Immunocytochemical studies of aquaporin 4 in the skeletal muscle of mdx mouse.

Immunostainability of anti aquaporin 4 antiserum was investigated in the muscles of dystrophin deficient mdx mice. Western blot analysis showed that the rabbit antiserum against aquaporin 4 reacted with a 28 kDa protein in extracts of normal mouse quadriceps femoris muscles but did not react with the protein in extracts of quadriceps femoris muscles of mdx mice. Immunoperoxidase staining of the muscles from normal and mdx mice revealed the positive immunoreaction at the myofiber surface of normal mice and the negative, or the faint and discontinuous immunostaining at the surface of mdx myofibers. Immunogold electron microscopy disclosed the localization of aquaporin 4 molecules at the myofiber plasma membranes of normal mice and the localization was consistent with that of orthogonal array particles in the protoplasmic face of normal muscle plasma membrane seen in freeze fracture replicas. This study demonstrated that the density of aquaporin 4 molecules was decreased in the muscle plasma membranes of mdx mice, resulting in the faulty function of mdx myofibers.