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α7B Integrin changes in mdx mouse muscles after l ‐arginine administration
Author(s) -
Chazalette Delphine,
Hnia Karim,
Rivier François,
Hugon Gérald,
Mornet Dominique
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.12.081
Subject(s) - dystrophin , integrin , laminin , utrophin , basal lamina , arginine , protein subunit , mdx mouse , diaphragm (acoustics) , chemistry , basal (medicine) , microbiology and biotechnology , duchenne muscular dystrophy , medicine , endocrinology , biology , anatomy , biochemistry , extracellular matrix , gene , receptor , ultrastructure , amino acid , acoustics , loudspeaker , physics , insulin
Muscle fibers attach to laminin in the basal lamina using two mechanisms, i.e., dystrophin with its associated proteins and α7β1 integrin. In humans, gene‐mutation defects in one member of these complexes result in muscular dystrophies. This study revealed changes after l ‐arginine treatment of utrophin‐associated proteins and the α7B integrin subunit in mdx mouse, a dystrophin‐deficient animal model. In the two studied muscles (cardiac muscle and diaphragm), the α7B integrin subunit was increased in 5‐week‐old treated mice. Interestingly, the diaphragm histopathological appearance was significantly improved by l ‐arginine administration. These results highlight a possible way to compensate for dystrophin deficiency via α7β1 integrin.