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Biochemistry Research International
Volume 2012 (2012), Article ID 824068, 11 pages
Cardiomyopathy-Related Mutations in Cardiac Troponin C, L29Q and G159D, Have Divergent Effects on Rat Cardiac Myofiber Contractile Dynamics
Department of Veterinary and Comparative Anatomy, Pharmacology, and Physiology (VCAPP), Washington State University, Pullman, WA 99164-6520, USA
Received 14 May 2012; Revised 6 July 2012; Accepted 8 August 2012
Academic Editor: Danuta Szczesna-Cordary
Copyright © 2012 Sampath K. Gollapudi and Murali Chandra. 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.
- B. Hoffmann, H. Schmidt-Traub, A. Perrot, K. J. Osterziel, and R. Gessner, “First mutation in cardiac troponin C, L29Q, in a patient with hypertrophic cardiomyopathy,” Human Mutation, vol. 17, no. 6, p. 524, 2001.
- A. P. Landstrom, M. S. Parvatiyar, J. R. Pinto et al., “Molecular and functional characterization of novel hypertrophic cardiomyopathy susceptibility mutations in TNNC1-encoded troponin C,” Journal of Molecular and Cellular Cardiology, vol. 45, no. 2, pp. 281–288, 2008.
- W. K. Chung, C. Kitner, and B. J. Maron, “Novel frameshift mutation in Troponin C (TNNC1) associated with hypertrophic cardiomyopathy and sudden death,” Cardiology in the Young, vol. 21, no. 3, pp. 345–348, 2011.
- C. C. Lim, H. Yang, M. Yang et al., “A novel mutant cardiac troponin C disrupts molecular motions critical for calcium binding affinity and cardiomyocyte contractility,” Biophysical Journal, vol. 94, no. 9, pp. 3577–3589, 2008.
- J. Mogensen, R. T. Murphy, T. Shaw et al., “Severe disease expression of cardiac troponin C and T mutations in patients with idiopathic dilated cardiomyopathy,” Journal of the American College of Cardiology, vol. 44, no. 10, pp. 2033–2040, 2004.
- R. E. Hershberger, N. Norton, A. Morales, D. Li, J. D. Siegfried, and J. Gonzalez-Quintana, “Coding sequence rare variants identified in MYBPC3, MYH6, TPM1, TNNC1, and TNNI3 from 312 patients with familial or idiopathic dilated cardiomyopathy,” Circulation, vol. 3, no. 2, pp. 155–161, 2010.
- K. B. Campbell, M. V. Razumova, R. D. Kirkpatrick, and B. K. Slinker, “Nonlinear myofilament regulatory processes affect frequency-dependent muscle fiber stiffness,” Biophysical Journal, vol. 81, no. 4, pp. 2278–2296, 2001.
- K. B. Campbell, M. V. Razumova, R. D. Kirkpatrick, and B. K. Slinker, “Myofilament kinetics in isometric twitch dynamics,” Annals of Biomedical Engineering, vol. 29, no. 5, pp. 384–405, 2001.
- T. E. Gillis, C. R. Marshall, and G. F. Tibbits, “Functional and evolutionary relationships of troponin C,” Physiological Genomics, vol. 32, no. 1, pp. 16–27, 2007.
- B. Liang, F. Chung, Y. Qu et al., “Familial hypertrophic cardiomyopathy-related cardiac troponin C mutation L29Q affects Ca2+ binding and myofilament contractility,” Physiological Genomics, vol. 33, no. 2, pp. 257–266, 2008.
- A. Schmidtmann, C. Lindow, S. Villard et al., “Cardiac troponin C-L29Q, related to hypertrophic cardiomyopathy, hinders the transduction of the protein kinase A dependent phosphorylation signal from cardiac troponin I to C,” FEBS Journal, vol. 272, no. 23, pp. 6087–6097, 2005.
- J. D. Potter, Z. Sheng, B. S. Pan, and J. Zhao, “A direct regulatory role for troponin T and a dual role for troponin C in the Ca2+ regulation of muscle contraction,” Journal of Biological Chemistry, vol. 270, no. 6, pp. 2557–2562, 1995.
- S. Takeda, A. Yamashita, K. Maeda, and Y. Maéda, “Structure of the core domain of human cardiac troponin in the Ca2+-saturated form,” Nature, vol. 424, no. 6944, pp. 35–41, 2003.
- D. Dweck, N. Hus, and J. D. Potter, “Challenging current paradigms related to cardiomyopathies: are changes in the Ca2+ sensitivity of myofilaments containing cardiac troponin C mutations (G159D and L29Q) good predictors of the phenotypic outcomes?” Journal of Biological Chemistry, vol. 283, no. 48, pp. 33119–33128, 2008.
- A. Neulen, R. Stehle, and G. Pfitzer, “The cardiac troponin C mutation Leu29Gln found in a patient with hypertrophic cardiomyopathy does not alter contractile parameters in skinned murine myocardium,” Basic Research in Cardiology, vol. 104, no. 6, pp. 751–760, 2009.
- E. C. Dyer, A. M. Jacques, A. C. Hoskins et al., “Functional analysis of a unique troponin c mutation, gly159asp, that causes Familial dilated cardiomyopathy, studied in explanted heart muscle,” Circulation, vol. 2, no. 5, pp. 456–464, 2009.
- M. Mirza, S. Marston, R. Willott et al., “Dilated cardiomyopathy mutations in three thin filament regulatory proteins result in a common functional phenotype,” Journal of Biological Chemistry, vol. 280, no. 31, pp. 28498–28506, 2005.
- P. Robinson, P. J. Griffiths, H. Watkins, and C. S. Redwood, “Dilated and hypertrophic cardiomyopathy mutations in troponin and α-tropomyosin have opposing effects on the calcium affinity of cardiac thin filaments,” Circulation Research, vol. 101, no. 12, pp. 1266–1273, 2007.
- B. J. Biesiadecki, T. Kobayashi, J. S. Walker, R. J. Solaro, and P. P. de Tombe, “The troponin C G159D mutation blunts myofilament desensitization induced by troponin I Ser23/24 phosphorylation,” Circulation Research, vol. 100, no. 10, pp. 1486–1493, 2007.
- L. C. Preston, C. C. Ashley, and C. S. Redwood, “DCM troponin C mutant Gly159Asp blunts the response to troponin phosphorylation,” Biochemical and Biophysical Research Communications, vol. 360, no. 1, pp. 27–32, 2007.
- M. Chandra, M. L. Tschirgi, S. J. Ford, B. K. Slinker, and K. B. Campbell, “Interaction between myosin heavy chain and troponin isoforms modulate cardiac myofiber contractile dynamics,” American Journal of Physiology, vol. 293, no. 4, pp. R1595–R1607, 2007.
- M. Chandra, M. L. Tschirgi, I. Rajapakse, and K. B. Campbell, “Troponin T modulates sarcomere length-dependent recruitment of cross-bridges in cardiac muscle,” Biophysical Journal, vol. 90, no. 8, pp. 2867–2876, 2006.
- M. Chandra, V. L. M. Rundell, J. C. Tardiff, L. A. Leinwand, P. P. De Tombe, and R. J. Solaro, “Ca2+ activation of myofilaments from transgenic mouse hearts expressing R92Q mutant cardiac troponin T,” American Journal of Physiology, vol. 280, no. 2, pp. H705–H713, 2001.
- X. Guo, J. Wattanapermpool, K. A. Palmiter, A. M. Murphy, and R. J. Solaro, “Mutagenesis of cardiac troponin I. Role of the unique NH2-terminal peptide in myofilament activation,” Journal of Biological Chemistry, vol. 269, no. 21, pp. 15210–15216, 1994.
- B. S. Pan and R. G. Johnson, “Interaction of cardiotonic thiadiazinone derivatives with cardiac troponin C,” Journal of Biological Chemistry, vol. 271, no. 2, pp. 817–823, 1996.
- D. E. Montgomery, J. C. Tardiff, and M. Chandra, “Cardiac troponin T mutations: correlation between the type of mutation and the nature of myofilament dysfunction in transgenic mice,” Journal of Physiology, vol. 536, no. 2, pp. 583–592, 2001.
- J. C. Tardiff, S. M. Factor, B. D. Tompkins et al., “A truncated cardiac troponin T molecule in transgenic mice suggests multiple cellular mechanisms for familial hypertrophic cardiomyopathy,” Journal of Clinical Investigation, vol. 101, no. 12, pp. 2800–2811, 1998.
- M. Chandra, M. L. Tschirgi, and J. C. Tardiff, “Increase in tension-dependent ATP consumption induced by cardiac troponin T mutation,” American Journal of Physiology, vol. 289, no. 5, pp. H2112–H2119, 2005.
- M. Chandra, D. E. Montgomery, J. J. Kim, and R. J. Solaro, “The N-terminal region of troponin T is essential for the maximal activation of rat cardiac myofilaments,” Journal of Molecular and Cellular Cardiology, vol. 31, no. 4, pp. 867–880, 1999.
- M. Chandra, J. J. Kim, and R. J. Solaro, “An improved method for exchanging troponin subunits in detergent skinned rat cardiac fiber bundles,” Biochemical and Biophysical Research Communications, vol. 263, no. 1, pp. 219–223, 1999.
- A. Fabiato and F. Fabiato, “Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells,” Journal de Physiologie, vol. 75, no. 5, pp. 463–505, 1979.
- R. L. Lieber, Y. Yeh, and R. J. Baskin, “Sarcomere length determination using laser diffraction. Effect of beam and fiber diameter,” Biophysical Journal, vol. 45, no. 5, pp. 1007–1016, 1984.
- P. P. de Tombe and G. J. M. Stienen, “Protein kinase A does not alter economy of force maintenance in skinned rat cardiac trabeculae,” Circulation Research, vol. 76, no. 5, pp. 734–741, 1995.
- G. J. M. Stienen, G. Zaremba, and G. Elzinga, “ATP utilization for calcium uptake and force production in skinned muscle fibres of Xenopus laevis,” Journal of Physiology, vol. 482, no. 1, pp. 109–122, 1995.
- K. B. Campbell, M. Chandra, R. D. Kirkpatrick, B. K. Slinker, and W. C. Hunter, “Interpreting cardiac muscle force-length dynamics using a novel functional model,” American Journal of Physiology, vol. 286, no. 4, pp. H1535–H1545, 2004.
- K. Campbell, “Rate constant of muscle force redevelopment reflects cooperative activation as well as cross-bridge kinetics,” Biophysical Journal, vol. 72, no. 1, pp. 254–262, 1997.
- M. V. Vinogradova, D. B. Stone, G. G. Malanina et al., “Ca2+-regulated structural changes in troponin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 14, pp. 5038–5043, 2005.