E. P. Hoffman, R. H. Brown, J. Kunkel, and L. M. , Dystrophin: the protein product of the Duchenne muscular dystrophy locus, Cell, vol.51, pp.919-947, 1987.

J. Finsterer and C. Stollberger, The heart in human dystrophinopathies, Cardiology, vol.99, pp.1-19, 2003.

J. B. Su, O. Cazorla, S. Blot, N. Blanchard-gutton, A. Mou et al., Bradykinin restores left ventricular function, sarcomeric protein phosphorylation, and e/nNOS levels in dogs with Duchenne muscular dystrophy cardiomyopathy, Cardiovasc Res, vol.95, pp.86-96, 2012.
URL : https://hal.archives-ouvertes.fr/inserm-00719576

D. Townsend, I. Turner, S. Yasuda, J. Martindale, J. Davis et al., Chronic administration of membrane sealant prevents severe cardiac injury and ventricular dilatation in dystrophic dogs, J Clin Invest, vol.120, pp.1140-50, 2010.

A. Mou, Y. Le-guennec, J. Y. Mosca, E. De-tombe, P. P. Cazorla et al., Differential contribution of cardiac sarcomeric proteins in the myofibrillar force response to stretch, Pflugers Arch, vol.457, pp.25-36, 2008.
URL : https://hal.archives-ouvertes.fr/hal-01824379

A. Mou, Y. Reboul, C. Andre, L. Lacampagne, A. Cazorla et al., Late exercise training improves nonuniformity of transmural myocardial function in rats with ischaemic heart failure, Cardiovasc Res, vol.81, pp.555-64, 2009.
URL : https://hal.archives-ouvertes.fr/hal-01824366

O. Cazorla, L. Guennec, J. Y. White, and E. , Length-tension relationships of sub-epicardial and subendocardial single ventricular myocytes from rat and ferret hearts, J Mol Cell Cardiol, vol.32, pp.735-779, 2000.
URL : https://hal.archives-ouvertes.fr/hal-01824407

O. Cazorla, S. Szilagyi, L. Guennec, J. Y. Vassort, G. Lacampagne et al., Transmural stretchdependent regulation of contractile properties in rat heart and its alteration after myocardial infarction, FASEB J, vol.19, pp.88-90, 2005.
URL : https://hal.archives-ouvertes.fr/hal-01824390

B. J. Cooper, N. J. Winand, H. Stedman, B. A. Valentine, E. P. Hoffman et al., The homologue of the Duchenne locus is defective in X-linked muscular dystrophy of dogs, Nature, vol.334, pp.154-160, 1988.

A. Dg and J. C. Kentish, The cellular basis of the length-tension relation in cardiac muscle, J Mol Cell Cardiol, vol.17, pp.821-861, 1985.

O. Cazorla and A. Lacampagne, Regional variation in myofilament length-dependent activation, Pflugers Arch, vol.462, pp.15-28, 2011.
URL : https://hal.archives-ouvertes.fr/inserm-00573260

P. P. De-tombe, R. D. Mateja, K. Tachampa, A. Mou, Y. et al., Myofilament length dependent activation, J Mol Cell Cardiol, vol.48, pp.851-859, 2010.

N. Witayavanitkul, A. Mou, Y. Kuster, D. W. Khairallah, R. J. Sarkey et al., Myocardial infarction-induced N-terminal fragment of cardiac myosin-binding protein C (cMyBP-C) impairs myofilament function in human myocardium, J Biol Chem, vol.289, pp.8818-8845, 2014.

R. Fischetti, S. Stepanov, G. Rosenbaum, R. Barrea, E. Black et al., The BioCAT undulator beamline 18ID: a facility for biological non-crystalline diffraction and X-ray absorption spectroscopy at the Advanced Photon Source, J Synchrotron Radiat, vol.11, pp.399-405, 2004.

T. C. Irving, J. Konhilas, D. Perry, R. Fischetti, and P. P. De-tombe, Myofilament lattice spacing as a function of sarcomere length in isolated rat myocardium, Am J Physiol Heart Circ Physiol, vol.279, pp.2568-73, 2000.

L. C. Yu, A. C. Steven, G. R. Naylor, R. C. Gamble, and R. J. Podolsky, Distribution of mass in relaxed frog skeletal muscle and its redistribution upon activation, Biophys J, vol.47, pp.311-332, 1985.

T. C. Irving and B. M. Millman, Changes in thick filament structure during compression of the filament lattice in relaxed frog sartorius muscle, J Muscle Res Cell Motil, vol.10, pp.385-94, 1989.

L. Andre, J. Fauconnier, C. Reboul, C. Feillet-coudray, P. Meschin et al., Subendocardial increase in reactive oxygen species production affects regional contractile function in ischemic heart failure, Antioxid Redox Signal, vol.18, pp.1009-1029, 2013.
URL : https://hal.archives-ouvertes.fr/hal-01837560

!. Citation-!!!-3,

B. G. Patel, T. Wilder, R. Solaro, R. J. Solaro, H. et al., Novel control of cardiac myofilament response to calcium by Sglutathionylation at specific sites of myosin binding protein C, Front Physiol, vol.4, pp.355-66, 2013.

J. P. Konhilas, T. C. Irving, and P. P. De-tombe, Length-dependent activation in three striated muscle types of the rat, J Physiol, vol.544, pp.225-261, 2002.

E. J. Lee, J. Nedrud, P. Schemmel, M. Gotthardt, I. Tc et al., Titin isoform variance and length dependence of activation in skinned bovine cardiac muscle, Arch Biochem Biophys, vol.535, pp.147-54, 2003.

J. P. Konhilas, T. C. Irving, and P. P. De-tombe, Myofilament calcium sensitivity in skinned rat cardiac trabeculae: role of interfilament spacing, Circ Res, vol.90, pp.59-65, 2002.

O. Cazorla, Y. Wu, T. C. Irving, and H. Granzier, Titin-based modulation of calcium sensitivity of active tension in mouse skinned cardiac myocytes, Circ Res, vol.88, pp.1028-1063, 2001.
URL : https://hal.archives-ouvertes.fr/hal-01824396

G. P. Farman, J. S. Walker, P. P. De-tombe, and T. C. Irving, Impact of osmotic compression on sarcomere structure and myofilament calcium sensitivity of isolated rat myocardium, Am J Physiol Heart Circ Physiol, vol.291, pp.1847-55, 2006.

G. P. Farman, D. Gore, A. E. Schoenfelt, K. , I. Tc et al., Myosin head orientation: a structural determinant for the Frank-Starling relationship, Am J Physiol Heart Circ Physiol, vol.300, pp.2155-60, 2011.

Y. Ait-mou, K. Hsu, G. P. Farman, M. Kumar, M. L. Greaser et al., Titin strain contributes to the Frank-Starling law of the heart by structural rearrangements of both thin-and thickfilament proteins, Proc Natl Acad Sci U S A, vol.113, pp.2306-2317, 2016.

A. Van-der-toorn, P. Barenbrug, G. Snoep, F. H. Van-der-veen, T. Delhaas et al., Transmural gradients of cardiac myofiber shortening in aortic valve stenosis patients using MRI tagging, Am J Physiol Heart Circ Physiol, vol.283, pp.1609-1624, 2002.

G. Derumeaux, P. Mulder, V. Richard, A. Chagraoui, C. Nafeh et al.,

, Tissue Doppler imaging differentiates physiological from pathological pressure-overload left ventricular hypertrophy in rats, Circulation, vol.105, pp.1602-1610, 2002.

J. C. Dosch, M. F. Szwerc, J. C. Lin, J. A. Magovern, and J. G. Edwards, Pressure overload induces heterologous expression of the atrial natriuretic factor (ANF) gene, IUBMB Life, vol.52, pp.315-324, 2001.

J. Prestle, S. Dieterich, M. Preuss, U. Bieligk, and G. Hasenfuss, Heterogeneous transmural gene expression of calcium-handling proteins and natriuretic peptides in the failing human heart, Cardiovasc Res, vol.43, pp.323-354, 1999.

D. D. Spragg, C. Leclercq, M. Loghmani, O. P. Faris, R. S. Tunin et al., Regional alterations in protein expression in the dyssynchronous failing heart, Circulation, vol.108, pp.929-961, 2003.

M. Kindo, S. Gerelli, J. Bouitbir, T. Hoang-minh, A. L. Charles et al., Left Ventricular Transmural Gradient in Mitochondrial Respiration Is Associated with Increased Sub-Endocardium Nitric Oxide and Reactive Oxygen Species Productions, Front Physiol, vol.7, p.331, 2016.

J. R. Macdonald, M. Oellermann, S. Rynbeck, G. Chang, K. Ruggiero et al.,

, Transmural differences in respiratory capacity across the rat left ventricle in health, aging, and streptozotocin-induced diabetes mellitus: evidence that mitochondrial dysfunction begins in the subepicardium, Am J Physiol Cell Physiol, vol.300, pp.246-55, 2011.

M. Sb and P. P. De-tombe, Troponin phosphorylation and myofilament Ca2+-sensitivity in heart failure: increased or decreased?, J Mol Cell Cardiol, vol.45, pp.603-610, 2008.

N. Hamdani, V. Kooij, S. Van-dijk, D. Merkus, W. J. Paulus et al., Sarcomeric dysfunction in heart failure, Cardiovasc Res, vol.77, pp.649-58, 2008.

E. E. Jweied, R. D. Mckinney, L. A. Walker, I. Brodsky, A. S. Geha et al., Depressed cardiac myofilament function in human diabetes mellitus, Am J Physiol Heart Circ Physiol, vol.289, pp.2478-83, 2005.

P. , J. K. Stienen, and G. J. , Increased Ca2+-sensitivity of the contractile apparatus in end-stage human heart failure results from altered phosphorylation of contractile proteins, Cardiovasc Res, vol.57, pp.37-47, 2003.

J. Van-der-velden, L. J. Klein, R. Zaremba, N. M. Boontje, M. A. Huybregts et al.,

J. W. Jong, C. A. Visser, F. C. Visser, and G. J. Stienen, Effects of calcium, inorganic phosphate, and pH on isometric force in single skinned cardiomyocytes from donor and failing human hearts, Circulation, vol.104, pp.1140-1146, 2001.

N. Hamdani, K. G. Bishu, V. Frieling-salewsky, M. , R. Mm et al., Deranged myofilament phosphorylation and function in experimental heart failure with preserved ejection fraction, Cardiovasc Res, vol.97, pp.464-71, 2013.

J. P. Konhilas, T. C. Irving, B. M. Wolska, E. E. Jweied, A. F. Martin et al., Troponin I in the murine myocardium: influence on length-dependent activation and interfilament spacing, J Physiol, vol.547, pp.951-61, 2003.

O. Cazorla, S. Szilagyi, N. Vignier, G. Salazar, E. Kramer et al., Length and protein kinase A modulations of myocytes in cardiac myosin binding protein C-deficient mice, Cardiovasc Res, vol.69, pp.370-80, 2006.
URL : https://hal.archives-ouvertes.fr/hal-01824389

B. A. Colson, T. Bekyarova, D. P. Fitzsimons, T. C. Irving, and R. L. Moss, Radial displacement of myosin cross-bridges in mouse myocardium due to ablation of myosin binding protein-C, J Mol Biol, vol.367, pp.36-41, 2007.

R. Mamidi, K. S. Gresham, and J. E. Stelzer, Length-dependent changes in contractile dynamics are blunted due to cardiac myosin binding protein-C ablation, Front Physiol, vol.5, p.461, 2014.

B. A. Colson, T. Bekyarova, M. R. Locher, D. P. Fitzsimons, T. C. Irving et al., Protein kinase Amediated phosphorylation of cMyBP-C increases proximity of myosin heads to actin in resting myocardium, Circ Res, vol.103, pp.244-51, 2008.

B. Brenner and E. Eisenberg, Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution, Proc Natl Acad Sci, vol.83, pp.3542-3548, 1986.

B. S. Pan and R. J. Solaro, Calcium-binding properties of troponin C in detergent-skinned heart muscle fibers, J Biol Chem, vol.262, pp.7839-7888, 1987.

J. D. Hannon, M. Da, and A. M. Gordon, Effects of cycling and rigor crossbridges on the conformation of cardiac troponin C, Circ Res, vol.71, pp.984-91, 1992.

R. L. Moss, M. Razumova, and D. P. Fitzsimons, Myosin crossbridge activation of cardiac thin filaments: implications for myocardial function in health and disease, Circ Res, vol.94, pp.1290-300, 2004.

P. A. Hofmann and F. Fuchs, Effect of length and cross-bridge attachment on Ca2+ binding to cardiac troponin C, Am J Physiol, vol.253, pp.90-96, 1987.

B. C. Tanner, G. P. Farman, T. C. Irving, D. W. Maughan, B. M. Palmer et al., Thick-to-thin filament surface distance modulates cross-bridge kinetics in Drosophila flight muscle, Biophys J, vol.103, pp.1275-84, 2012.

T. Kampourakis, Y. B. Sun, and M. Irving, Myosin light chain phosphorylation enhances contraction of heart muscle via structural changes in both thick and thin filaments, Proc Natl Acad Sci, vol.113, pp.3039-3086, 2016.

W. G. Kerrick, K. Kazmierczak, Y. Xu, W. Y. Szczesna-cordary, and D. , Malignant familial hypertrophic cardiomyopathy D166V mutation in the ventricular myosin regulatory light chain causes profound effects in skinned and intact papillary muscle fibers from transgenic mice, FASEB J, vol.23, pp.855-65, 2009.

C. C. Yuan, P. Muthu, K. Kazmierczak, J. Liang, W. Huang et al., Constitutive phosphorylation of cardiac myosin regulatory light chain prevents development of hypertrophic cardiomyopathy in mice, Proc Natl Acad Sci U S A, vol.112, pp.4138-4184, 2015.

E. Donal, C. Bergerot, H. Thibault, L. Ernande, J. Loufoua et al., Influence of afterload on left ventricular radial and longitudinal systolic functions: a two-dimensional strain imaging study, Eur J Echocardiogr, vol.10, pp.914-935, 2009.
URL : https://hal.archives-ouvertes.fr/hal-00911661

V. Chetboul, C. Escriou, D. Tessier, V. Richard, J. L. Pouchelon et al., Tissue Doppler imaging detects early asymptomatic myocardial abnormalities in a dog model of Duchenne's cardiomyopathy, Eur Heart J, vol.25, pp.1934-1943, 2004.

A. Mou, Y. Toth, A. Cassan, C. Czuriga, D. De-tombe et al., Beneficial effects of SR33805 in failing myocardium, Cardiovasc Res, vol.91, pp.412-421, 2011.
URL : https://hal.archives-ouvertes.fr/hal-01824337