Efficiency of cross-bridges and mitochondria in mouse cardiac muscle
作者： C. J. Barclay , C. Widén
DOI: 10.1007/978-1-4419-6366-6_15
关键词: Contraction (grammar) 、 Work output 、 Biophysics 、 Skeletal muscle 、 Biology 、 Cardiac muscle 、 ATP hydrolysis 、 Oxidative phosphorylation 、 Muscle contraction 、 Isometric exercise 、 Anatomy
摘要: The aim of this study was to make cellular-level measurements the mechanical efficiency mouse cardiac muscle and use these determine (1) work performed by a cross-bridge in one ATP-splitting cycle (2) fraction free energy available metabolic substrates that is transferred oxidative phosphorylation ATP (i.e. mitochondrial thermodynamic efficiency). Experiments were using isolated left ventricular papillary muscles (n = 9; studied at 27°C) myothermic technique. production heat measured during after 40 contractions contraction frequency 2 Hz. Each consisted brief isometric period followed isovelocity shortening. Work output, output enthalpy all independent shortening velocity. Maximum initial (mean ± SEM) 31.1 1.3% maximum net 16.9 1.5%. It calculated per 20 zJ, comparable values for skeletal muscle, 72%. Analysis data literature suggests from other species also likely be between 70 80%.
uq.edu.au
springer.com
core.ac.uk参考文章(32)
CJ Barclay, CL Weber, None, Slow skeletal muscles of the mouse have greater initial efficiency than fast muscles but the same net efficiency. The Journal of Physiology. ,vol. 559, pp. 519- 533 ,(2004) , 10.1113/JPHYSIOL.2004.069096
M Spindler, K W Saupe, M E Christe, H L Sweeney, C E Seidman, J G Seidman, J S Ingwall, Diastolic dysfunction and altered energetics in the alphaMHC403/+ mouse model of familial hypertrophic cardiomyopathy. Journal of Clinical Investigation. ,vol. 101, pp. 1775- 1783 ,(1998) , 10.1172/JCI1940
G. P. Dobson, J. P. Headrick, Bioenergetic scaling: metabolic design and body-size constraints in mammals Proceedings of the National Academy of Sciences of the United States of America. ,vol. 92, pp. 7317- 7321 ,(1995) , 10.1073/PNAS.92.16.7317
R.C. Woledge, P.J. Reilly, Molar enthalpy change for hydrolysis of phosphorylcreatine under conditions in muscle cells. Biophysical Journal. ,vol. 54, pp. 97- 104 ,(1988) , 10.1016/S0006-3495(88)82934-5
Geoffrey P Dobson, Uwe Himmelreich, Heart design: free ADP scales with absolute mitochondrial and myofibrillar volumes from mouse to human. Biochimica et Biophysica Acta. ,vol. 1553, pp. 261- 267 ,(2002) , 10.1016/S0005-2728(01)00247-X
H Kammermeier, Free energy change of ATP-hydrolysis: a causal factor of early hypoxic failure of the myocardium? Journal of Molecular and Cellular Cardiology. ,vol. 14, pp. 267- 277 ,(1982) , 10.1016/0022-2828(82)90205-X
C. J. Barclay, G. A. Lichtwark, N. A. Curtin, The energetic cost of activation in mouse fast-twitch muscle is the same whether measured using reduced filament overlap or N-benzyl-p-toluenesulphonamide Acta Physiologica. ,vol. 193, pp. 381- 391 ,(2008) , 10.1111/J.1748-1716.2008.01855.X
J. Rosing, E.C. Slater, The value of ΔG° for the hydrolysis of ATP☆ Biochimica et Biophysica Acta. ,vol. 267, pp. 275- 290 ,(1972) , 10.1016/0005-2728(72)90116-8
M. J. Kushmerick, T. S. Moerland, R. W. Wiseman, Mammalian skeletal muscle fibers distinguished by contents of phosphocreatine, ATP, and Pi. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 89, pp. 7521- 7525 ,(1992) , 10.1073/PNAS.89.16.7521
Kurt W. Saupe, Matthias Spindler, James C. A. Hopkins, Weiqun Shen, Joanne S. Ingwall, Kinetic, Thermodynamic, and Developmental Consequences of Deleting Creatine Kinase Isoenzymes from the Heart Journal of Biological Chemistry. ,vol. 275, pp. 19742- 19746 ,(2000) , 10.1074/JBC.M001932200