Regulation of myosin phosphorylation and myofilament Ca^<2+> sensitivity in vascular smooth muscle
スポンサーリンク
概要
- 論文の詳細を見る
The Ca^<2+>-dependent, reversible phosphorylation of the 20 kDa regulatory myosin light chain (MLC) plays a primary role in regulating the contraction of smooth muscle. However, it is well known that the Ca^<2+> signal is not the only factor which regulates such contraction, however, the alteration of the Ca^<2+> sensitivity in the contractile apparatus is also known to play an important role. The degree of MLC phosphorylation is determined by the balance of the activity between phosphorylation and dephosphorylation. Either the Ca^<2+>-independent activation of MLC phosphorylation or the inhibition of MLC dephosphorylation causes a greater MLC phosphorylation for a given level of Ca^<2+> signal and thereby potentiates the myofilament Ca^<2+> sensitivity. The smooth muscle myosin light chain phosphatase (MLCP) consisting of three subunits was first isolated and cloned in the early '90s. The intensive investigation thereafter has uncovered the biochemical basis for regulating the activity of MLCP. The regulation of the MLCP activity is now considered to play a critical role in regulating the myofilament Ca^<2+> sensitivity. There are three major mechanisms in the regulation of MLCP ; (1) the phosphorylation of a 110 kDa regulatory subunit of MLCP (2) the conformational change of the trimeric structure, and (3) the inhibition by a smooth muscle specific inhibitor protein, CPI-17. Furthermore, some kinases have been found to phosphorylate the MLC and activate the contraction of smooth muscle in a Ca^<2+>-independent manner. Numerous protein kinases have been found to be involved in the regulation of MLC phosphorylation, and rho-kinase is one of the most frequently investigated kinases. The smooth muscle physiology is now asked to integrate the current understanding of the biochemical mechanisms and to clarify which kinases and/or proteins in the contractile apparatus play a physiological role in regulating the myofilament Ca^<2+> sensitivity and how such extracellular contractile stimulation modulates these mechanisms.
著者
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Hirano Katsuya
Division of Molecular Cardiology, Research Institute of Angiocardiology, Graduate School of Medical
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Hirano Katsuya
Division Of Molecular Cardiology Graduate School Of Medical Sciences Kyushu University
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Kanaide Hideo
Division of Molecular Cardiology, Res. Inst. of Angiocardiol., Fac,of Med., Kyushu Univ.
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Hirano Mayumi
Division of Molecular Cardiology, Research Institute of Angiocardiology, Graduate School of Medical
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Hirano Katsuya
Research Institute Of Angiocardiology Faculty Of Medicine Kyushu University
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Kanaide Hideo
Division Of Molecular Cardiology Res. Inst. Of Angiocardiol. Fac Of Med. Kyushu Univ.
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Hirano Mayumi
Division Of Molecular Cardiology Research Institute Of Angiocardiology Graduate School Of Medical Sc
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Hirano Mayumi
Division Of Molecular Cardiology Graduate School Of Medical Sciences Kyushu University
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Hirano Katsunari
Division Of Molecular Cardiology Research Institute Of Angiocardiology Graduate School Of Medical Sc
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Kanaide Hideo
International University Of Health And Welfare
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Hirano Katsuya
Division Of Molecular Cardiology Research Institute Of Angiocardiology Graduate School Of Medical Sc
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Kanaide Hideo
Research Institute Of Angiocardiology And Cardiovascular Clinic Faculty Of Medicine Kyushu Universit
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