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JCS ePress online publication date 9 May 2006
doi: 10.1242/jcs.02952

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Research Article

Severe muscular dystrophy in mice that lack dystrophin and {alpha}7 integrin


Jachinta E. Rooney, Jennifer V. Welser, Melissa A. Dechert, Nichole L. Flintoff-Dye, Stephen J. Kaufman, and Dean J. Burkin*
* Author for correspondence (e-mail: dburkin{at}med.unr.edu)

The dystrophin glycoprotein complex links laminin in the extracellular matrix to the cell cytoskeleton. Loss of dystrophin causes Duchenne muscular dystrophy, the most common human X-chromosome-linked genetic disease. The {alpha}7{beta}1 integrin is a second transmembrane laminin receptor expressed in skeletal muscle. Mutations in the {alpha}7 integrin gene cause congenital myopathy in humans and mice. The {alpha}7{beta}1 integrin is increased in the skeletal muscle of Duchenne muscular dystrophy patients and mdx mice. This observation has led to the suggestion that dystrophin and {alpha}7{beta}1 integrin have complementary functional and structural roles. To test this hypothesis, we generated mice lacking both dystrophin and {alpha}7 integrin (mdx/{alpha}7-/-). The mdx/{alpha}7-/- mice developed early-onset muscular dystrophy and died at 2-4 weeks of age. Muscle fibers from mdx/{alpha}7-/- mice exhibited extensive loss of membrane integrity, increased centrally located nuclei and inflammatory cell infiltrate, greater necrosis and increased muscle degeneration compared to mdx or {alpha}7-integrin null animals. In addition, loss of dystrophin and/or {alpha}7 integrin resulted in altered expression of laminin-{alpha}2 chain. These results point to complementary roles for dystrophin and {alpha}7{beta}1 integrin in maintaining the functional integrity of skeletal muscle.


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© The Company of Biologists Ltd 2006