Limb girdle muscular dystrophy in a sibling pair with a homozygous Ser606Leu mutation in the alternatively spliced IS2 region of calpain 3

References

Alexa, A., Bozoky, Z., Farkas, A., Tompa, P., and Friedrich, P. (2004). Contribution of distinct structural elements to activation of calpain by Ca²⁺ ions. J. Biol. Chem.279, 20118–20126.10.1074/jbc.M311969200Search in Google Scholar

de Paula, F., Vainzof, M., Passos-Bueno, M.R., de Cassia, M.P., Matioli, S.R., Anderson, V.B., Nigro, V., and Zatz, M. (2002). Clinical variability in calpainopathy: what makes the difference?Eur. J. Hum. Genet.10, 825–832.10.1038/sj.ejhg.5200888Search in Google Scholar

Dib, C., Faure, S., Fizames, C., Samson, D., Drouot, N., Vignal, A., Millasseau, P., Marc, S., Hazan, J., Seboun, E., et al. (1996). A comprehensive genetic map of the human genome based on 5264 microsatellites. Nature380, 152–154.10.1038/380152a0Search in Google Scholar

Fanin, M., Nascimbeni, A.C., Fulizio, L., Trevisan, C.P., Meznaric-Petrusa, M., and Angelini, C. (2003). Loss of calpain-3 autocatalytic activity in LGMD2A patients with normal protein expression. Am. J. Pathol.163, 1929–1936.10.1016/S0002-9440(10)63551-1Search in Google Scholar

Fanin, M., Fulizio, L., Nascimbeni, A.C., Spinazzi, M., Piluso, G., Ventriglia, V.M., Ruzza, G., Siciliano, G., Trevisan, C.P., Politano, L. et al. (2004). Molecular diagnosis in LGMD2A: mutation analysis or protein testing?Hum. Mutat.24, 52–62.10.1002/humu.20058Search in Google Scholar

Fukiage, C., Nakajima, E., Ma, H., Azuma, M., and Shearer, T.R. (2002). Characterization and regulation of lens-specific calpain Lp82. J. Biol. Chem.277, 20678–20685.10.1074/jbc.M200697200Search in Google Scholar

Herasse, M., Ono, Y., Fougerousse, F., Kimura, E., Stockholm, D., Beley, C., Montarras, D., Pinset, C., Sorimachi, H., Suzuki, K., et al. (1999). Expression and functional characteristics of calpain 3 isoforms generated through tissue-specific transcriptional and posttranscriptional events. Mol. Cell. Biol.19, 4047–4055.10.1128/MCB.19.6.4047Search in Google Scholar

Jia, Z., Petrounevitch, V., Wong, A., Moldoveanu, T., Davies, P.L., Elce, J.S., and Beckmann, J.S. (2001). Mutations in calpain 3 associated with limb girdle muscular dystrophy: analysis by molecular modeling and by mutation in m-calpain. Biophys. J.80, 2590–2596.10.1016/S0006-3495(01)76229-7Search in Google Scholar

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, 1373–1388.10.1093/hmg/ddh153Search in Google Scholar

Kruglyak, L., Daly, M.J., Reeve Daly, M.P., and Lander, E.S. (1996). Parametric and nonparametric linkage analysis: aunified multipoint approach. Am. J. Hum. Genet.58, 1347–1363.Search in Google Scholar

Nakajima, T., Fukiage, C., Azuma, M., Ma, H., and Shearer, T.R. (2001). Different expression patterns for ubiquitous calpains and Capn3 splice variants in monkey ocular tissues. Biochim. Biophys. Acta1519, 55–64.10.1016/S0167-4781(01)00212-3Search in Google Scholar

Ono, Y., Shimada, H., Sorimachi, H., Richard, I., Saido, T.C., Beckmann, J.S., Ishiura, S., and Suzuki, K. (1998). Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A. J. Biol. Chem.273, 17073–17078.10.1074/jbc.273.27.17073Search in Google Scholar

Ono, Y., Sorimachi, H., and Suzuki, K. (1999). New aspect of the research on limb-girdle muscular dystrophy 2A: a molecular biologic and biochemical approach to pathology. Trends Cardiovasc. Med.9, 114–118.10.1016/S1050-1738(99)00018-3Search in Google Scholar

Reverter, D., Sorimachi, H., and Bode, W. (2001). The structure of calcium-free human m-calpain: implications for calcium activation and function. Trends Cardiovasc. Med.11, 222–229.10.1016/S1050-1738(01)00112-8Search in Google Scholar

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. Cell81, 27–40.10.1016/0092-8674(95)90368-2Search in Google Scholar

Richard, I., Brenguier, L., Dincer, P., Roudaut, C., Bady, B., Burgunder, J.M., Chemaly, R., Garcia, C.A., Halaby, G., Jackson, C.E. et al. (1997). Multiple independent molecular etiology for limb-girdle muscular dystrophy type 2A patients fromvarious geographical origins. Am. J. Hum. Genet.60, 1128–1138.Search in Google Scholar

Richard, I., Roudaut, C., Saenz, A., Pogue, R., Grimbergen, J.E.M.A., Anderson, L.V.B., Beley, C., Cobo, A.M., de Diego, C., Eymard, B. et al. (1999). Calpainopathy – a survey of mutations and polymorphisms. Am. J. Hum. Genet.64, 1524–1540.10.1086/302426Search in Google Scholar PubMed PubMed Central

Sorimachi, H., Kinbara, K., Kimura, S., Takahashi, M., Ishiura, S., Sasagawa, N., Sorimachi, N., Shimada, H., Tagawa, K., Maruyama, K., and Suzuki, K. (1995). Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence. J. Biol. Chem.270, 31158–31162.10.1074/jbc.270.52.31158Search in Google Scholar PubMed

Witt, C.C., Ono, Y., Puschmann, E., McNabb, M., Wu, Y., Gotthardt, M., Witt, S.H., Haak, M., Labeit, D., Gregorio, C.C., et al. (2004). Induction and myofibrillar targeting of CARP, and suppression of the Nkx2.5 pathway in the MDM mouse with impaired titin-based signaling. J. Mol. Biol.336, 145–154.Search in Google Scholar