Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 201-206 |
| Number of pages | 6 |
| Journal | BBA - General Subjects |
| Volume | 1245 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Oct 19 1995 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Molecular Biology
Cite this
Characterization of a novel 550-kDa protein in skeletal muscle of chick embryo. / Hattori, Akihito; Wakamatsu, Jun ichi; Ishii, Tatsuo; Kuwahara, Kyoko; Tatsumi, Ryuichi.
In: BBA - General Subjects, Vol. 1245, No. 2, 19.10.1995, p. 201-206.Research output: Contribution to journal › Article
}
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
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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UR - http://www.scopus.com/inward/citedby.url?scp=0028793979&partnerID=8YFLogxK
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 -