Effects of Protein Kinase A on the Phosphorylation Status and Transverse Stiffness of Cardiac Myofibrils
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概要
- 論文の詳細を見る
Stimulation of β-adrenergic receptors in cardiac myocytes activates cyclic AMP–dependent protein kinase A (PKA). PKA-mediated phosphorylation of myofibrils decreases their longitudinal stiffness, but its effect on transverse stiffness is not fully understood. We thus examined the effects of PKA treatment on the transverse stiffness of cardiac myofibrils by atomic force microscopy and determined the phosphorylation levels of myofibril components by SDS-PAGE. Transverse stiffness was significantly decreased by PKA treatment concomitantly with increased phosphorylation of troponin I, myosin-binding protein C, and titin (also called connectin). Subsequent treatment with protein phosphatase 1 abrogated these PKA-mediated effects. [Supplementary methods: available only at http://dx.doi.org/10.1254/jphs.13110SC]
- 公益社団法人 日本薬理学会の論文
著者
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Saeki Yasutake
Department Of Physialogy Tsurumi Univ. School Of Dental Medicine
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Ohnuki Yoshiki
Department Of Physiology Tsurumi University School Of Dental Medicine
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Umeki Daisuke
Department Of Orthodontics Tsurumi University School Of Dental Medicine
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Shiozawa Kouichi
Department Of Physiology Tsurumi University School Of Dental Medicine
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Yamada Takenori
Department Of Biology Faculty Of Science Kyushu University
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Fujita Takayuki
Cardiovascular Research Institute Yokohama City University Graduate School Of Medicine
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Okumura Satoshi
Department Of Cardilogy Nippon Medical School
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MOTOTANI Yasumasa
Department of Physiology, Tsurumi University School of Dental Medicine
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Okumura Satoshi
Department of Physiology, Tsurumi University School of Dental Medicine, Japan
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Saeki Yasutake
Department of Cardiovascular Medicine, Graduate School of Medicine, University of Tokyo
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