Cofilin Phosphorylation Mediates Proliferation in Response to Platelet-Derived Growth Factor-BB in Rat Aortic Smooth Muscle Cells

Kyung-Jong Won; Seung Hwa Park; Taekyu Park; Chang-Kwon Lee; Hwan Myung Lee; Wahn Soo Choi; Sun-Jong Kim; Pyo-Jam Park; Hyung-Kwan Jang; Soon Heum Kim; Bokyung Kim

doi:10.1254/jphs.FP0072354

Full Papers

Cofilin Phosphorylation Mediates Proliferation in Response to Platelet-Derived Growth Factor-BB in Rat Aortic Smooth Muscle Cells

Kyung-Jong Won, Seung Hwa Park, Taekyu Park, Chang-Kwon Lee, Hwan Myung Lee, Wahn Soo Choi, Sun-Jong Kim, Pyo-Jam Park, Hyung-Kwan Jang, Soon Heum Kim, Bokyung Kim

Author information

Kyung-Jong Won
Institute of Medical Sciences, School of Medicine, Konkuk University, Korea
Seung Hwa Park
Institute of Medical Sciences, School of Medicine, Konkuk University, Korea
Taekyu Park
Division of Life Science, College of Biomedical and Health Science, Konkuk University, Korea
Chang-Kwon Lee
Institute of Medical Sciences, School of Medicine, Konkuk University, Korea
Hwan Myung Lee
Institute of Medical Sciences, School of Medicine, Konkuk University, Korea
Wahn Soo Choi
Institute of Medical Sciences, School of Medicine, Konkuk University, Korea
Sun-Jong Kim
Institute of Medical Sciences, School of Medicine, Konkuk University, Korea
Pyo-Jam Park
Division of Life Science, College of Biomedical and Health Science, Konkuk University, Korea
Hyung-Kwan Jang
Department of Microbiology, College of Veterinary Medicine, Chonbuk National University, Korea
Soon Heum Kim
Institute of Medical Sciences, School of Medicine, Konkuk University, Korea
Bokyung Kim
Institute of Medical Sciences, School of Medicine, Konkuk University, Korea

Keywords: cofilin, proliferation, rat aortic smooth muscle cell (RASMC), platelet-derived growth factor-BB (PDGF-BB), c-Jun N-terminal kinase (JNK)

JOURNAL FREE ACCESS

2008 Volume 108 Issue 3 Pages 372-379

DOI https://doi.org/10.1254/jphs.FP0072354

Details

Abstract

Cofilin, an actin-binding protein, is essential for a variety of cell responses. In this study, we investigated the correlation between proliferation and cofilin phosphorylation in response to platelet-derived growth factor (PDGF) in rat aortic smooth muscle cells (RASMCs). The phosphorylation of cofilin and activity of mitogen-activated protein kinase (MAPK) were measured by Western analyses and proliferation in RASMCs was measured by BrdU incorporation assays. The phosphorylation of cofilin in RASMCs was decreased by PDGF-BB treatment at 10 min, but recovered to the level of the quiescent state at 60 min. PDGF-BB–induced dephosphorylation of cofilin was inhibited by pretreatment with piceatannol (a spleen tyrosine kinase [Syk] inhibitor), PP2 (a Src inhibitor), or SP600125 (a c-Jun N-terminal kinase [JNK] inhibitor), but not by PD98059, an inhibitor of extracellular signal-regulated kinase 1/2. PDGF-BB increased JNK activity and proliferation, and these responses were suppressed by kinase inhibitors and small interference RNA-cofilin. The results suggest that PDGF-BB–induced dephosphorylation of cofilin can be promoted via the JNK pathway, which is regulated by both Syk and Src kinases and that cofilin dephosphorylation may be involved in PDGF-BB–induced RASMC proliferation.

Corresponding author

Register with J-STAGE for free!