CELL SPIKE FORMATION AND m-CALPAIN ACTIVATION IN SKIN FIBROBLASTS ADHERING TO FIBRILLAR COLLAGEN I.
スポンサーリンク
概要
- 論文の詳細を見る
Collagen I is the most abundant matrix protein that forms highly ordered fibrillar structure composed of triple helical monomers. Skin fibroblasts respond to monomeric collagen I using integrins α1β1 and α2β1, and to fibrillar collagen I using integrins α1β1, α2β1, αvβ3, and discoidin domain receptor 2 (DDR2). The fibrillar collagen I induces the formation of numerous dendrite-like cell spikes via F-actin reorganization of peripheral stress fibers, but not of central stress fibers, in fibroblasts. This cell extension requires an intracellular Ca^<2+> increase. Calpains, cytoplasmic Ca^<2+> -dependent cysteine proteases, are key molecules that regulate the lamellipodium formation through activation of Rho GTPase, Rac or RhoA. μ-Calpain, a highly Ca^<2+> -sensitive form, was more activated in the cells on monomeric collagen than that on fibrillar one. However, m-calpain, a low Ca^<2+> -sensitive form was activated only in the cells on fibrillar collagen. Talin and fodrin, well-known calpain substrates, were dramatically degraded by calpain in 3-10 minutes only in the cells on fibrillar collagen, and their fragments, talin 47 kDa fragment and fodrin 140 kDa fragment, were detected by immunoblot analysis. A calpain inhibitor, Z-Leu-Leu-al, inhibited formation of both lamellipodia and cell spikes. Further, m-calpain interacted with the activated forms of focal adhesion kinase (FAK), FAK-related kinase PYK2, and DDR2. During the cell spike formation, Cdc42, Rac1, followed by RhoA, were activated, of which only Cdc42 activation was inhibited by the calpain inhibitor. These results show that calpain activity is essential for the cell spike extension and Cdc42 is a downstream molecule of calpain in skin fibroblasts on cell spike formation by fibrillar collagen.
- 日本結合組織学会の論文
著者
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Sato Kaori
Department of Pathology, The Nippon Dental University, School of Dentistry at Tokyo
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Hattori S
Nippi Research Institute Of Biomatrix And Japan Institute Of Leather Research
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Hattori Shunji
Nippi Research Institute Of Biomatrix
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INOMATA Mitsushi
Department of Protein Biochemistry, Tokyo Metropolitan Institute of Gerontology
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Irie Shinkichi
Nippi Research Institute of Biomatrix
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KAWASHIMA Seiichi
Department of Molecular Biology, Tokyo Metropolitan Institute of Medical Science
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Irie S
Nippi Research Institute Of Biomatrix
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Irie Shinkichi
Research Institute Of Biomatrix Nippi Inc.
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Kawashima S
Department Of Molecular Biology Tokyo Metropolitan Institute Of Medical Science
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Kawashima Seiichi
Department Of Molecular Biology Tokyo Metropolitan Institute Of Medical Science
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Kawashima Seiichi
Department Of Molecular Biology Tokyo Metropolitan Institute For Medical Science
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Kawashima Seiichi
Department Of Biochemistry Tokyo Metropolitan Institute Of Gerontology
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Inomata Mitsushi
Department Of Protein Chemistry Tokyo Metropolitan Institute Of Gerontology
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Inomata Mitsushi
Department Of Enzyme Biochemistry Tokyo Metropolitan Institute Of Gerontology
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Sato Kaori
Department Of Molecular Biology Tokyo Metropolitan Institute Of Medical Science
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Sato Kaori
Department Of Bacteriology Shinshu University School Of Medicine
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Hattori Shunji
Nippi Res. Inst. Of Biomatrix Jpn
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Hattori Shunji
Nippi Research Institute Of Biomatrix And Institute Of Leather Research Nippi Co. Ltd.
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Irie S
Nippi Res. Inst. Biomatrix Tokyo Jpn
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SATO Kaori
Department of Anatomy, School of Medicine, Sapporo Medical University
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