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Impact of temperature on cross‐bridge cycling kinetics in rat myocardium
Author(s) -
De Tombe Pieter P.,
Stienen G. J. M.
Publication year - 2007
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.2007.138693
Subject(s) - cycling , kinetics , bridge (graph theory) , chemistry , biophysics , temperature cycling , materials science , cardiology , medicine , thermodynamics , physics , biology , quantum mechanics , archaeology , thermal , history
The dependence of contractile properties on intracellular calcium in cardiac tissue is a highly cooperative process. Here, the temperature and calcium dependence of contractile and energetical properties in permeabilized cardiac trabeculae from rat were studied to provide novel insights into the underlying kinetic processes. Myofilament Ca 2+ sensitivity significantly increased with temperature between 15 and 25°C, whereas its steepness was independent of temperature. A direct proportionality between active tension and Ca 2+ ‐activated rate of ATP hydrolysis was observed; the slope of this relationship (tension cost) was highly temperature dependent. The rate of tension redevelopment following a quick release–restretch manoeuvre ( k tr ) depended in a complex manner on the level of contractile activation and on temperature. At saturating calcium levels, the temperature dependence ( Q 10 ) of k tr and Ca 2+ ‐activated ATP hydrolysis rate were similar ( Q 10 ∼3.5), and significantly higher than the Q 10 for maximum tension ( T max ; Q 10 ∼1.3) or tension cost ( Q 10 ∼2.5). In contrast, at a low level of contractile activation (∼5% of T max) , the Q 10 of k tr was similar to that of tension cost, and significantly lower than the Q 10 of Ca 2+ ‐activated ATP hydrolysis at that level of contractile activation. Our results are consistent with the hypothesis that at high levels of contractile activation, the rates of tension redevelopment and Ca 2+ ‐activated ATP hydrolysis are determined by both apparent cross‐bridge attachment and detachment rates, while at low levels, k tr is limited by cross‐bridge detachment rate. Tension cost, on the other hand, is determined solely by cross‐bridge detachment kinetics at all temperatures and levels of contractile activation.