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Published on: September 17, 2015
Kinetic properties of cardiac myosin heavy chain isoforms in rat
Stefan Galler1, Emma Puchert, Bärbel Gohlsch
1Zoologisches Institut, Universität Salzburg, Hellbrunnerstrasse 34, 5020 Salzburg, Austria. Stefan.Galler@sbg.ac.at
Insights
Cardiac myosin heavy chain (MHC) kinetics differ significantly. Cardiac alphaMHC is 3x faster than betaMHC, with distinct properties compared to skeletal muscle MHC isoforms.
Area of Science:
- Muscle Physiology
- Molecular Biology
- Biochemistry
Background:
- Myosin heavy chain (MHC) head is crucial for force generation in muscle.
- Previous studies indicated MHC isoform-specific differences in myosin head kinetics.
- Stretch activation kinetics in skeletal muscle correlate with MHC isoform composition.
Purpose of the Study:
- To investigate and compare the kinetic properties of cardiac alpha-MHC and beta-MHC isoforms.
- To compare the stretch activation kinetics of cardiac MHC isoforms with those in rat skeletal muscle fibers.
Main Methods:
- Utilized stretch activation methodology on muscle strips from hyper- and hypothyroid rat atria and ventricles.
- Measured isometric conditions and maximal Ca2+ activation to assess kinetic properties.
- Compared kinetic parameters (time constant t3) between different muscle types and MHC isoforms.
Main Results:
- Cardiac alpha-MHC kinetics were found to be 3 times faster than cardiac beta-MHC under isometric conditions and maximal Ca2+ activation.
- 100% alpha-MHC heart muscle strips showed faster stretch activation kinetics (t3: 108+/-18 ms) than rat type-IIA skeletal muscle fibers (t3: 157+/-19 ms).
- 100% beta-MHC heart muscle strips exhibited faster kinetics (t3: 351+/-44 ms) compared to rat type-I skeletal muscle fibers (t3: 901+/-348 ms).
Conclusions:
- Cardiac alpha-MHC and beta-MHC isoforms possess distinct kinetic properties.
- The observed kinetic differences between cardiac beta-MHC and skeletal muscle type-I fibers challenge the assumed identity between beta-MHC and MHCIbeta.
Abstract:
The head portion of the myosin heavy chain (MHC) is essential in force generation. As previously shown, Ca2+-activated fibres of mammalian skeletal muscle display a strong correlation between their MHC isoform complement and the kinetics of stretch activation, suggesting isoform-specific differences in kinetic properties of myosin heads. Using the same methodology on muscle strips of atria and ventricles of hyper- and hypothyroid rats, this study showed that the kinetics of cardiac alphaMHC are 3 times faster than those of cardiac betaMHC under isometric conditions and maximal Ca2+ activation. Comparison of rat heart and skeletal muscle fibres revealed that 100% alphaMHC heart muscle strips exhibited faster stretch activation kinetics (time parameter t3: 108+/-18 ms, mean+/-SD) than rat type-IIA fibres ( t3: 157+/-19 ms), but slower than type-IID fibres ( t3: 55+/-10 ms). The kinetics of 100% betaMHC heart muscle strips ( t3: 351+/-44 ms) were faster than that of type-I fibres in rat skeletal muscle ( t3: 901+/-348 ms). This difference between the two muscle types calls in question the generally accepted identity of betaMHC and MHCIbeta.
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