This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 12 print issues and online access
$209.00 per year
only $17.42 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Fardeau, M. et al. Juvenile limb-girdle muscular dystrophy: clinical, histopathological and genetic data on a small community living in the Reunion Island. Brain 119, 295–308 ( 1996).
Bushby, K.M.D. & Beckmann, J.S. Report of the 30 and 31st ENMC international workshop of the LGMDs - Proposal for a new nomenclature. Neuromusc. Disord. 5, 337– 343 (1995).
Beckmann, J.S. & Fardeau, M. in Neuromuscular Disorder: Clinical and Molecular Genetic Ch. 6 (ed. Emery, A.E.H.) 123– 156 (John Wiley and sons, Chichester, UK, (1998).
Richard, I. et al. Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell 81, 27– 40 (1995).
Richard, I. et al. Multiple independent molecular etiology for limb-girdle muscular dystrophy type 2A patients from various geographical origins. Am. J. Hum. Genet. 60, 1128–1138 (1997).
Anderson, L.V.B. et al. Characterization of monoclonal antibodies to calpain 3 and protein expression in muscle from patients with LGMD type 2A. Am. J. Pathol. 153, 1169–1179 (1998).
Sorimachi, H. et al. Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle. J. Biol. Chem. 268,10593–10605 ( 1993).
Baldwin, A.S. Jr. The NF-κB and IκB proteins: new discoveries and insights. Ann. Rev. Immunol. 14, 649 –681 (1996).
Ghosh, S. May, M.J. & Kopp, E.B. NF-κB and rel proteins: evolutionarily conserved mediators of immune responses. Ann. Rev. Immunol. 16 , 225–260 (1998).
Yang, J. et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science 275, 1129– 1132 (1997).
Mayo, M.W. et al. Requirement of NF-κB activation to suppress p53-independent apoptosis induced by oncogenic ras. Science 278, 1812–1815 (1997).
Spencer, M.J., Walsh, C.M., Dorshkind, K.A., Rodriguez, E.M. & Tidball J.G. Myonuclear apoptosis in dystrophic mdx muscle occurs by perforin-mediated cytotoxicity. J. Clin. Invest. 99, 2745– 2751 (1997).
Hack, A.A. et al. γ-sarcoglycan deficiency leads to muscle membrane defects and apoptosis independent of dystrophin. J. Cell. Biol. 142, 1279–1287 (1998).
Sandri, M., Minetti, C., Predemonte, M. & Carraro, U. Apoptotic myonuclei in human Duchenne muscular dystrophy. Lab. Invest. 78, 1005–1016 ( 1998).
Tews, D.S. & Goebel, H.H. DNA-fragmentation and expression of apoptosis-related proteins in muscular dystrophy. Neuropathol. Appl. Neurobiol. 23, 331–338 (1997).
Tews, D.S. & Goebel, H.H. DNA-fragmentation and Bcl-2 expression in infantile spinal muscular atrophy. Neuromusc. Disord. 6, 265–273 (1996).
Allen, D.L. et al. Apoptosis: a mechanism contributing to remodeling of skeletal muscle in response to hindlimb unweighting. Am. J. Physiol. 273, C579–C587 (1997).
Fougerousse, F. et al. Expression of genes (calpain 3, SGCA, SGCB and TTN) involved in progressive muscular dystrophies during early human development. Genomics 48, 145–156 ( 1998).
Liu, J. et al. Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy. Nature Genet. 20, 31–36 (1998).
Bashir, R. et al. A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B. Nature Genet. 20, 37–42 ( 1998).
Suyang, H., Phillips, R., Douglas, I. & Ghosh, S. Role of unphosphorylated, newly synthesized IκBβ in persistent activation of NFκB. Mol. Cell. Biol. 16, 5444–5449 (1996).
Han, Y. Weinman, S. Boldogh, I. Walker, R.K. & Brasier, A.R. Tumor necrosis factor-α-inducible IκBα proteolysis mediated by cytosolic m-calpain. A mechanism parallel to the ubiquitin-proteasome pathway for NF-κB activation. J. Biol. Chem. 274, 787–794 (1999).
Zabel, U., Henkel, T. Silva, M.S. & Baeuerle, P.A. Nuclear uptake control of NF-κB by MAD-3, an IκB protein present in the nucleus. EMBO J. 12, 201–211 (1993).
Arenzana-Seisdedos, F. et al. Inducible nuclear expression of newly synthesized IκBα negatively regulates DNA-binding and transcriptional activation of NF-κB. Mol. Cell. Biol. 15, 2689– 2696 (1995).
Arenzana-Seisdedos, F. et al. Nuclear localization of I kappa B alpha promotes active transport of NF-kappa B from the nucleus to the cytoplasm. J. Cell. Sci. 110, 369–378 ( 1997).
Sachdev, S. Hoffmann, A. & Hannink, M. Nuclear localization of IκBα is mediated by the second ankyrin repeat: the IκBα ankyrin repeats define a novel class of cis-acting nuclear import sequence. Mol. Cell. Biol. 18, 2524–2534 ( 1998).
Guo, Q. Robinson, N. & Mattson M.P. Secreted β-amyloid precursor protein counteracts the proapoptotic action of mutant presenilin-1 by activation of NF-κB and stabilization of calcium homeostasis. J. Biol. Chem. 273, 12341–12351 (1998).
Zhi-Liang C. et al. Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-κB control. Proc. Natl. Acad. Sci. USA 94, 10057–10062 (1997).
Wang, C.Y., Mayo, M.W., Korneluk, R.G., Goeddel, D.V. & Baldwin, A.S. Jr. NF-κB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science 281, 1680–1683 (1998).
Stehlik, C., de Martin, R. Binder, B.R. & Lipp, J. Cytokine induced expression of porcine inhibitor of apoptosis protein (iap) family member is regulated by NF-κB. Biochem. Biophys. Res. Commun. 243, 827–832 ( 1998).
Sorimachi, H. et al. Muscle-specific calpain, p94, responsible for LGMD2A, associates with connectin through IS2, p94 specific sequence. J. Biol. Chem. 270, 31158–31162 ( 1995).
Klietsch, R., Ervasti, J.M., Arnold, W., Campbell, K.P. & Jorgensen, A.O. Dystrophin glycoprotein complex and laminin colocalize to the sarcolemma and transverse tubules of cardiac muscle. Circ. Res. 72, 349– 60 (1993).
Pons, F., Nicholson, L.V.B., Robert, A., Voit, T. & Leger, J.J. Dystrophin and dystrophin-related protein (utrophin) distribution in normal and dystrophin-deficient skeletal muscles. Neuromusc. Disord. 3, 507– 514 (1993).
Marini, J.F. et al. Expression of myosin heavy chain isoforms in Duchenne muscular dystrophy patients and carriers. Neuromusc. Disord. 1, 397–409 (1991).
Jaffray, E., Wood, K.M. & Hay, R.T. Domain organization of IκBα and sites of interaction with NF-κB p65. Mol. Cell. Biol. 15, 2166–2172 (1995).
Guénal, C., Sidoti, T., de Fraisse, S., Gaumer S. & Mignotte, B. Bcl-2 and Hsp27 act at different levels to suppress programmed cell death. Oncogene 15, 347–360 (1997).
Martin, M., Roy, C., Montcourrier, P., Sahuquet, A. & Mangeat, P. Three determinants in ezrin are responsible for cell extension activity. Mol. Biol. Cell. 8, 1543–1557 (1997).
Rodriguez, M..S., Michalopoulos, I., Arenzana-Seisdedos, F. & Hay, R.T. Inducible degradation of IκBα in vitro and in vivo requires the acidic C-terminal domain of the protein. Mol. Cell. Biol. 15, 2413–2419 (1995).
Edom, F. Mouly, V. Barbet, J.P. Fiszman, M.Y. & Butler-Browne, G.S. Clones of human satellites cells can express in vitro both fast and slow myosin heavy chains. Dev. Biol. 164, 219–229 (1994).
Acknowledgements
We are particularly indebted to the L5988 and L7111 families members and A21 and A13 for their continued and invaluable cooperation. We also thank P. Farah, A. Megarbane, J. Ducret, H. Aydenian, J. Maarrawi, G. Abadjian, N. Salem and the clinicians of the North Lebanon. We also acknowledge J. Demaille, I. Touitou, B. Vallet, N. Romero, G. Restagno, A.M. Cobo, I. Penisson, A. Vila and X. Ferrer as well as A. Sahuquet, H. Lelouard and S. Bonavaud. We are also indebted to J.L. Vayssière and B. Mignotte for discussions and S. Artero for statistical analysis. This work was supported by grants from the Saint-Joseph and Montpellier II Universities, the Lebanese and French CNRS (International Programs of Scientific Cooperation), the Association Française contre les Myopathies (AFM), the INSERM and the Ambassade de France.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Baghdiguian, S., Martin, M., Richard, I. et al. Calpain 3 deficiency is associated with myonuclear apoptosis and profound perturbation of the IκBα/NF-κB pathway in limb-girdle muscular dystrophy type 2A. Nat Med 5, 503–511 (1999). https://doi.org/10.1038/8385
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/8385
This article is cited by
-
Mitochondrial dysfunction and consequences in calpain-3-deficient muscle
Skeletal Muscle (2020)
-
A muscular hypotonia-associated STIM1 mutant at R429 induces abnormalities in intracellular Ca2+ movement and extracellular Ca2+ entry in skeletal muscle
Scientific Reports (2019)
-
Life or death by NFκB, Losartan promotes survival in dy2J/dy2J mouse of MDC1A
Cell Death & Disease (2015)
-
Oxidative Stress, NF-κB and the Ubiquitin Proteasomal Pathway in the Pathology of Calpainopathy
Neurochemical Research (2013)
-
2-Benzamido-N-(1H-benzo[d]imidazol-2-yl)thiazole-4-carboxamide derivatives as potent inhibitors of CK1δ/ε
Amino Acids (2012)