International Journal of Cell Biology
Volume 2009 (2009), Article ID 340346, 12 pages
doi:10.1155/2009/340346
Research Article
Alteration of Sarcoplasmic Reticulum Ca2+ Release in Skeletal Muscle from Calpain 3-Deficient Mice
Govindan Dayanithi,
1,2 Isabelle Richard,
3 Cédric Viero,
4 Elsa Mazuc,
5,6 Sylvie Mallie,
5 Jean Valmier,
5 Nathalie Bourg,
3 Muriel Herasse,
3 Isabelle Marty,
7 Gérard Lefranc,
8 Paul Mangeat,
9 and
Stephen Baghdiguian10
1Department of Cellular Neurophysiology, Institute of Experimental Medicine, Academy of Sciences of the Czech Republic, European Union Centre of Excellence, Videnska 1083, 142 20 Prague 4, Czech Republic
2Départment Biologie Santé, Université Montpellier 2, place Eugène Bataillon, 34095 Montpellier, Cedex 05, France
3Généthon CNRS-UMR8587 LAMBE, 1, rue de l'Internationale, 91000 Evry, France
4Department of Cardiology, Wales Heart Research Institute, School of Medicine, Cardiff University, Heath Park, Cardiff CF14 4XN, UK
5INSERM U583, Institut des Neurosciences de Montpellier, Hôpital St Eloi, 80, rue Augustin Fliche, 34091 Montpellier, Cedex 05, France
6Institut de Recherche en Cancérologie de Montpellier, CRLC Val d'Aurelle-Paul Lamarque, 34298 Montpellier, Cedex 05, France
7Grenoble Institut des Neurosciences, INSERM U836, Equipe Muscle et Pathologies, UJF Site santé-BP170, 38042 Grenoble Cedex 9, France
8Laboratoire d'Immunogénétique Moléculaire, UPR 1142 CNRS-Institut de Génétique Humaine, Université Montpellier 2, place Eugène Bataillon, 34095 Montpellier, Cedex 05, France
9Centre de Recherche de Biochimie Macromoléculaire, Universités Montpellier 2 & 1, 1919 Route de Mende, 34293 Montpellier, Cedex 05, France
10UMR CNRS 5554, Institut des Sciences de l'Evolution, Université Montpellier 2, place Eugène Bataillon, 34095 Montpellier, Cedex 05, France
Received 21 August 2009; Accepted 2 December 2009
Academic Editor: Gerhard Wiche
Copyright © 2009 Govindan Dayanithi et al. This is an open access article distributed under the
Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Linked References
- D. E. Goll, V. F. Thompson, H. Li, W. Wei, and J. Cong, “The calpain system,” Physiological Reviews, vol. 83, no. 3, pp. 731–801, 2003. View at Scopus
- D. E. Croall and G. N. DeMartino, “Calcium-activated neutral protease (calpain) system: structure, function, and regulation,” Physiological Reviews, vol. 71, no. 3, pp. 813–847, 1991. View at Scopus
- E. Carafoli and M. Molinari, “Calpain: a protease in search of a function?” Biochemical and Biophysical Research Communications, vol. 247, no. 2, pp. 193–203, 1998. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- I. Richard, O. Broux, V. Allamand, et al., “Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A,” Cell, vol. 81, no. 1, pp. 27–40, 1995. View at Scopus
- S. Baghdiguian, M. Martin, I. Richard, et al., “Calpain 3 deficiency is associated with myonuclear apoptosis and profound perturbation of the IB /NF-B pathway in limb-girdle muscular dystrophy type 2A,” Nature Medicine, vol. 5, no. 5, pp. 503–511, 1999. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
- I. Richard, C. Roudaut, S. Marchand, et al., “Loss of calpain 3 proteolytic activity leads to muscular dystrophy and to apoptosis-associated IB/nuclear factor B pathway perturbation in mice,” Journal of Cell Biology, vol. 151, no. 7, pp. 1583–1590, 2000. View at Publisher · View at Google Scholar · View at Scopus
- V. Shoshan-Barmatz, S. Weil, H. Meyer, M. Varsanyi, and L. M. G. Heilmeyer, “Endogenous, -dependent cysteine-protease cleaves specifically the ryanodine receptor/ release channel in skeletal muscle,” Journal of Membrane Biology, vol. 142, no. 3, pp. 281–288, 1994. View at Scopus
- J. Alterio, Y. Courtois, J. Robelin, D. Bechet, and I. Martelly, “Acidic and basic fibroblasts growth factor mRNAs are expressed by skeletal muscle satellite cells,” Biochemical and Biophysical Research Communications, vol. 166, no. 3, pp. 1205–1212, 1990. View at Publisher · View at Google Scholar · View at Scopus
- S. J. Martin, M. A. P. Audrain, F. Oksman, et al., “Antineutrophil cytoplasmic antibodies (ANCA) in chronic graft-versus-host disease after allogeneic bone marrow transplantation,” Bone Marrow Transplantation, vol. 20, no. 1, pp. 45–48, 1997. View at Scopus
- R. C. Lambert, G. Dayanithi, F. C. Moos, and Ph. Richard, “A rise in the intracellular concentration of isolated rat supraoptic cells in response to oxytocin,” Journal of Physiology, vol. 478, no. 2, pp. 275–287, 1994. View at Scopus
- G. Dayanithi, H. Widmer, and Ph. Richard, “Vasopressin-induced intracellular increase in isolated rat supraoptic cells,” Journal of Physiology, vol. 490, no. 3, pp. 713–727, 1996. View at Scopus
- F. Jamen, G. Alonso, I. Shibuya, et al., “Impaired somatodendritic responses to pituitary adenylate cyclase-activating polypeptide (PACAP) of supraoptic neurones in PACAP type I-receptor deficient mice,” Journal of Neuroendocrinology, vol. 15, no. 9, pp. 871–881, 2003. View at Publisher · View at Google Scholar · View at Scopus
- G. Grynkiewicz, M. Poenie, and R. Y. Tsien, “A new generation of indicators with greatly improved fluorescence properties,” Journal of Biological Chemistry, vol. 260, no. 6, pp. 3440–3450, 1985. View at Scopus
- I. Marty, M. Robert, M. Villaz, et al., “Biochemical evidence for a complex involving dihydropyridine receptor and ryanodine receptor in triad junctions of skeletal muscle,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 6, pp. 2270–2274, 1994. View at Scopus
- S. Shevchenko, W. Feng, M. Varsanyi, and V. Shoshan-Barmatz, “Identification, characterization and partial purification of a thiol-protease which cleaves specifically the skeletal muscle ryanodine receptor/ release channel,” Journal of Membrane Biology, vol. 161, no. 1, pp. 33–43, 1998. View at Publisher · View at Google Scholar · View at Scopus
- B. Benayoun, S. Baghdiguian, A. Lajmanovich, et al., “NF-B-dependent expression of the antiapoptotic factor c-FLIP is regulated by calpain 3, the protein involved in limb-girdle muscular dystrophy type 2A,” FASEB Journal, vol. 22, no. 5, pp. 1521–1529, 2008. View at Publisher · View at Google Scholar · View at PubMed
- R. Wang, L. Zhang, J. Bolstad, et al., “Residue Gln4863 within a predicted transmembrane sequence of the release channel (ryanodine receptor) is critical for ryanodine interaction,” Journal of Biological Chemistry, vol. 278, no. 51, pp. 51557–51565, 2003. View at Publisher · View at Google Scholar · View at PubMed
- J. D. Fessenden, L. Chen, Y. Wang, et al., “Ryanodine receptor point mutant E4032A reveals an allosteric interaction with ryanodine,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 5, pp. 2865–2870, 2001. View at Publisher · View at Google Scholar · View at PubMed
- T. Yang, P. D. Allen, I. N. Pessah, and J. R. Lopez, “Enhanced excitation-coupled calcium entry in myotubes is associated with expression of RyR1 malignant hyperthermia mutations,” Journal of Biological Chemistry, vol. 282, no. 52, pp. 37471–37478, 2007. View at Publisher · View at Google Scholar · View at PubMed
- F. Naro, V. De Arcangelis, D. Coletti, et al., “Increase in cytosolic induced by elevation of extracellular in skeletal myogenic cells,” American Journal of Physiology, vol. 284, no. 4, pp. C969–C976, 2003.
- N. Khandoudi, J. Percevault-Albadine, and A. Bril, “Consequences of the inhibition of the sarcoplasmic reticulum calcium ATPase on cardiac function and coronary flow in rabbit isolated perfused heart: role of calcium and nitric oxide,” Journal of Molecular and Cellular Cardiology, vol. 30, no. 10, pp. 1967–1977, 1998. View at Publisher · View at Google Scholar · View at PubMed
- E. B. Okon, A. Golbabaie, and C. van Breemen, “In the presence of L-NAME SERCA blockade induces endothelium-dependent contraction of mouse aorta through activation of smooth muscle prostaglandin H2/thromboxane A2 receptors,” British Journal of Pharmacology, vol. 137, no. 4, pp. 545–553, 2002. View at Publisher · View at Google Scholar · View at PubMed
- R. I. Jabr, H. Toland, C. H. Gelband, X. X. Wang, and J. R. Hume, “Prominent role of intracellular release in hypoxic vasoconstriction of canine pulmonary artery,” British Journal of Pharmacology, vol. 122, no. 1, pp. 21–30, 1997. View at Publisher · View at Google Scholar · View at PubMed
- P. R. Turner, T. Westwood, C. M. Regen, and R. A. Steinhardt, “Increased protein degradation results from elevated free calcium levels found in muscle from mdx mice,” Nature, vol. 335, no. 6192, pp. 735–738, 1988.
- F. Salamino, B. Sparatore, E. Melloni, et al., “The plasma membrane calcium pump is the preferred calpain substrate within the erythrocyte,” Cell Calcium, vol. 15, no. 1, pp. 28–35, 1994. View at Publisher · View at Google Scholar
- G. Dayanithi, I. Mechaly, C. Viero, et al., “Intracellular regulation in rat motoneurons during development,” Cell Calcium, vol. 39, no. 3, pp. 237–246, 2006. View at Publisher · View at Google Scholar · View at PubMed
- D. M. Bers, Excitation-Contraction Coupling and Cardiac Contractile Force, Kluwer Academic Publishers, Dordrecht, The Netherlands, 2001.
- E. Verburg, R. M. Murphy, I. Richard, and G. D. Lamb, “Involvement of calpains in -induced disruption of excitation-contraction coupling in mammalian skeletal muscle fibers,” American Journal of Physiology, vol. 296, no. 5, pp. C1115–C1122, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus