J. Biochem, 1993, Vol. 114, No. 4 582-587
© 1993 Japanese Biochemical Society
research-article |
Increased Expression of Cofilin in Dystrophic Chicken and Mouse Skeletal Muscles1
*Department of Biology, Chiba University Yayoi-cho, Inage-ku, Chiba 263
**Japan-Red Cross Saitama Branch Yono, Saitama 338
***Department of Physiology, Institute of Developmental Research Aichi Prefectural Colony, Aichi 480-03
3To whom correspondence should be addressed.
A monoclonal antibody (McAb) specific for actin depolymerizing factor (ADF) was prepared. With this and previously prepared anti-cofilin McAb (MAB-22) and other antibodies, the expression of cofilin and ADF in the muscles of dystrophic (NH-413) chicken and dystrophic (C57BL/6Jdy/dy) mice was compared with that in normal control animals by immunoblotting and immunocytochemical methods. Since cofilin expression is down-regulated during normal postnatal development of skeletal muscles [Abe et al. (1989) J. Biochem. 106, 696–702], cofilin was detected in the breast (pectoralis) muscle of normal adult chicken and the leg (femoris and tibialis anterior) muscles of normal mice only at a low level. ADF was not detectable in adult skeletal muscles. However, a significant increase of cofilin amount, but not of ADF amount, was observed in these muscles of the dystrophic animals, when the symptom of muscular dystrophy became evident. In order to localize cofilin in individual muscle fibers, serial cryosections of the dystrophic chicken muscle were examined with anti-cofilin antibody (MAB-22). The antibody stained cells of different size in the dystrophic muscle, indicating that cofilin expression was induced in the regenerating muscle cells as well as in the pre-existing myofibers. We suggest that cofilin is involved in disassembly or reorganization of actin in the dystrophic muscle.
1This work was supported by research grants from the Ministry of Education, Science and Culture, the National Center of Neurology and Psychiatry (PCNP) of the Ministry of Health and Welfare of Japan, Yamada Science Foundation, Futaba Denshi Memorial Foundation, and Uehara Memorial Foundation.
2Present address: Kotaikasei Co., Ltd., Kamikawa-machi, Kodamagun,Saitama 367-02.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  K. Nakashima, N. Sato, T. Nakagaki, H. Abe, S. Ono, and T. Obinata Two Mouse Cofilin Isoforms, Muscle-Type (MCF) and Non-Muscle Type (NMCF), Interact with F-Actin with Different Efficiencies J. Biochem., October 1, 2005; 138(4): 519 - 526. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. Ono, M. Parast, C. Alberico, G. M. Benian, and S. Ono Specific requirement for two ADF/cofilin isoforms in distinct actin-dependent processes in Caenorhabditis elegans J. Cell Sci., May 15, 2003; 116(10): 2073 - 2085. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Ono, D. L. Baillie, and G. M. Benian UNC-60B, an ADF/Cofilin Family Protein, Is Required for Proper Assembly of Actin into Myofibrils in Caenorhabditis elegans Body Wall Muscle J. Cell Biol., May 3, 1999; 145(3): 491 - 502. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. S. Minamide, W. B. Painter, G. Schevzov, P. Gunning, and J. R. Bamburg Differential Regulation of Actin Depolymerizing Factor and Cofilin in Response to Alterations in the Actin Monomer Pool J. Biol. Chem., March 28, 1997; 272(13): 8303 - 8309. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R Nagaoka, K Kusano, H Abe, and T Obinata Effects of cofilin on actin filamentous structures in cultured muscle cells. Intracellular regulation of cofilin action J. Cell Sci., January 2, 1995; 108(2): 581 - 593. [Abstract] [PDF]
|
|