Key result
Myosin isolated from cloned mouse fibroblasts demonstrated structural and functional similarities to muscle myosin, including actin binding, ATPase activity, and bipolar aggregate formation.
This basic science study demonstrates that myosin isolated from non-muscle cells (mouse fibroblasts) shares key structural and functional properties with muscle myosin.
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No immediate clinical implications for cardiac care; extends myosin biology to fibroblasts but leaves in vivo roles open.
Myosin has been isolated from cloned mouse fibroblasts, line L-929. Fibroblast myosin: (i) binds to rabbit muscle actin and is dissociated from it by ATP, (ii) has an ATPase activity that is suppressed by Mg(2+) in 0.6 M KCl and is activated by rabbit muscle actin in the presence of Mg(2+) in 14 mM KCl, (iii) forms thin bipolar aggregates in 0.1 M KCl when viewed in the electron microscope, (iv) possesses a heavy chain with the same mobility as muscle myosin (molecular weight 200,000) in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. In these respects, fibroblast myosin appears to be similar to muscle myosin in structure and function.
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Adelstein et al. (1972) studied this question. Myosin isolation and characterization vs. Rabbit skeletal muscle myosin was evaluated on Biochemical and structural characterization of fibroblast myosin. Myosin isolated from cloned mouse fibroblasts demonstrated structural and functional similarities to muscle myosin, including actin binding, ATPase activity, and bipolar aggregate formation.
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