Modulation of cardiac function by essential myosin light chains in health and disease
作者： I. Morano
DOI: 10.1007/978-3-642-57710-9_19
关键词: Cell biology 、 Myosin 、 Actin 、 Myosin light-chain kinase 、 Chemistry 、 Contractility 、 Myosin head 、 Gene isoform 、 Hypertrophic cardiomyopathy 、 Molecular motor
摘要: Cardiac contraction is performed by the ATP-consuming cyclic interaction of “molecular motor” myosin with actin filament. The heavy chain (MHC) contains and ATP binding sites. Two different MHC genes (α β) distinct biochemical features are expressed in human atrium, but only β-MHC ventricle. Mutations coding for ventricular subunits associated hypertrophic cardiomyopathy. Motor function could be tuned essential light (MLC-1) isoforms. Expression atrial MLC-1 isoform hypertrophied ventricle increases cross-bridge cycling kinetics contractility. It suggested that acts as a MHC/actin tether. Weakening this tether increased function.
springer.com
springerlink.com参考文章(60)
D Hailstones, P Barton, P Chan-Thomas, S Sasse, C Sutherland, E Hardeman, P Gunning, Differential regulation of the atrial isoforms of the myosin light chains during striated muscle development Journal of Biological Chemistry. ,vol. 267, pp. 23295- 23300 ,(1992) , 10.1016/S0021-9258(18)50090-9
Ian P. TRAYER, Hylary R. TRAYER, Barry A. LEVINE, Evidence that the N‐terminal region of A1‐light chain of myosin interacts directly with the C‐terminal region of actin FEBS Journal. ,vol. 164, pp. 259- 266 ,(1987) , 10.1111/J.1432-1033.1987.TB11019.X
W L Fodor, B Darras, J Seharaseyon, S Falkenthal, U Francke, E F Vanin, Human Ventricular/Slow Twitch Myosin Alkali Light Chain Gene Characterization, Sequence, and Chromosomal Location Journal of Biological Chemistry. ,vol. 264, pp. 2143- 2149 ,(1989) , 10.1016/S0021-9258(18)94153-0
Sweeney Hl, Function of the N terminus of the myosin essential light chain of vertebrate striated muscle. Biophysical Journal. ,vol. 68, ,(1995)
H O Hirzel, C R Tuchschmid, J Schneider, H P Krayenbuehl, M C Schaub, Relationship between myosin isoenzyme composition, hemodynamics, and myocardial structure in various forms of human cardiac hypertrophy. Circulation Research. ,vol. 57, pp. 729- 740 ,(1985) , 10.1161/01.RES.57.5.729
T. Q. Uyeda, P. D. Abramson, J. A. Spudich, The neck region of the myosin motor domain acts as a lever arm to generate movement Proceedings of the National Academy of Sciences of the United States of America. ,vol. 93, pp. 4459- 4464 ,(1996) , 10.1073/PNAS.93.9.4459
I Morano, H Haase, Different actin affinities of human cardiac essential myosin light chain isoforms FEBS Letters. ,vol. 408, pp. 71- 74 ,(1997) , 10.1016/S0014-5793(97)00390-6
Ingo Morano, Kerstin Hädicke, Hannelore Haase, Michael Böhm, Erland Erdmann, Marcus C. Schaub, CHANGES IN ESSENTIAL MYOSIN LIGHT CHAIN ISOFORM EXPRESSION PROVIDE A MOLECULAR BASIS FOR ISOMETRIC FORCE REGULATION IN THE FAILING HUMAN HEART Journal of Molecular and Cellular Cardiology. ,vol. 29, pp. 1177- 1187 ,(1997) , 10.1006/JMCC.1996.0353
N D Epstein, G M Cohn, F Cyran, L Fananapazir, Differences in clinical expression of hypertrophic cardiomyopathy associated with two distinct mutations in the beta-myosin heavy chain gene. A 908Leu----Val mutation and a 403Arg----Gln mutation. Circulation. ,vol. 86, pp. 345- 352 ,(1992) , 10.1161/01.CIR.86.2.345
I. Rayment, H. M. Holden, J. R. Sellers, L. Fananapazir, N. D. Epstein, Structural interpretation of the mutations in the beta-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathy. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 92, pp. 3864- 3868 ,(1995) , 10.1073/PNAS.92.9.3864