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Detection of the transition between the two myosin isoforms α- and β-myosin in living cardiomyocytes is essential for understanding cardiac physiology and pathology. In this study, the differences in symmetry of polarization spectra obtained from α- and β-myosin in various mammalian ventricles and propylthiouracil-treated rats are explored through polarization-dependent second harmonic generation microscopy. Here, we report for the, to our knowledge, first time that α- and β-myosin, as protein crystals, possess different symmetries: the former has C6 symmetry, and the latter has C3v. A single-sarcomere line scan further demonstrated that the differences in polarization-spectrum symmetry between α- and β-myosin came from their head regions: the head and neck domains of α- and β-myosin account for the differences in symmetry. In addition, the dynamic transition of the polarization spectrum from C6 to C3v line profile was observed in a cell culture in which norepinephrine induced an α- to β-myosin transition. Copyright © 2019. Published by Elsevier Inc.

Citation

Cai Yuan, Xiaolei Zhao, Zhonghai Wang, Thomas K Borg, Tong Ye, Zain I Khalpey, Raymond B Runyan, Yonghong Shao, Bruce Z Gao. Study of the Expression Transition of Cardiac Myosin Using Polarization-Dependent SHG Microscopy. Biophysical journal. 2020 Mar 10;118(5):1058-1066

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PMID: 31995740

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