期刊
BULLETIN OF EXPERIMENTAL BIOLOGY AND MEDICINE
卷 162, 期 1, 页码 42-44出版社
SPRINGER
DOI: 10.1007/s10517-016-3540-x
关键词
tropomyosin; actin-myosin interaction; calcium regulation; in vitro motility assay
资金
- Russian Foundation for Basic Research [15-04-01558, 15-34-20136, 16-04-00688, 16-34-00654, 16-0420060]
- Program of the Presidium of Ural Division of the Russian Academy of Sciences [15-9-4-18]
- Government of the Russian Federation [211, 02.A03.21.0006]
- Presidium of the Ural Division of Russian Academy of Sciences
Tropomyosin plays an important role in the regulation of actin-myosin interaction in striated muscles. Mutations in the tropomyosin gene disrupt actin-myosin interaction and lead to myopathies and cardiomyopathies. Tropomyosin with mutations in the a-chain is expressed in both the myocardium and skeletal muscles. We studied the effect of mutations in the a-chain of tropomyosin related to hypertrophic (D175N and E180G) and dilated cardiomyopathies (E40K and E54K) on calcium regulation of the actin-myosin interaction in skeletal muscles. We analyzed the calcium-dependent sliding velocity of reconstructed thin filaments containing F-actin, troponin, and tropomyosin over myosin surface in an in vitro motility assay. Mutations D175N and E180G in tropomyosin increased the sliding velocity and its calcium sensitivity, while mutation E40K reduced both these parameters. E54K mutation increased the sliding velocity of thin filaments, but did not affect its calcium sensitivity.
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