Some characteristics of a novel 550-kDa protein which is abundant in skeletal muscle tissues at an early stage of the chick embryo, and localized in the peripheries of adult muscle fibers and at the Z-disks of isolated myofibrils, was investigated. A cosedimentation experiment and solid phase immunoabsorbent assay showed that the 550-kDa protein binds directly to F-actin. Therefore, it is concluded that the 550-kDa protein is a novel actin-binding protein. The 550-kDa protein was also interacted with α-actinin, laminin, fibronectin and Type IV collagen. Reactions with several kinds of lectin revealed that the 550-kDa protein is a glycoprotein containing oligosaccharides. Electron microscopic observation of negatively stained 550-kDa protein showed that native 550-kDa protein molecules are particles with an average diameter of 26.5 nm, but those particles treated with ethanol/ether are filamentous structures. These results suggest that the 550-kDa protein in the cytoplasm of unorganized skeletal muscle tissues exists as lipid-protein complex. Consequently, the 550-kDa protein may play an important role in the binding of myofibrils to the basal lamina by interaction with F-actin, α-actinin, laminin, fibronectin or Type IV collagen.
All Science Journal Classification (ASJC) codes
- Molecular Biology