Down-Regulation of Myosin Light Chain Kinase Expression in Vascular Smooth Muscle Cells Accelerates Cell Proliferation: Requirement of Its Actin-binding Domain for Reversion to Normal Rates

Hong Hui Wang; Akio Nakamura; Shinji Yoshiyama; Ryoki Ishikawa; Na Cai; Li-Hong Ye; Hiromi Takano-Ohmuro; Kazuhiro Kohama

doi:10.1254/jphs.11213SC

Short Communication

Down-Regulation of Myosin Light Chain Kinase Expression in Vascular Smooth Muscle Cells Accelerates Cell Proliferation: Requirement of Its Actin-binding Domain for Reversion to Normal Rates

Hong Hui Wang, Akio Nakamura, Shinji Yoshiyama, Ryoki Ishikawa, Na Cai, Li-Hong Ye, Hiromi Takano-Ohmuro, Kazuhiro Kohama

Author information

Hong Hui Wang
Department of Molecular and Cellular Pharmacology, Gunma University Graduate School of Medicine, Japan
Akio Nakamura
Department of Molecular and Cellular Pharmacology, Gunma University Graduate School of Medicine, Japan
Shinji Yoshiyama
Department of Molecular and Cellular Pharmacology, Gunma University Graduate School of Medicine, Japan
Ryoki Ishikawa
Department of Molecular and Cellular Pharmacology, Gunma University Graduate School of Medicine, Japan
Na Cai
Department of Biochemistry, College of Life Sciences, Nankai University, P.R. China
Li-Hong Ye
Department of Biochemistry, College of Life Sciences, Nankai University, P.R. China
Hiromi Takano-Ohmuro
Research Institute of Pharmaceutical Sciences, Musashino University, Japan
Kazuhiro Kohama
Department of Molecular and Cellular Pharmacology, Gunma University Graduate School of Medicine, Japan
Research Institute of Pharmaceutical Sciences, Musashino University, Japan

Keywords: myosin light-chain kinase, actin-binding domain, vascular smooth muscle proliferation

JOURNAL FREE ACCESS

2012 Volume 119 Issue 1 Pages 91-96

DOI https://doi.org/10.1254/jphs.11213SC

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Abstract

Myosin light-chain kinase (MLCK) is a multi-domain protein with kinase and actin-binding domains, among others. Deficiency of MLCK expression in GBaSM-4 vascular smooth muscle cells enhanced cell proliferation rate and shortened cell doubling time. Transient transfection of the MLCK-deficient cells with cDNA constructs of either wild-type MLCK or its mutant lacking the kinase activity reverted the cell proliferation rate to that of wild-type cells, whereas that of MLCK lacking the actin-binding domain maintained cell proliferation at an elevated rate similar to the MLCK-deficient cells. Thus, the actin-binding domain of MLCK seems to play a role in regulating cell proliferation.

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