2000 Fiscal Year Final Research Report Summary
Analysis of functional significance of mutant actin identified in hereditary dilated cardiomyopathy
| Project/Area Number |
11670661
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Circulatory organs internal medicine
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| Research Institution | University of Tokyo |
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Principal Investigator |
SUGIURA Seiryo University of Tokyo, Facuulty of Medicine Assistant, 医学部・附属病院, 助手 (10272551)
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| Co-Investigator(Kenkyū-buntansha) |
FUJITA Hideo University of Tokyo, Facuulty of Medicine Assistant, 医学部・附属病院, 助手
YAMASHITA Hiroshi University of Tokyo, Facuulty of Medicine Assistant, 医学部・附属病院, 助手 (50323572)
AOYAGI Teruhiko University of Tokyo, Facuulty of Medicine Assistant, 医学部・附属病院, 助手 (10251240)
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| Project Period (FY) |
1999 – 2000
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| Keywords | Actin / myosin light chain / in vitro motility assay |
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| Research Abstract |
In this study, we evaluated the functional significance of cardiac actin focussing on its interaction with myosin ligh chain. We compared the atrial and ventricular types of cardiac myosin obtained from rat heart which are known to differ only in light chain structure. Although acitn-activated ATPase activity did not differ between the two myosins atrial type myosin showed higher actin sliding velocity in vitro. Force generating ability in vitro, however, was highe for ventricular type myosin. Single molecular measurement of force suggested the distinct kinetics of actin-myosin interaction of these myosins. We concluded that the heavy chain structure of myosin determines the catalytic activity and that the light chains are modifiers of its kinetics. To further elucidate the mechanism of this modification, we studied the effect of N-terminus peptide of essentila light chain on contractile function of cardiac myocyte. N-terminu peptide enhanced the contractility supporting the hypothesis of tethering effect of this peptide. We also developed novel experimental set up for measuring the fwitch force developed by a single cardiac mnyocyle.
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Research Products
(12 results)
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[Publications] Sata M, Kakoki M, Nagata D, Nishimatsu H, Suzuki E, Aoyagi T, Sugiura S, Kojima H, Nagano T, Kangawa K, Matsuo H, Omata M, Nagai R, Hirata Y: "Adrenomedullin and nitric oxide inhibit human endothelial cell apoptosis via a cGMP-independent mechanism."Hypertension. 36. 83-88 (2000)
Description
「研究成果報告書概要(欧文)」より
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[Publications] Eto Y, Yonekura K, Sonoda M, Arai N, Sata M, Sugiura S, Takenaka K, Gualberto A, Hixon M.L., Wagner M.W., Aoyagi T: "Calcineurin is activated in rat hearts with physiological left ventricular hypertrophy induced by voluntary exercise training."Circulation. 101. 2134-2137 (2000)
Description
「研究成果報告書概要(欧文)」より
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