- About this Journal ·
- Abstracting and Indexing ·
- Aims and Scope ·
- Annual Issues ·
- Article Processing Charges ·
- Articles in Press ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
Journal of Biomedicine and Biotechnology
Volume 2011 (2011), Article ID 310791, 8 pages
Titin-Actin Interaction: PEVK-Actin-Based Viscosity in a Large Animal
1Molecular Cardiovascular Research Program, Sarver Heart Center, Department of Physiology, University of Arizona, Tucson, AZ 85724, USA
2Department of Integrative Pathophysiology, Universitätsmedizin Mannheim, University of Heidelberg, Theodor-Kutzer-Ufer 1-3, 68167 Mannheim, Germany
Received 23 July 2011; Accepted 1 September 2011
Academic Editor: Guy Benian
Copyright © 2011 Charles S. Chung 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.
- M. Ohno, C. P. Cheng, and W. C. Little, “Mechanism of altered patterns of left ventricular filling during the development of congestive heart failure,” Circulation, vol. 89, no. 5, pp. 2241–2250, 1994.
- L. Shmuylovich and S. J. Kovács, “E-wave deceleration time may not provide an accurate determination of LV chamber stiffness if LV relaxation/viscoelasticity is unknown,” American Journal of Physiology—Heart and Circulatory Physiology, vol. 292, no. 6, pp. H2712–H2720, 2007.
- M. R. Zile and D. L. Brutsaert, “New concepts in diastolic dysfunction and diastolic heart failure: part I: diagnosis, prognosis, and measurements of diastolic function,” Circulation, vol. 105, no. 11, pp. 1387–1393, 2002.
- C. S. Chung and H. L. Granzier, “Contribution of titin and extracellular matrix to passive pressure and measurement of sarcomere length in the mouse left ventricle,” Journal of Molecular and Cellular Cardiology, vol. 50, no. 4, pp. 731–739, 2011.
- C. S. Chung and S. J. Kovács, “Physical determinants of left ventricular isovolumic pressure decline: model prediction with in vivo validation,” American Journal of Physiology—Heart and Circulatory Physiology, vol. 294, no. 4, pp. H1589–H1596, 2008.
- D. A. Kass, J. G. F. Bronzwaer, and W. J. Paulus, “What mechanisms underlie diastolic dysfunction in heart failure?” Circulation Research, vol. 94, no. 12, pp. 1533–1542, 2004.
- S. J. Kovács, B. Barzilai, and J. E. Pérez, “Evaluation of diastolic function with Doppler echocardiography: the PDF formalism,” American Journal of Physiology—Heart and Circulatory Physiology, vol. 252, no. 1, part 2, pp. H178–H187, 1987.
- K. Wang, J. McClure, and A. Tu, “Titin: major myofibrillar components of striated muscle,” Proceedings of the National Academy of Sciences of the United States of America, vol. 76, no. 8, pp. 3698–3702, 1979.
- K. Maruyama, “Connectin, an elastic protein from myofibrils,” Journal of Biochemistry, vol. 80, no. 2, pp. 405–407, 1976.
- M. M. Lewinter and H. Granzier, “Cardiac titin: a multifunctional giant,” Circulation, vol. 121, no. 19, pp. 2137–2145, 2010.
- W. A. Linke and M. Krüger, “The giant protein titin as an integrator of myocyte signaling pathways,” Physiology, vol. 25, no. 3, pp. 186–198, 2010.
- H. L. Granzier and S. Labeit, “The giant protein titin: a major player in myocardial mechanics, signaling, and disease,” Circulation Research, vol. 94, no. 3, pp. 284–295, 2004.
- R. Yamasaki, M. Berri, Y. Wu et al., “Titin-actin interaction in mouse myocardium: passive tension modulation and its regulation by calcium/S100A1,” Biophysical Journal, vol. 81, no. 4, pp. 2297–2313, 2001.
- H. P. Erickson, “Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 21, pp. 10114–20118, 1994.
- L. Tskhovrebova, J. Trinick, J. A. Sleep, and R. M. Simmons, “Elasticity and unfolding of single molecules of the giant muscle protein titin,” Nature, vol. 387, no. 6630, pp. 308–312, 1997.
- M. Rief, M. Gautel, A. Schemmel, and H. E. Gaub, “The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy,” Biophysical Journal, vol. 75, no. 6, pp. 3008–3014, 1998.
- M. Gautel, E. Lehtonen, and F. Pietruschka, “Assembly of the cardiac I-band region of titin/connectin: expression of the cardiac-specific regions and their structural relation to the elastic segments,” Journal of Muscle Research and Cell Motility, vol. 17, no. 4, pp. 449–461, 1996.
- K. Trombitás, M. Greaser, S. Labeit et al., “Titin extensibility in situ: entropic elasticity of permanently folded and permanently unfolded molecular segments,” Journal of Cell Biology, vol. 140, no. 4, pp. 853–859, 1998.
- K. Trombitás, Y. Wu, M. McNabb et al., “Molecular basis of passive stress relaxation in human soleus fibers: assessment of the role of immunoglobulin-like domain unfolding,” Biophysical Journal, vol. 85, no. 5, pp. 3142–3153, 2003.
- M. Helmes, K. Trombitás, T. Centner et al., “Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence: titin is an adjustable spring,” Circulation Research, vol. 84, no. 11, pp. 1339–1352, 1999.
- H. Granzier, M. Kellermayer, M. Helmes, and K. Trombitás, “Titin elasticity and mechanism of passive force development in rat cardiac myocytes probed by thin-filament extraction,” Biophysical Journal, vol. 73, no. 4, pp. 2043–2053, 1997.
- T. Funatsu, E. Kono, H. Higuchi et al., “Elastic filaments in situ in cardiac muscle: deep-etch replica analysis in combination with selective removal of actin and myosin filaments,” Journal of Cell Biology, vol. 120, no. 3, pp. 711–724, 1993.
- M. S. Kellermayer and H. L. Granzier, “Calcium-dependent inhibition of in vitro thin-filament motility by native titin,” FEBS Letters, vol. 380, no. 3, pp. 281–286, 1996.
- S. Kimura, K. Maruyama, and Y. P. Huang, “Interactions of muscle β-connectin with myosin, actin, and actomyosin at low ionic strengths,” Journal of Biochemistry, vol. 96, no. 2, pp. 499–506, 1984.
- A. Soteriou, M. Gamage, and J. Trinick, “A survey of interactions made by the giant protein titin,” Journal of Cell Science, vol. 104, no. 1, part 1, pp. 119–123, 1993.
- M. Kulke, S. Fujita-Becker, E. Rostkova et al., “Interaction betweeen PEVK-titin and actin filaments origin of a viscous force component in cardiac myofibrils,” Circulation Research, vol. 89, no. 10, pp. 874–881, 2001.
- W. A. Linke, M. Ivemeyer, S. Labeit, H. Hinssen, J. C. Rüegg, and M. Gautel, “Actin-titin interaction in cardiac myofibrils: probing a physiological role,” Biophysical Journal, vol. 73, no. 2, pp. 905–919, 1997.
- H. L. Granzier, M. H. Radke, J. Peng et al., “Truncation of titin's elastic PEVK region leads to cardiomyopathy with diastolic dysfunction,” Circulation Research, vol. 105, no. 6, pp. 557–564, 2009.
- C. S. Chung, M. Methawasin, O. L. Nelson et al., “Titin based viscosity in ventricular physiology: an integrative investigation of PEVK-actin interactions,” Journal of Molecular and Cellular Cardiology, vol. 51, no. 3, pp. 428–434, 2011.
- M. Greaser, “Identification of new repeating motifs in titin,” Proteins, vol. 43, no. 2, pp. 145–149, 2001.
- A. Nagy, P. Cacciafesta, L. Grama, A. Kengyel, A. Málnási-Csizmadia, and M. S. Kellermayer, “Differential actin binding along the PEVK domain of skeletal muscle titin,” Journal of Cell Science, vol. 117, part 24, pp. 5781–5789, 2004.
- C. Hidalgo, B. Hudson, J. Bogomolovas et al., “PKC phosphorylation of titin's PEVK element: a novel and conserved pathway for modulating myocardial stiffness,” Circulation Research, vol. 105, no. 7, pp. 631–638, 2009.
- P. P. de Tombe and H. E. ter Keurs, “An internal viscous element limits unloaded velocity of sarcomere shortening in rat myocardium,” Journal of Physiology, vol. 454, pp. 619–642, 1992.
- T. S. Harris, C. F. Baicu, C. H. Conrad et al., “Constitutive properties of hypertrophied myocardium: cellular contribution to changes in myocardial stiffness,” American Journal of Physiology—Heart and Circulatory Physiology, vol. 282, no. 6, pp. H2173–H2182, 2002.
- H. L. Granzier and K. Wang, “Interplay between passive tension and strong and weak binding cross-bridges in insect indirect flight muscle: a functional dissection by gelsolin-mediated thin filament removal,” Journal of General Physiology, vol. 101, no. 2, pp. 235–270, 1993.
- H. Fukushima, C. S. Chung, and H. Granzier, “Titin-isoform dependence of titin-actin interaction and its regulation by S100A1/ Ca2+ in skinned myocardium,” Journal of Biomedicine and Biotechnology, vol. 2010, Article ID 727239, 9 pages, 2010.
- W. A. Linke, M. Kulke, H. Li et al., “PEVK domain of titin: an entropic spring with actin-binding properties,” Journal of Structural Biology, vol. 137, no. 1-2, pp. 194–205, 2002.
- M. M. Lewinter, J. Popper, M. McNabb, L. Nyland, S. B. Bell, and H. Granzier, “Extensible behavior of titin in the miniswine left ventricle,” Circulation, vol. 121, no. 6, pp. 768–774, 2010.
- S. F. Nagueh, C. P. Appleton, T. C. Gillebert et al., “Recommendations for the evaluation of left ventricular diastolic function by echocardiography,” Journal of the American Society of Echocardiography, vol. 22, no. 2, pp. 107–133, 2009.
- L. Shmuylovich, C. S. Chung, and S. J. Kovács, “Point: left ventricular volume during diastasis is the physiological in vivo equilibrium volume and is related to diastolic suction,” Journal of Applied Physiology, vol. 109, no. 2, pp. 606–608, 2010.
- J. D. Stroud, C. F. Baicu, M. A. Barnes, F. G. Spinale, and M. R. Zile, “Viscoelastic properties of pressure overload hypertrophied myocardium: effect of serine protease treatment,” American Journal of Physiology—Heart and Circulatory Physiology, vol. 282, no. 6, pp. H2324–H2335, 2002.
- S. Nishimura, S. Nagai, M. Katoh et al., “Microtubules modulate the stiffness of cardiomyocytes against shear stress,” Circulation Research, vol. 98, no. 1, pp. 81–87, 2006.
- M. Vlkers, D. Rohde, C. Goodman, and P. Most, “S100A1: a regulator of striated muscle sarcoplasmic reticulum Ca2+ handling, sarcomeric, and mitochondrial function,” Journal of Biomedicine and Biotechnology, vol. 2010, Article ID 178614, 10 pages, 2010.
- B. D. Hudson, C. G. Hidalgo, M. Gotthardt, and H. L. Granzier, “Excision of titin's cardiac PEVK spring element abolishes PKCα-induced increases in myocardial stiffness,” Journal of Molecular and Cellular Cardiology, vol. 48, no. 5, pp. 972–978, 2010.
- E. Churchill, G. Budas, A. Vallentin, T. Koyanagi, and D. Mochly-Rosen, “PKC isozymes in chronic cardiac disease: possible therapeutic targets?” Annual Review of Pharmacology and Toxicology, vol. 48, pp. 569–599, 2008.
- S. S. Palaniyandi, L. Sun, J. C. Ferreira, and D. Mochly-Rosen, “Protein kinase C in heart failure: a therapeutic target?” Cardiovascular Research, vol. 82, no. 2, pp. 229–239, 2009.