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Am J Physiol Cell Physiol (January 18, 2006). doi:10.1152/ajpcell.00317.2005
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Submitted on July 1, 2005
Accepted on January 11, 2006

{alpha}7{beta}1 Integrin Regulates Mechanotransduction and Prevents Skeletal Muscle Injury

Marni D Boppart1, Dean J Burkin2, and Stephen J Kaufman1*

1 Cell and Developmental Biology, University of Illinois, Urbana, IL, USA
2 Cell and Developmental Biology, University of Illinois, Urbana, IL, USA; Pharmacology, University of Nevada, Reno, NV, USA

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

{alpha}7{beta}1 integrin links laminin in the extracellular matrix with the cell cytoskeleton and therein mediates transduction of mechanical forces into chemical signals. Muscle contraction and stretching ex vivo result in activation of intracellular signaling molecules that are integral to post-exercise injury responses. Since {alpha}7{beta}1 integrin stabilizes muscle and provides communication between the matrix and cytoskeleton, the role of this integrin in exercise-induced cell signaling and skeletal muscle damage was assessed in wildtype and transgenic mice over-expressing the {alpha}7BX2 chain. We report here that increasing {alpha}7{beta}1 integrin inhibits phosphorylation of molecules associated with muscle damage, including the mitogen-activated protein kinases (JNK, p38, and ERK), following downhill running. Likewise, activation of molecules associated with hypertrophy (AKT, mTOR, p70S6k) was diminished in mice over-expressing integrin. Whereas exercise resulted in Evans blue dye positive fibers, an index of muscle damage, increased integrin protected mice from injury. Moreover, exercise leads to an increase in {alpha}7{beta}1 protein. These experiments provide the first evidence that {alpha}7{beta}1 integrin is a negative regulator of mechanotransduction in vivo and provides resistance to exercise-induced muscle damage.




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