| Project/Area Number |
13307005
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
General pharmacology
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| Research Institution | Gunma University |
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Principal Investigator |
KOHAMA Kazuhiro Gunma University, Medicine, Professor, 医学部, 教授 (30101116)
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| Co-Investigator(Kenkyū-buntansha) |
KUMAGAI Hiroyuki Gunma University, Medicine, Assistant, 医学部, 助手 (20321945)
NAKAMURA Akio Gunma University, Medicine, Assistant, 医学部, 助手 (30282388)
ISHIKAWA Ryoki Gunma University, Medicine, Lecturer, 医学部, 講師 (20212863)
宮崎 淳一 筑波大学, 生物科学系, 講師 (80229830)
大石 一彦 明治薬科大学, 薬学部, 講師 (80203701)
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| Project Period (FY) |
2001 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥50,180,000 (Direct Cost: ¥38,600,000、Indirect Cost: ¥11,580,000)
Fiscal Year 2003: ¥11,700,000 (Direct Cost: ¥9,000,000、Indirect Cost: ¥2,700,000)
Fiscal Year 2002: ¥11,310,000 (Direct Cost: ¥8,700,000、Indirect Cost: ¥2,610,000)
Fiscal Year 2001: ¥27,170,000 (Direct Cost: ¥20,900,000、Indirect Cost: ¥6,270,000)
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| Keywords | Smooth muscle / regulation / myosin / myosin light chain kinase / down-regulation |
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| Research Abstract |
Myosin light chain kinase (MLCK) is a regulatory protein for smooth muscle contraction, which acts by phosphorylating 20-kDa myosin light chain (MLC20) to activate the myosin ATPase activity. Although this mode of action is well-established, there are numerous reports of smooth muscle contraction that is not associated with MLC20 phosphorylation. The kinase activity for the phosphorylation is localized at the central part of MLCK, which is also furnished with actin-binding activity at its N terminal and myosin-binding activity at its C terminal. The present study shows how such multifunctional properties of MLCK modify the actin-myosin interaction and presents our observations that the phosphorylation is not obligatory in induction of smooth muscle contraction.
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