TY - JOUR
T1 - Characterization of a novel 550-kDa protein in skeletal muscle of chick embryo
AU - Hattori, Akihito
AU - Wakamatsu, Jun ichi
AU - Ishii, Tatsuo
AU - Kuwahara, Kyoko
AU - Tatsumi, Ryuichi
N1 - Funding Information:
We would like to express our sincere appreciation to Professor K. Maruyama (Chiba University, Chiba, Japan) for his helpful discussions and encouragement throughout this study. We wish to thank Professor K. Takahashi in our laboratory for his valuable discussions throughout this study. We wish to express our gratitude to Mr. T. Ito the Electron Microscope Laboratory, Faculty of Agriculture, Hokkaido University, for his technical assistance in taking electron micrographs. This study was supported in part by research grants from the Ministry of Education, Science and Culture of Japan; by research grants from the Ito Foundation of Japan.
PY - 1995/10/19
Y1 - 1995/10/19
N2 - 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.
AB - 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.
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U2 - 10.1016/0304-4165(95)00097-U
DO - 10.1016/0304-4165(95)00097-U
M3 - Article
C2 - 7492578
AN - SCOPUS:0028793979
VL - 1245
SP - 201
EP - 206
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
SN - 0304-4165
IS - 2
ER -