscle atrophy. When the small GTPases were assayed after depleting laminin or ß-dystroglycan, H-Ras, Rac1 and Cdc42 activities were reduced, suggesting a physical linkage between the DGC and the GTPases. Dominant-negative Cdc42, introduced using a retroviral vector, resulted in muscle fiber diameters that resembled muscle atrophy. These data support a putative role for the DGC in transduction of mechanical signals in muscle.




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