Abstract:
: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.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Yuan C,Zhao X,Wang Z,Borg TK,Ye T,Khalpey ZI,Runyan RB,Shao Y,Gao BZdoi
10.1016/j.bpj.2019.12.030subject
Has Abstractpub_date
2020-03-10 00:00:00pages
1058-1066issue
5eissn
0006-3495issn
1542-0086pii
S0006-3495(19)34430-3journal_volume
118pub_type
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