Characterization of skeletal muscle in the synemin knock-out mouse

• Main Authors: García-Pelagio, Karla P, Joaquin, Muriel, Lovering, Richard M, Lund, Linda, Bond, Meredith, Bloch, Robert J
• Format: Conference Proceeding
• Language: English
• Subjects: Biomechanics; Cell membranes; Disks; Homology; Muscles; Musculoskeletal system; Proteins; Vinculin; Viscoelasticity
• ISSN: 0094-243X; 1551-7616
• DOI: 10.1063/1.4901362

Diseases linked to intermediate filament (IF) proteins are associated with defects in the organization of the contractile apparatus of skeletal and cardiac muscle and its links to costameres, which connect the sarcomeres to the cell membrane. Synemin is a large IF protein that associates with dystrobrevin, vinculin, and talin at costameres of the cell membrane of striated muscle, as well as with α-actinin and desmin at the Z disks. Synemin can be expressed in either 210 kDa α- or 180 kDa β- alternatively spliced forms. We generated mice null for synemin by homologous recombination to study synemin's function in skeletal muscle. Skeletal muscle in the knock out (syn KO) mouse does not make synemin mRNA or protein. Preliminary characterization of the syn KO mouse suggests that it has a mild skeletal muscle phenotype. The organization of costameres appears to be normal. Treadmill running uphill test results was not significantly affected when compared to controls at any age. More notably, the biomechanical properties of the cell membrane are different in the syn KO, though they are less affected than by the absence of desmin or dystrophin. These results suggest that the viscoelastic properties of the cell membrane-costamere-myofibril complex are significantly influenced by synemin.