*. Doyle, M. Haley, and P. , [17] Meizothrombin: Active intermediate formed during prothrombinase-catalyzed activation of prothrombin, Methods Enzymol, vol.222, pp.299-312, 1993.
DOI : 10.1016/0076-6879(93)22020-G

*. Drummond, G. Duncan, and L. , Activation of cardiac phosphorylase b kinase, J, 1966.

*. Dubiel, W. Ferrell, K. Rechsteiner, and M. , Subunits of the regulatory complex of the 26S protease, Molecular Biology Reports, vol.252, issue.1, pp.27-34, 1995.
DOI : 10.1007/BF00990967

*. Duguez, S. Bartoli, M. , and R. I. , Calpain 3: a key regulator of the sarcomere?, FEBS Journal, vol.35, issue.15, pp.3427-3463, 2006.
DOI : 10.1073/pnas.95.21.12100

*. Dutaud and D. , Quantification et caractérisation du protéasome 20S de muscle de bovin en relation avec l'attendrissage de la viande bovine, Thèse science des aliments, 1998.

*. Elamrani, N. Brustis, J. Dourdin, N. Balcerzak, D. Poussard et al., Desmin degradation and Ca2+???dependent proteolysis during myoblast fusion, Biology of the Cell, vol.9, issue.2-3, pp.177-83, 1995.
DOI : 10.1016/0248-4900(96)85278-6

*. Elce, J. Davies, P. Hegadorn, C. Maurice, D. Arthur et al., The effects of truncations of the small subunit on m-calpain activity and heterodimer formation, Biochemical Journal, vol.326, issue.1, 1997.
DOI : 10.1042/bj3260031

*. Inomata, M. Hayashi, M. Ohno-iwashita, Y. Tsubuki, S. Saido et al., Involvement of Calpain in Integrin-Mediated Signal Transduction, Archives of Biochemistry and Biophysics, vol.328, issue.1, pp.129-163, 1996.
DOI : 10.1006/abbi.1996.0152

*. Ishiguro, H. Higashiyama, S. Namikawa, C. Kunimatsu, M. Takano et al., Interaction of human calpains I and II with high molecular weight and low molecular weight kininogens and their heavy chain: mechanism of interaction and the role of divalent cations, Biochemistry, vol.26, issue.10, pp.262863-70, 1987.
DOI : 10.1021/bi00384a030

*. Ishisaka, R. Utsumi, T. Yabuki, M. Kanno, T. Furuno et al., Activation of caspase-3-like protease by digitonin-treated lysosomes, FEBS Letters, vol.88, issue.2-3, pp.233-239, 1998.
DOI : 10.1016/S0014-5793(98)01080-1

*. Ishiura, S. Sugita, H. Nonaka, I. Imahori, and K. , Calcium-Activated Neutral Protease: Its Localization in the Myofibril, Especially at the Z-Band1, The Journal of Biochemistry, vol.87, issue.1, pp.343-349, 1980.
DOI : 10.1093/oxfordjournals.jbchem.a132743

*. Jékely, G. Friedrich, and P. , Characterization of Two Recombinant DrosophilaCalpains: CALPA AND A NOVEL HOMOLOG, CALPB, Journal of Biological Chemistry, vol.274, issue.34, pp.23893-900, 1999.
DOI : 10.1074/jbc.274.34.23893

*. Jia, Z. Petrounevitch, V. Wong, A. Moldoveanu, T. Davies et al., Mutations in Calpain 3 Associated with Limb Girdle Muscular Dystrophy: Analysis by Molecular Modeling and by Mutation in m-Calpain, Biophysical Journal, vol.80, issue.6, pp.2590-2596, 2001.
DOI : 10.1016/S0006-3495(01)76229-7

*. Johnson, J. Tikunova, and S. , Fluorescence Methods for Measuring Calcium Affinity and Calcium Exchange with Proteins, Methods Mol Biol, vol.173, pp.89-102, 2002.
DOI : 10.1385/1-59259-184-1:089

K. Kapprell, H. Goll, and D. , Effect of Ca2+ on binding of the calpains to calpastatin, J Biol Chem, vol.264, issue.30, pp.17888-96, 1989.

*. Stauber, W. Bird, J. Schottelius, and B. , Catalase: An enzymatic indicator of the degree of muscle wasting, Experimental Neurology, vol.55, issue.2, pp.381-390, 1977.
DOI : 10.1016/0014-4886(77)90008-5

*. Strobl, S. Fernandez-catalan, C. Braun, M. Huber, R. Masumoto et al., The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium, Proceedings of the National Academy of Sciences, vol.97, issue.2, pp.588-92, 2000.
DOI : 10.1073/pnas.97.2.588

*. Suzuki, K. Sorimachi, and H. , A novel aspect of calpain activation, FEBS Letters, vol.325, issue.1-2, pp.1-4, 1998.
DOI : 10.1016/S0014-5793(98)00856-4

*. Suzuki, Y. Yoshida, K. Ichimiya, T. Yamamoto, T. Sinohara et al., Trypsin Inhibitors in Guinea Pig Plasma: Isolation and Characterization of Contrapsin and Two Isoforms of ?? -1-Antiproteinase and Acute Phase Response of Four Major Trypsin Inhibitors, The Journal of Biochemistry, vol.107, issue.2, pp.173-182, 1990.
DOI : 10.1093/oxfordjournals.jbchem.a123021

*. Takahara, H. Sinohara, and H. , Mouse plasma trypsin inhibitors. Isolation and characterization of alpha-1-antitrypsin and contrapsin, a novel trypsin inhibitor, J Biol Chem, vol.257, issue.5, pp.2438-2484, 1982.

*. Takano, E. Kitahara, A. Sasaki, T. Kannagi, R. Murachi et al., Two different molecular species of pig calpastatin. Structural and functional relationship between 107 kDa and 68 kDa molecules, Biochemical Journal, vol.235, issue.1, pp.97-102, 1986.
DOI : 10.1042/bj2350097

*. Takano, E. Maki, M. Mori, H. Hatanaka, M. Marti et al., Pig heart calpastatin: identification of repetitive domain structures and anomalous behavior in polyacrylamide gel electrophoresis, Biochemistry, vol.27, issue.6, pp.1964-72, 1988.
DOI : 10.1021/bi00406a024

*. Takano, E. Nosaka, T. Lee, W. Nakamura, K. Takahashi et al., Molecular Diversity of Calpastatin in Human Erythroid Cells, Archives of Biochemistry and Biophysics, vol.303, issue.2, pp.349-54, 1993.
DOI : 10.1006/abbi.1993.1294

*. Takano, E. Ma, H. Yang, H. Maki, M. Hatanaka et al., Preference of calcium-dependent interactions between calmodulin-like domains of calpain and calpastatin subdomains, FEBS Letters, vol.92, issue.1, pp.93-100, 1995.
DOI : 10.1016/0014-5793(95)00219-Y

. Publications, . Communications-publications, M. Sentendreu, G. Coulis, and A. Ouali, Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends in Food Science and Technology, pp.400-421, 2002.

F. Raynaud, E. Fernandez, G. Coulis, L. Aubry, X. Vignon et al., Calpain 1-titin interactions concentrate calpain 1 in the Z-band edges and in the N2-line region within the skeletal myofibril, FEBS Journal, vol.268, issue.150, pp.2578-90, 2005.
DOI : 10.1111/j.1742-4658.2005.04683.x

C. Herrera-mendez, L. Brémaud, G. Coulis, P. Pélissier, M. Sentandreu et al., Purification of the skeletal muscle protein Endopin 1B and characterization of the genes encoding Endopin 1A and 1B isoforms, FEBS Letters, vol.228, issue.14, 2006.
DOI : 10.1016/j.febslet.2006.04.099

URL : https://hal.archives-ouvertes.fr/hal-01211871

A. Ouali, C. H. Herrera-mendez, G. Coulis, S. Becila, A. Boudjellal et al., Revisiting the conversion of muscle into meat and the underlying mechanisms, Meat Science, vol.74, issue.1, pp.44-58, 2006.
DOI : 10.1016/j.meatsci.2006.05.010

S. Baghdiguian, M. Martin, I. Richard, F. Pons, C. Astier et al., Calpain 3 deficiency is associated with myonuclear apoptosis and profound perturbation of the IkappaB alpha ? NF-kappaB pathway in limb-girdle muscular dystrophy type 2A, Nat Med, vol.5, pp.503-511, 1999.

Y. Benyamin, The structural basis of calpain behavior, FEBS Journal, vol.388, issue.15, pp.3413-3414, 2006.
DOI : 10.1073/pnas.97.2.588

M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Analytical Biochemistry, vol.72, issue.1-2, pp.248-254, 1976.
DOI : 10.1016/0003-2697(76)90527-3

E. Carafoli and M. Molinari, Calpain: A Protease in Search of a Function?, Biochemical and Biophysical Research Communications, vol.247, issue.2, pp.193-203, 1998.
DOI : 10.1006/bbrc.1998.8378

G. Coulis, M. Sentandreu, N. Bleimling, M. Gautel, Y. Benyamin et al., Myofibrillar tightly bound calcium in skeletal muscle fibers: a possible role of this cation in titin strands aggregation, FEBS Letters, vol.26, issue.1-3, pp.271-275, 2004.
DOI : 10.1016/S0014-5793(03)01436-4

W. Dayton and J. Schollmeyer, Immunocytochemical localization of a calcium-activated protease in skeletal muscle cells, Experimental Cell Research, vol.136, issue.2, pp.423-433, 1981.
DOI : 10.1016/0014-4827(81)90022-7

P. Dutt, C. Spriggs, P. Davies, Z. Jia, and J. Elce, Origins of the difference in Ca2+ requirement for activation of ??- and m-calpain, Biochemical Journal, vol.367, issue.1, pp.263-272, 2002.
DOI : 10.1042/bj20020485

A. Freiburg, K. Trombitas, W. Hell, O. Cazorla, F. Fougerousse et al., Series of Exon-Skipping Events in the Elastic Spring Region of Titin as the Structural Basis for Myofibrillar Elastic Diversity, Circulation Research, vol.86, issue.11, pp.1114-1135, 2000.
DOI : 10.1161/01.RES.86.11.1114

T. Funatsu, E. Kono, H. Higuchi, S. Kimura, S. Ishiwata et al., Elastic filaments in situ in cardiac muscle: deep-etch replica analysis in combination with selective removal of actin and myosin filaments, The Journal of Cell Biology, vol.120, issue.3, pp.711-724, 1993.
DOI : 10.1083/jcb.120.3.711

D. E. Goll and G. H. Geesink, Measurement of calpain activity in postmortem muscle extracts underestimates levels of _-calpain, Proc. 41st Ann, pp.547-549, 1995.

D. Goll, V. Thompson, H. Li, W. Wei, and J. Cong, The Calpain System, Physiological Reviews, vol.83, issue.3, pp.731-801, 2003.
DOI : 10.1152/physrev.00029.2002

C. Gregorio, H. Granzier, H. Sorimachi, and S. Labeit, Muscle assembly: a titanic achievement?, Current Opinion in Cell Biology, vol.11, issue.1, pp.18-25, 1999.
DOI : 10.1016/S0955-0674(99)80003-9

Y. Huang and K. K. Wang, The calpain family and human disease, Trends in Molecular Medicine, vol.7, issue.8, pp.355-362, 2001.
DOI : 10.1016/S1471-4914(01)02049-4

S. Ishiura, H. Sugita, I. Nonaka, and K. Imahori, Calcium-Activated Neutral Protease: Its Localization in the Myofibril, Especially at the Z-Band1, The Journal of Biochemistry, vol.87, issue.1, pp.343-346, 1980.
DOI : 10.1093/oxfordjournals.jbchem.a132743

C. Knupp, P. K. Luther, and J. M. Squire, Titin Organisation and the 3D Architecture of the Vertebrate-striated Muscle I-band, Journal of Molecular Biology, vol.322, issue.4, pp.731-739, 2002.
DOI : 10.1016/S0022-2836(02)00819-7

D. Labeit, K. Watanabe, C. Witt, H. Fujita, Y. Wu et al., Calcium-dependent molecular spring elements in the giant protein titin, Proceedings of the National Academy of Sciences, vol.100, issue.23, pp.13716-13737, 2003.
DOI : 10.1073/pnas.2235652100

U. K. Laemmli, Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4, Nature, vol.244, issue.5259, pp.680-685, 1970.
DOI : 10.1038/227680a0

M. Lebart and Y. Benyamin, Calpain involvement in the remodeling of cytoskeletal anchorage complexes, FEBS Journal, vol.280, issue.15, pp.3415-3441, 2006.
DOI : 10.1002/(SICI)1097-4547(19960601)44:5<438::AID-JNR4>3.3.CO;2-J

URL : https://hal.archives-ouvertes.fr/hal-00643656

S. Linse, Calcium Binding to Proteins Studied via Competition with Chromophoric Chelators, Methods and Techniques, vol.2, pp.15-24, 2002.
DOI : 10.1385/1-59259-184-1:015

A. D. Liversage, D. Holmes, P. J. Knight, L. Tskhovrebova, and J. A. Trinick, Titin and the sarcomere symmetry paradox11Edited by J. Karn, Journal of Molecular Biology, vol.305, issue.3, pp.401-409, 2001.
DOI : 10.1006/jmbi.2000.4279

H. Ma, C. Fukiage, Y. Kim, M. Duncan, N. Reed et al., Characterization and Expression of Calpain 10. A NOVEL UBIQUITOUS CALPAIN WITH NUCLEAR LOCALIZATION, Journal of Biological Chemistry, vol.276, issue.30, pp.28525-28531, 2001.
DOI : 10.1074/jbc.M100603200

K. Maruyama, Connectin/titin, giant elastic protein of muscle, FASEB J, vol.11, pp.341-346, 1997.

R. L. Mitrovic, B. Pihlar, and P. Simonc, Speciation of trace amounts of aluminium in environmental samples by cation-exchange FPLC - ETAAS, Analusis, vol.26, issue.10, pp.381-388, 1998.
DOI : 10.1051/analusis:1998189

F. Raynaud, C. Bonnal, E. Fernandez, L. Bremaud, M. Cerutti et al., The calpain 1?alpha?actinin interaction. Resting complex between the calcium-dependent protease and its target in cytoskeleton, 2003.
URL : https://hal.archives-ouvertes.fr/hal-01211854

F. Raynaud, G. Carnac, A. Marcilhac, and Y. Benyamin, m-Calpain implication in cell cycle during muscle precursor cell activation, Experimental Cell Research, vol.298, issue.1, pp.48-57, 2004.
DOI : 10.1016/j.yexcr.2004.03.053

F. Raynaud, E. Fernandez, G. Coulis, L. Aubry, X. Vignon et al., Calpain 1-titin interactions concentrate calpain 1 in the Z-band edges and in the N2-line region within the skeletal myofibril, FEBS Journal, vol.268, issue.150, pp.2578-90, 2005.
DOI : 10.1111/j.1742-4658.2005.04683.x

R. Rudolph and H. Lilie, In vitro folding of inclusion body proteins, FASEB J, vol.10, pp.49-56, 1996.

R. Seckler and R. Jaenicke, Protein folding and protein refolding, FASEB J, vol.6, pp.2545-52, 1992.

M. A. Sentandreu, L. Aubry, and A. Ouali, Purification of bovine cathepsin B: proteomic characterization of the different forms and production of specific antibodies, Biochemistry and Cell Biology, vol.81, issue.4, pp.317-326, 2003.
DOI : 10.1139/o03-060

H. Sorimachi, S. Imajoh-ohmi, Y. Emori, H. Kawasaki, S. Ohno et al., Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m-and mu-types. Specific expression of the mRNA in skeletal muscle, J Biol Chem, vol.264, pp.20106-20111, 1989.

H. Sorimachi, S. Ishiura, and K. Suzuki, Structure and physiological function of calpains, Biochemical Journal, vol.328, issue.3, pp.721-732, 1997.
DOI : 10.1042/bj3280721

K. Suzuki, S. Hata, Y. Kawabata, and H. Sorimachi, Structure, Activation, and Biology of Calpain, Diabetes, vol.53, issue.Supplement 1, pp.12-18, 2004.
DOI : 10.2337/diabetes.53.2007.S12

R. Tatsumi, K. Maeda, A. Hattori, and K. Takahashi, Calcium binding to an elastic portion of connectin/titin filaments, Journal of Muscle Research and Cell Motility, vol.22, issue.2, pp.149-62, 2001.
DOI : 10.1023/A:1010349416723

J. A. Trinick, End-filaments: A new structural element of vertebrate skeletal muscle thick filaments, Journal of Molecular Biology, vol.151, issue.2, pp.309-314, 1981.
DOI : 10.1016/0022-2836(81)90517-9

L. Tskhovrebova and J. Trinick, Role of titin in vertebrate striated muscle, Philosophical Transactions of the Royal Society B: Biological Sciences, vol.357, issue.1418, pp.199-206, 2002.
DOI : 10.1098/rstb.2001.1028

X. Vignon, J. Beaulaton, and A. Ouali, Ultrastructural localization of calcium in post-mortem bovine muscle: A cytochemical and X-ray microanalytical study, The Histochemical Journal, vol.21, issue.7, pp.403-411, 1989.
DOI : 10.1007/BF01789738

D. Goll, V. Thompson, H. Li, W. Wei, and J. Cong, The Calpain System, Physiological Reviews, vol.83, issue.3, pp.731-801, 2003.
DOI : 10.1152/physrev.00029.2002

H. Sorimachi, S. Ishiura, and K. Suzuki, Structure and physiological function of calpains, Biochemical Journal, vol.328, issue.3, pp.721-732, 1997.
DOI : 10.1042/bj3280721

E. Carafoli and M. Molinari, Calpain: A Protease in Search of a Function?, Biochemical and Biophysical Research Communications, vol.247, issue.2, pp.193-203, 1998.
DOI : 10.1006/bbrc.1998.8378

K. Wang, Calpain and caspase: can you tell the difference?, Trends in Neurosciences, vol.23, issue.1, pp.20-26, 2000.
DOI : 10.1016/S0166-2236(99)01479-4

S. Baghdiguian, M. Martin, I. Richard, F. Pons, C. Astier et al., Calpain 3 deficiency is associated with myonuclear apoptosis and profound perturbation of the IkappaB alpha ? NF-kappaB pathway in limb-girdle muscular dystrophy type 2A, Nat Med, vol.5, pp.503-511, 1999.

F. Raynaud, G. Carnac, A. Marcilhac, and Y. Benyamin, m-Calpain implication in cell cycle during muscle precursor cell activation, Experimental Cell Research, vol.298, issue.1, pp.48-57, 2004.
DOI : 10.1016/j.yexcr.2004.03.053

T. Yamashima, Ca2+-dependent proteases in ischemic neuronal death, Cell Calcium, vol.36, issue.3-4, pp.285-293, 2004.
DOI : 10.1016/j.ceca.2004.03.001

J. Rios-doria, K. Day, R. Kuefer, M. Rashid, A. Chinnaiyan et al., The Role of Calpain in the Proteolytic Cleavage of E-cadherin in Prostate and Mammary Epithelial Cells, Journal of Biological Chemistry, vol.278, issue.2, pp.1372-1379, 2003.
DOI : 10.1074/jbc.M208772200

S. Strobl, C. Fernandez-catalan, M. Braun, R. Huber, H. Masumoto et al., The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium, Proceedings of the National Academy of Sciences, vol.97, issue.2, pp.588-592, 2000.
DOI : 10.1073/pnas.97.2.588

T. Moldoveanu, C. Hosfield, Z. Jia, J. Elce, and P. Davies, Ca2+-induced structural changes in rat m-calpain revealed by partial proteolysis, Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol.1545, issue.1-2, pp.245-254, 2001.
DOI : 10.1016/S0167-4838(00)00286-7

C. Hosfield, T. Moldoveanu, P. Davies, J. Elce, and Z. Jia, Calpain Mutants with Increased Ca2+ Sensitivity and Implications for the Role of the C2-like Domain, Journal of Biological Chemistry, vol.276, issue.10, pp.7404-7407, 2001.
DOI : 10.1074/jbc.M007352200

M. Michetti, F. Salamino, R. Minafra, E. Melloni, and S. Pontremoli, Calcium-binding properties of human erythrocyte calpain, Biochemical Journal, vol.325, issue.3, pp.721-726, 1997.
DOI : 10.1042/bj3250721

H. Sorimachi, S. Imajoh-ohmi, Y. Emori, H. Kawasaki, S. Ohno et al., Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m-and mu-types. Specific expression of the mRNA in skeletal muscle, J Biol Chem, vol.264, pp.20106-20111, 1989.

H. Ma, C. Fukiage, Y. Kim, M. Duncan, N. Reed et al., Characterization and Expression of Calpain 10. A NOVEL UBIQUITOUS CALPAIN WITH NUCLEAR LOCALIZATION, Journal of Biological Chemistry, vol.276, issue.30, pp.28525-28531, 2001.
DOI : 10.1074/jbc.M100603200

S. Dedieu, G. Mazeres, N. Dourdin, P. Cottin, and J. Brustis, Transactivation of capn2 by Myogenic Regulatory Factors During Myogenesis, Journal of Molecular Biology, vol.326, issue.2, pp.453-465, 2003.
DOI : 10.1016/S0022-2836(02)01310-4

S. Dedieu, S. Poussard, G. Mazeres, F. Grise, E. Dargelos et al., Myoblast migration is regulated by calpain through its involvement in cell attachment and cytoskeletal organization, Experimental Cell Research, vol.292, issue.1, pp.187-200, 2004.
DOI : 10.1016/j.yexcr.2003.08.014

G. Geesink and M. Koohmaraie, Postmortem proteolysis and calpain/calpastatin activity in callipyge and normal lamb biceps femoris during extended postmortem storage., Journal of Animal Science, vol.77, issue.6, pp.1490-1501, 1999.
DOI : 10.2527/1999.7761490x

R. Jackman and S. Kandarian, The molecular basis of skeletal muscle atrophy, AJP: Cell Physiology, vol.287, issue.4, pp.834-843, 2004.
DOI : 10.1152/ajpcell.00579.2003

E. Delgado, G. Geesink, J. Marchello, D. Goll, and M. Koohmaraie, Properties of myofibril-bound calpain activity in longissimus muscle of callipyge and normal sheep., Journal of Animal Science, vol.79, issue.8, pp.2097-2107, 2001.
DOI : 10.2527/2001.7982097x

H. Sorimachi, K. Kinbara, S. Kimura, M. Takahashi, S. Ishiura et al., Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence, J Biol Chem, vol.270, pp.31158-31162, 1995.

K. Kinbara, H. Sorimachi, S. Ishiura, and K. Suzuki, Muscle-Specific Calpain, p94, Interacts with the Extreme C-Terminal Region of Connectin, a Unique Region Flanked by Two Immunoglobulin C2 Motifs, Archives of Biochemistry and Biophysics, vol.342, issue.1, pp.99-107, 1997.
DOI : 10.1006/abbi.1997.0108

M. Taveau, N. Bourg, G. Sillon, C. Roudaut, M. Bartoli et al., Calpain 3 Is Activated through Autolysis within the Active Site and Lyses Sarcomeric and Sarcolemmal Components, Molecular and Cellular Biology, vol.23, issue.24, pp.9127-9135, 2003.
DOI : 10.1128/MCB.23.24.9127-9135.2003

D. Furst, M. Osborn, R. Nave, and K. Weber, The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M line, The Journal of Cell Biology, vol.106, issue.5, pp.1563-1572, 1988.
DOI : 10.1083/jcb.106.5.1563

F. Raynaud, Titins: giant proteins in charge of muscle ultrastructure and elasticity, Calpain 1?titin interactions in myofibrils, pp.293-296, 1995.

L. Tskhovrebova and J. Trinick, Role of titin in vertebrate striated muscle, Philosophical Transactions of the Royal Society B: Biological Sciences, vol.357, issue.1418, pp.199-206, 2002.
DOI : 10.1098/rstb.2001.1028

S. Ishiura, H. Sugita, I. Nonaka, and K. Imahori, Calcium-Activated Neutral Protease: Its Localization in the Myofibril, Especially at the Z-Band1, The Journal of Biochemistry, vol.87, issue.1, pp.343-346, 1980.
DOI : 10.1093/oxfordjournals.jbchem.a132743

W. Dayton and J. Schollmeyer, Immunocytochemical localization of a calcium-activated protease in skeletal muscle cells, Experimental Cell Research, vol.136, issue.2, pp.423-433, 1981.
DOI : 10.1016/0014-4827(81)90022-7

N. Yoshimura, T. Murachi, R. Heath, J. Kay, B. Jasani et al., Immunogold electron-microscopic localisation of calpain I in skeletal muscle of rats, Cell and Tissue Research, vol.244, issue.2, pp.265-270, 1986.
DOI : 10.1007/BF00219201

N. Konig, F. Raynaud, H. Feane, M. Durand, N. Mestre-frances et al., Calpain 3 is expressed in astrocytes of rat and Microcebus brain, Journal of Chemical Neuroanatomy, vol.25, issue.2, pp.129-136, 2003.
DOI : 10.1016/S0891-0618(02)00102-3

P. Salmikangas, O. Mykkanen, M. Gronholm, L. Heiska, J. Kere et al., Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy, Human Molecular Genetics, vol.8, issue.7, pp.1329-1336, 1999.
DOI : 10.1093/hmg/8.7.1329

P. Van-der-ven, S. Wiesner, P. Salmikangas, D. Auerbach, M. Himmel et al., Indications for a Novel Muscular Dystrophy Pathway, The Journal of Cell Biology, vol.18, issue.2, pp.235-248, 2000.
DOI : 10.1093/emboj/17.6.1614

J. Bendall, POSTMORTEM CHANGES IN MUSCLE, The Structure and Function of Muscle, pp.227-274, 1973.
DOI : 10.1016/B978-0-12-119102-3.50012-4

X. Vignon, J. Beaulaton, and A. Ouali, Ultrastructural localization of calcium in post-mortem bovine muscle: A cytochemical and X-ray microanalytical study, The Histochemical Journal, vol.21, issue.7, pp.403-411, 1989.
DOI : 10.1007/BF01789738

C. Astier, J. Labbe, C. Roustan, and Y. Benyamin, Sarcomeric disorganization in post-mortem fish muscles, Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, vol.100, issue.3, pp.459-465, 1991.
DOI : 10.1016/0305-0491(91)90204-Q

E. Huff-lonergan, T. Mitsuhashi, D. Beekman, F. Parrish, D. Olson et al., Proteolysis of specific muscle structural proteins by mu-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle., Journal of Animal Science, vol.74, issue.5, pp.993-1008, 1996.
DOI : 10.2527/1996.745993x

K. Maruyama, M. Kimura, S. Kimura, K. Ohashi, K. Suzuki et al., Connectin, an Elastic Protein of Muscle. Effects of Proteolytic Enzymes in Situ1, The Journal of Biochemistry, vol.89, issue.3, pp.711-715, 1981.
DOI : 10.1093/oxfordjournals.jbchem.a133250

C. Lim, C. Zuppinger, X. Guo, G. Kuster, M. Helmes et al., Anthracyclines Induce Calpain-dependent Titin Proteolysis and Necrosis in Cardiomyocytes, Journal of Biological Chemistry, vol.279, issue.9, pp.8290-8299, 2004.
DOI : 10.1074/jbc.M308033200

R. Yarom and U. Meiri, N Lines in Striated Muscle: a Site of Intracellular Ca2+, Nature New Biology, vol.234, issue.51, pp.254-256, 1971.
DOI : 10.1038/newbio234254a0

R. Tatsumi, K. Maeda, A. Hattori, and K. Takahashi, Calcium binding to an elastic portion of connectin ? titin filaments, Journal of Muscle Research and Cell Motility, vol.22, issue.2, pp.149-162, 2001.
DOI : 10.1023/A:1010349416723

F. Raynaud, C. Bonnal, E. Fernandez, L. Bremaud, M. Cerutti et al., The calpain???1-??-actinin interaction, European Journal of Biochemistry, vol.159, issue.23, pp.4662-4670, 2003.
DOI : 10.1046/j.1432-1033.2003.03859.x

URL : https://hal.archives-ouvertes.fr/hal-01211854

G. Coulis, M. Sentandreu, N. Bleimling, M. Gautel, Y. Benyamin et al., Myofibrillar tightly bound calcium in skeletal muscle fibers: a possible role of this cation in titin strands aggregation, FEBS Letters, vol.26, issue.1-3, pp.271-275, 2004.
DOI : 10.1016/S0014-5793(03)01436-4

J. Barnes and A. Gomes, PEST sequences in calmodulin-binding proteins, Mol Cell Biochem, vol.149150, pp.17-27, 1995.

J. Barnes and A. Gomes, Proteolytic signals in the primary structure of annexins, Molecular and Cellular Biochemistry, vol.231, issue.1/2, pp.1-7, 2002.
DOI : 10.1023/A:1014476123120

R. Wallace, E. Tallant, and M. Mcmanus, Human platelet calmodulin-binding proteins: identification and calcium-dependent proteolysis upon platelet activation, Biochemistry, vol.26, issue.10, pp.2766-2773, 1987.
DOI : 10.1021/bi00384a017

S. Shumway, M. Maki, and S. Miyamoto, The PEST Domain of I??B?? Is Necessary and Sufficient forin Vitro Degradation by ??-Calpain, Journal of Biological Chemistry, vol.274, issue.43, pp.30874-30881, 1999.
DOI : 10.1074/jbc.274.43.30874

S. Kimura, T. Matsuura, S. Ohtsuka, Y. Nakauchi, A. Matsuno et al., Characterization and localization of ??-connectin (titin 1): An elastic protein isolated from rabbit skeletal muscle, Journal of Muscle Research and Cell Motility, vol.7, issue.1, pp.39-47, 1992.
DOI : 10.1007/BF01738426

Y. Kawamura, H. Kume, Y. Itoh, S. Ohtsuka, S. Kimura et al., Localization of Three Fragments of Connectin in Chicken Breast Muscle Sarcomeres1, The Journal of Biochemistry, vol.117, issue.1, pp.201-207, 1995.
DOI : 10.1093/oxfordjournals.jbchem.a124711

Y. Bassaglia, J. Cebrian, S. Covan, M. Garcia, and J. Foucrier, Proteasomes are tightly associated to myofibrils in mature skeletal muscle, Experimental Cell Research, vol.302, issue.2, pp.221-232, 2005.
DOI : 10.1016/j.yexcr.2004.08.038

R. Taylor, I. Papa, C. Astier, F. Ventre, Y. Benyamin et al., Fish muscle cytoskeleton integrity is not dependent on intact thin filaments, Journal of Muscle Research and Cell Motility, vol.18, issue.3, pp.285-294, 1997.
DOI : 10.1023/A:1018665924412

M. Miller, M. Bang, C. Witt, D. Labeit, C. Trombitas et al., The Muscle Ankyrin Repeat Proteins: CARP, ankrd2/Arpp and DARP as a Family of Titin Filament-based Stress Response Molecules, Journal of Molecular Biology, vol.333, issue.5, pp.951-964, 2003.
DOI : 10.1016/j.jmb.2003.09.012

F. Raynaud, Calpain 1-titin interactions concentrate calpain 1 in the Z-band edges and in the N2-line region within the skeletal myofibril, FEBS Journal, vol.268, issue.150, pp.2578-2590, 2005.
DOI : 10.1111/j.1742-4658.2005.04683.x

S. Kojic, E. Medeot, E. Guccione, H. Krmac, I. Zara et al., The Ankrd2 Protein, a Link Between the Sarcomere and the Nucleus in Skeletal Muscle, Journal of Molecular Biology, vol.339, issue.2, pp.313-325, 2004.
DOI : 10.1016/j.jmb.2004.03.071

C. Astier, F. Raynaud, M. Lebart, C. Roustan, and Y. Benyamin, Binding of a native titin fragment to actin is regulated by PIP2, FEBS Letters, vol.22, issue.1, pp.95-98, 1998.
DOI : 10.1016/S0014-5793(98)00572-9

M. Sebestyen, J. Wolff, and M. Greaser, Characterization of a 5.4 kb cDNA fragment from the Z-line region of rabbit cardiac titin reveals phosphorylation sites for proline-directed kinases, J Cell Sci, vol.108, pp.3029-3037, 1995.

K. Trombitas, M. Greaser, G. French, and H. Granzier, PEVK Extension of Human Soleus Muscle Titin Revealed by Immunolabeling with the Anti-titin Antibody 9D10, Journal of Structural Biology, vol.122, issue.1-2, pp.188-196, 1998.
DOI : 10.1006/jsbi.1998.3984

V. Thompson and D. Goll, Purification of mucalpain , m-calpain, and calpastatin from animal tissues, Methods Mol Biol, vol.144, pp.3-16, 2000.

C. Astier, J. Labbe, C. Roustan, and Y. Benyamin, Effects of different enzymic treatments on the release of titin fragments from rabbit skeletal myofibrils. Purification of an 800 kDa titin polypeptide, Biochemical Journal, vol.290, issue.3, pp.731-734, 1993.
DOI : 10.1042/bj2900731

F. Raynaud, C. Astier, and Y. Benyamin, Evidence for a direct but sequential binding of titin to tropomyosin and actin filaments, Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol.1700, issue.2, pp.171-178, 2004.
DOI : 10.1016/j.bbapap.2004.05.001

N. Niederlander, F. Raynaud, C. Astier, and P. Chaussepied, Regulation of the actin-myosin interaction by titin, European Journal of Biochemistry, vol.481, issue.22, pp.4572-4581, 2004.
DOI : 10.1074/jbc.M008851200

M. Gautel, D. Goulding, B. Bullard, K. Weber, and D. Furst, The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers, J Cell Sci, vol.109, pp.2747-2754, 1996.

M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Analytical Biochemistry, vol.72, issue.1-2, pp.248-254, 1976.
DOI : 10.1016/0003-2697(76)90527-3

U. Laemmli, Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4, Nature, vol.244, issue.5259, pp.680-685, 1970.
DOI : 10.1038/227680a0

P. Matsudaira, Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes, J Biol Chem, vol.262, pp.10035-10038, 1987.

J. Stirling, Immuno- and affinity probes for electron microscopy: a review of labeling and preparation techniques., Journal of Histochemistry & Cytochemistry, vol.38, issue.2, pp.145-157, 1990.
DOI : 10.1177/38.2.2405054

J. Appleton and D. Morris, The use of the potassium pyroantimonate-osmium method as a means of identifying and localizing calcium at the ultrastructural level in the cells of calcifying systems., Journal of Histochemistry & Cytochemistry, vol.27, issue.2, pp.676-680, 1979.
DOI : 10.1177/27.2.448059

C. Mejean, M. Lebart, M. Boyer, C. Roustan, and Y. Benyamin, Localization and identification of actin structures involved in the filamin - actin interaction, European Journal of Biochemistry, vol.581, issue.2, pp.555-562, 1992.
DOI : 10.1016/0014-5793(85)81125-X

C. Renoult, L. Blondin, A. Fattoum, D. Ternent, S. Maciver et al., Binding of gelsolin domain 2 to actin, European Journal of Biochemistry, vol.34, issue.23, pp.6165-6175, 2001.
DOI : 10.1046/j.0014-2956.2001.02574.x

D. O. Furst, M. Osborn, R. Nave, and K. Weber, The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M line, The Journal of Cell Biology, vol.106, issue.5, pp.1563-1572, 1988.
DOI : 10.1083/jcb.106.5.1563

A. D. Liversage, D. Holmes, P. J. Knight, L. Tskhovrebova, and J. A. Trinick, Titin and the sarcomere symmetry paradox11Edited by J. Karn, Journal of Molecular Biology, vol.305, issue.3, pp.401-409, 2001.
DOI : 10.1006/jmbi.2000.4279

C. Knupp, P. K. Luther, and J. M. Squire, Titin Organisation and the 3D Architecture of the Vertebrate-striated Muscle I-band, Journal of Molecular Biology, vol.322, issue.4, pp.731-739, 2002.
DOI : 10.1016/S0022-2836(02)00819-7

J. A. Trinick, End-filaments: A new structural element of vertebrate skeletal muscle thick filaments, Journal of Molecular Biology, vol.151, issue.2, pp.309-314, 1981.
DOI : 10.1016/0022-2836(81)90517-9

T. Funatsu, E. Kono, H. Higuchi, S. Kimura, S. Ishiwata et al., Elastic filaments in situ in cardiac muscle: deep-etch replica analysis in combination with selective removal of actin and myosin filaments, The Journal of Cell Biology, vol.120, issue.3, pp.711-724, 1993.
DOI : 10.1083/jcb.120.3.711

R. Yarom and U. Meiri, N Lines in Striated Muscle: a Site of Intracellular Ca2+, Nature New Biology, vol.234, issue.51, pp.254-256, 1971.
DOI : 10.1038/newbio234254a0

X. Vignon, J. Beaulaton, and A. Ouali, Ultrastructural localization of calcium in post-mortem bovine muscle: A cytochemical and X-ray microanalytical study, The Histochemical Journal, vol.21, issue.7, pp.403-411, 1989.
DOI : 10.1007/BF01789738

G. Musco, C. Tziatzios, P. Schuck, and A. Pastore, Dissecting Titin into Its Structural Motifs: Identification of an .alpha.-Helix Motif near the Titin N-Terminus, Biochemistry, vol.34, issue.2, pp.553-561, 1995.
DOI : 10.1021/bi00002a021

R. Tatsumi, K. Shimada, and A. Hattori, Fluorescence Detection of Calcium-Binding Proteins with Quinoline Ca-Indicator Quin2, Analytical Biochemistry, vol.254, issue.1, pp.126-131, 1997.
DOI : 10.1006/abio.1997.2369

M. J. Berridge, M. D. Bootman, and H. L. Roderick, Calcium: Calcium signalling: dynamics, homeostasis and remodelling, Nature Reviews Molecular Cell Biology, vol.4, issue.7, pp.517-529, 2003.
DOI : 10.1038/nrm1155

C. Cohen and D. A. Parry, ??-Helical coiled coils and bundles: How to design an ??-helical protein, Proteins: Structure, Function, and Genetics, vol.77, issue.1, pp.1-15, 1990.
DOI : 10.1002/prot.340070102

B. Kolmerer, N. Olivieri, B. Herrmann, and S. Labeit, A systematic search of the data bases for sequences homologous to titin/connectin, Advances in Biophysics, vol.33, pp.3-11, 1996.
DOI : 10.1016/0065-227X(96)81659-5

G. Coulis, Myofibrillar tightly bound calcium in skeletal muscle fibers: a possible role of this cation in titin strands aggregation, FEBS Letters, vol.26, issue.1-3, pp.271-275, 2004.
DOI : 10.1016/S0014-5793(03)01436-4