The C-terminal extremity of smooth muscle myosin heavy chains influences the assembly of myosin molecules into filaments, which may impact smooth muscle contractility.
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May impact smooth muscle contractility via filament assembly; hypothesis-generating in animal models and requires human validation.
The two light meromyosin isoforms from rabbit smooth muscle were prepared as recombinant proteins in Escherichia coli. These species which differed only by their C-terminal extremity showed the same circular dichroism spectra and endotherms in measurements of differential scanning calorimetry. Their solubility properties were different at pH 7.0 in the absence of monovalent salts. Their paracrystals formed at low pH differed by their aspect and number. These data suggest a role for the C-terminal extremity of myosin heavy chains in the assembly of myosin molecules in filaments and consequently in the contractility of smooth muscles.
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Quevillon‐Chéruel et al. (1999) studied this question.
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