Absence of α7 integrin in dystrophin-deficient mice causes a myopathy similar to Duchenne muscular dystrophy

C Guo, M Willem, A Werner, G Raivich… - Human molecular …, 2006 - academic.oup.com
C Guo, M Willem, A Werner, G Raivich, M Emerson, L Neyses, U Mayer
Human molecular genetics, 2006academic.oup.com
Both the dystrophin–glycoprotein complex and α7β1 integrin have critical roles in the
maintenance of muscle integrity via the provision of mechanical links between muscle fibres
and the basement membrane. Absence of either dystrophin or α7 integrin results in a
muscular dystrophy. To clarify the role of α7 integrin and dystrophin in muscle development
and function, we generated integrin α7/dystrophin double-mutant knockout (DKO) mice.
Surprisingly, DKO mice survived post-natally and were indistinguishable from wild-type …
Abstract
Both the dystrophin–glycoprotein complex and α7β1 integrin have critical roles in the maintenance of muscle integrity via the provision of mechanical links between muscle fibres and the basement membrane. Absence of either dystrophin or α7 integrin results in a muscular dystrophy. To clarify the role of α7 integrin and dystrophin in muscle development and function, we generated integrin α7/dystrophin double-mutant knockout (DKO) mice. Surprisingly, DKO mice survived post-natally and were indistinguishable from wild-type, integrin α7-deficient and mdx mice at birth, but died within 24–28 days. Histological analysis revealed a severe muscular dystrophy in DKO mice with endomysial fibrosis and ectopic calcification. Weight loss was correlated with the loss of muscle fibres, indicating that progressive muscle wasting in the double mutant was most likely due to inadequate muscle regeneration. The data further support that premature death of DKO mice is due to cardiac and/or respiratory failure. The integrin α7/dystrophin-deficient mouse model, therefore, resembles the pathological changes seen in Duchenne muscular dystrophy and suggests that the different clinical severity of dystrophin deficiency in human and mouse may be due to a fine-tuned difference in expression of dystrophin and integrin α7 in both species. Together, these findings indicate an essential role for integrin α7 in the maintenance of dystrophin-deficient muscles.
Oxford University Press