Degradation of Fodrin by m-Calpain in Fibroblasts Adhering to Fibrillar Collagen I Gel
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概要
- 論文の詳細を見る
When skin fibroblasts were cultured on fibrillar collagen I gel, we observed rapid degradation of talin, fodrin and ezrin, which are well-known calpain substrates. The protease m-calpain was activated only in cells adhering to fibrillar collagen, whereas tscalpain was activated in cells adhering to monomeric or fibrillar collagen at the same level. The calpain inhibitor Z-Leu-Leu-aldehyde inhibited degradation of fodrin, but not talin. Degradation of fodrin, a-actinin and ezrin was prevented by over-expression of dominant negative m-calpain. However, over-expression of calpastatin, an endogenous calpain inhibitor, had no effect the degradation of these three proteins. These results suggest that m-calpain is responsible for degradation of their membrane proteins via adhesion to fibrillar collagen I gel.
- 社団法人 日本生化学会の論文
著者
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Irie Shinkichi
Nippi Research Institute of Biomatrix
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Kawashima Seiichi
Department Of Biochemistry Tokyo Metropolitan Institute Of Gerontology
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Inomata Mitsushi
Department Of Enzyme Biochemistry Tokyo Metropolitan Institute Of Gerontology
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Hattori Shunji
Nippi Res. Inst. Of Biomatrix Jpn
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SORIMACHI Hiroyuki
Department of Advanced Science for Biomolecules, Tokyo Metropolitan Institute of Medical Science
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SATO Kaori
Department of Anatomy, School of Medicine, Sapporo Medical University
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Irie Shinkichi
Nippi Research Institute of Biomatrix and Institute of Leather Research, Nippi Co., Ltd.
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