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The ATP hydrolysis and phosphate release steps control the time course of force development in rabbit skeletal muscle
Author(s) -
Sleep John,
Irving Malcolm,
Burton Kevin
Publication year - 2005
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2004.078873
Subject(s) - sarcomere , chemistry , isometric exercise , biophysics , atp hydrolysis , apyrase , exponential decay , biochemistry , enzyme , myocyte , physics , biology , physiology , atpase , endocrinology , nuclear physics
The time course of isometric force development following photolytic release of ATP in the presence of Ca 2+ was characterized in single skinned fibres from rabbit psoas muscle. Pre‐photolysis force was minimized using apyrase to remove contaminating ATP and ADP. After the initial force rise induced by ATP release, a rapid shortening ramp terminated by a step stretch to the original length was imposed, and the time course of the subsequent force redevelopment was again characterized. Force development after ATP release was accurately described by a lag phase followed by one or two exponential components. At 20°C, the lag was 5.6 ± 0.4 ms ( s.e.m. , n = 11), and the force rise was well fitted by a single exponential with rate constant 71 ± 4 s −1 . Force redevelopment after shortening–restretch began from about half the plateau force level, and its single‐exponential rate constant was 68 ± 3 s −1 , very similar to that following ATP release. When fibres were activated by the addition of Ca 2+ in ATP‐containing solution, force developed more slowly, and the rate constant for force redevelopment following shortening–restretch reached a maximum value of 38 ± 4 s −1 ( n = 6) after about 6 s of activation. This lower value may be associated with progressive sarcomere disorder at elevated temperature. Force development following ATP release was much slower at 5°C than at 20°C. The rate constant of a single‐exponential fit to the force rise was 4.3 ± 0.4 s −1 ( n = 22), and this was again similar to that after shortening–restretch in the same activation at this temperature, 3.8 ± 0.2 s −1 . We conclude that force development after ATP release and shortening–restretch are controlled by the same steps in the actin–myosin ATPase cycle. The present results and much previous work on mechanical–chemical coupling in muscle can be explained by a kinetic scheme in which force is generated by a rapid conformational change bracketed by two biochemical steps with similar rate constants – ATP hydrolysis and the release of inorganic phosphate – both of which combine to control the rate of force development.