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Characterization of human muscle type cofilin (CFL2) in normal and regenerating muscle

Thirion, C., Stucka, R., Mendel, B., Gruhler, A., Jaksch, M., Nowak, K.J., Binz, N., Laing, N.G. and Lochmüller, H. (2001) Characterization of human muscle type cofilin (CFL2) in normal and regenerating muscle. European Journal of Biochemistry, 268 (12). pp. 3473-3482.

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Cofilins are actin binding proteins and regulate actin assembly in vivo. Numerous cofilin homologues have been characterized in various organisms including mammals. In mice, a ubiquitously expressed cofilin (CFL1) and a skeletal muscle specific cofilin (CFL2) have been described. In the present study, we identified and characterized a human CFL2 gene localized on chromosome 14, with high homology to murine CFL2. Furthermore, we provide evidence for differentially spliced CFL2 transcripts (CFL2a and CFL2b). CFL2b is expressed predominantly in human skeletal muscle and heart, while CFL2a is expressed in various tissues. Genetic defects of CFL2 were excluded for one human muscle disorder, the chromosome 14 linked distal myopathy MPD1, and shown to be only possible to be a rare cause of another, nemaline myopathy. In a mouse model of mechanically induced muscle damage the changes of cofilin expression were monitored during the first 10 days of regeneration, with dephosphorylated CFL2 being the major isoform at later stages of muscle regeneration. A similar predominance of dephosphorylated CFL2 was observed in chronically regenerating dystrophin-deficient muscles of Duchenne muscular dystrophy patients. Therefore, the CFL2 isoform may play an important role in normal muscle function and muscle regeneration.

Item Type: Journal Article
Murdoch Affiliation(s): School of Veterinary Biology and Biomedical Science
Copyright: FEBS 2001
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