Calpain 3 participates in sarcomere remodeling by acting upstream of the ubiquitin–proteasome pathway-Reference-Cited by-同舟云学术

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Calpain 3 participates in sarcomere remodeling by acting upstream of the ubiquitin–proteasome pathway

Published:2005-06-16 Issue:15 Volume:14 Page:2125-2134
ISSN:1460-2083
Container-title:Human Molecular Genetics
language:en
Short-container-title:

Author:

Kramerova Irina,Kudryashova Elena,Venkatraman Gayathri,Spencer Melissa J.

Publisher

Oxford University Press (OUP)

Subject

Genetics(clinical),Genetics,Molecular Biology,General Medicine

Link

http://academic.oup.com/hmg/article-pdf/14/15/2125/1463630/ddi217.pdf

Reference36 articles.

1. Goll, D.E., Thompson, V.F., Li, H., Wei, W. and Cong, J. (2003) The calpain system. Physiol. Rev., 83, 731–801.

2. Richard, I., Broux, O., Allamand, V., Fougerousse, F., Chiannilkulchai, N., Bourg, N., Brenguier, L., Devaud, C., Pasturaud, P., Roudaut, C. et al. (1995) Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell, 81, 27–40.

3. Richard, I., Roudaut, C., Marchand, S., Baghdiguian, S., Herasse, M., Stockholm, D., Ono, Y., Suel, L., Bourg, N., Sorimachi, H. et al. (2000) Loss of calpain 3 proteolytic activity leads to muscular dystrophy and to apoptosis-associated IKBa/nuclear factor KB pathway perturbation in mice. J. Cell Biol., 151, 1–9.

4. Kramerova, I., Kudryashova, E., Tidball, J.G. and Spencer, M.J. (2004) Null mutation of calpain 3 (p94) in mice causes abnormal sarcomere formation in vivo and in vitro. Hum. Mol. Genet., 13, 1373–1388.

5. Gregorio, C.C., Granzier, H., Sorimachi, H. and Labeit, S. (1999) Muscle assembly: a titanic achievement? Curr. Opin. Cell Biol., 11, 18–25.

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