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Diphosphorylation of the myosin regulatory light chain enhances the tension acting on stress fibers in fibroblasts.

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タイトル: Diphosphorylation of the myosin regulatory light chain enhances the tension acting on stress fibers in fibroblasts.
著者: Mizutani, Takeomi 著作を一覧する
Haga, Hisashi 著作を一覧する
Koyama, Yoshikazu 著作を一覧する
Takahashi, Masayuki 著作を一覧する
Kawabata, Kazushige 著作を一覧する
発行日: 2006年12月
出版者: Wiley-Liss, Inc.
誌名: Journal of Cellular Physiology
巻: 209
号: 3
開始ページ: 726
終了ページ: 731
出版社 DOI: 10.1002/jcp.20773
抄録: Regulation of the contractile force is crucial for cell migration, cell proliferation, and maintenance of cell morphology. Phosphorylation of the myosin II regulatory light chain (MRLC) is involved in these processes. To show whether the diphosphorylation of MRLC increases the tension acting on stress fibers, changes in the stiffness of fibroblasts expressing wild-type MRLC and a mutant type, which cannot be diphosphorylated, on treatment with lysophosphatidic acid (LPA) were examined by a mechanical-scanning probe microscope (M-SPM). The LPA treatment increased cellular stiffness in the wild-type MRLC expressing cells, while it had no effect on the mutated cells. Immunostaining showed that LPA stimulation induced the diphosphorylation of MRLC. These results suggest that the diphosphorylation of MRLC enhances the tension acting on stress fibers. J. Cell. Physiol. 209: 726-731, 2006. © 2006 Wiley-Liss, Inc.
Rights: Copyright © 2006 Wiley-Liss, Inc., Journal of Cellular Physiology,209(3), Pages 726 - 731
Relation (URI): http://www.interscience.wiley.com/
資料タイプ: article (author version)
URI: http://hdl.handle.net/2115/16009
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 水谷 武臣

 

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