J. Biochem, 1989, Vol. 106, No. 4 696-702
© 1989 Japanese Biochemical Society
research-article |
A Cofilin-Like Protein Is Involved in the Regulation of Actin Assembly in Developing Skeletal Muscle1
*Graduate School and Technology, Chiba University Chiba, Chiba 260
**Department of Biology, Faculty of Science, Chiba University Chiba, Chiba 260
2To whom reprint requests should be addressed.
An actin-binding protein of 20 kDa (called 20K protein) was purified from the sarcoplasmic fraction of embryonic chicken skeletal muscle. The properties of this protein were very similar to cofilin, which was discovered in porcine brain (Nishida et al. (1984) Biochemistry, 23, 5307–5313): it bound to both G- and F-actin, inhibited actin polymerization in a pH-dependent manner, inhibited binding of tropomyosin to F-actin, and had almost the same molecular size and pi as cofilin. A specific monoclonal antibody to 20K protein (MAB-22) was prepared to examine the expression and location of 20K protein during skeletal muscle development. When the whole protein lysates of embryonic and post-hatched chicken skeletal muscles were examined by means of immunoblotting combined with SDS-PAGE, 20K protein was detected in skeletal muscle through the developmental stages. Location of 20K protein in the cells differed between the embryonic and adult tissues; immunofluorescence staining of the cryosections of embryonic muscle with MAB-22 visualized irregular dot-like structures, but adult muscle sections were stained faintly and uniformly. 20K protein was present as a complex with actin in embryonic muscle, as judged by the ability to bind to a DNase I affinity column, while the same protein was free from actin in the cytoplasm of adult muscle. From these results, it is suggested that 20K protein regulates actin assembly transiently in developing skeletal muscle.
1This study was supported by research grants from the Ministry of Education, Science and Culture, the National Center of Neurology and Psychiatry (NCNP) of the Ministry of Health and Welfare of Japan, the Muscular Dystrophy Association of America (MDA), and the Shimadzu Science Foundation.
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