Abstract:
:X-ray diffraction and tension measurement experiments were conducted on rat left ventricular skinned fibers with or without "troponin-T treatment," which exchanges the endogenous troponin T/I/C complex with exogenous troponin-T. These experiments were performed to observe the structural changes in troponin-T within a fiber elicited by contractile crossbridge formation and investigate the abnormality of hypertrophic cardiomyopathy-related troponin-T mutants. The intensity of the troponin reflection at 1/38.5 nm-1 was decreased significantly by ATP addition after treatment with wild-type or mutant troponin-T, indicating that crossbridge formation affected the conformation of troponin-T. In experiments on cardiac fibers treated with the hypertrophic cardiomyopathy-related mutants E244D- and K247R-troponin-T, treatment with K247R-troponin-T did not recruit contracting actomyosin to a greater extent than wild-type-troponin-T, although a similar drop in the intensity of the troponin reflection occurred. Therefore, the conformational change in K247R-troponin-T was suggested to be unable to fully recruit actomyosin interaction, which may be the cause of cardiomyopathy.
journal_name
Int J Mol Scijournal_title
International journal of molecular sciencesauthors
Yamaguchi M,Kimura M,Ohno T,Nakahara N,Akiyama N,Takemori S,Yagi Ndoi
10.3390/ijms21103520subject
Has Abstractpub_date
2020-05-15 00:00:00issue
10issn
1422-0067pii
ijms21103520journal_volume
21pub_type
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