A Fibronectin-Derived Anti-Adhesive Peptide Suppresses the Integrin α_4β_1-Mediated Cell Adhesion
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概要
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We previously reported that fibronectin(FN)has an anti-adhesive site(YTIYVIAL)within the carboxyl-terminal heparin-binding domain and that a FN peptide containing this sequence, termed III14-2, suppresses the integrin α_5β_1-mediated cell adhesion to FN substrate. In this study, we investigated the effects of III14-2 on cell adhesion mediated by α_4β_1. U937 cells adhered in the presence of Mn^<2+> on the culture plate coated with both anti-α_4 mAb and CS-1 peptide, respectively. III14-2 suppressed the U937 cell adhesions on either substrate in a dose-dependent manner. III14-2 also suppressed the Mn^<2+>-activated cell adhesion of Ramos cells which are known to express dominantly α_4β_1 as a β_1 integrin, indicating that III14-2 shows anti-adhesive effect on the Mn^<2+>-activated cell adhesion mediated by integrin α_4β_1. Affinity labeling of cell surface proteins with biotinylated III14-2 showed the presence of specific binding proteins, with Mr. 55-and 40-kDa, for III14-2. Anti-adhesive site of FN molecule seems to be capable of inactivating the active form of integrin α_4β_1 through an "inside-out" signaling mediated by a putative cell surface receptor.
- 日本結合組織学会の論文
- 1999-03-25
著者
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Fukai Fumio
Department Of Patho-physiology Faculty Of Pharmaceutical Sciences Science University Of Tokyo
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Fukai Fumio
Department Of Patho-physilogy Faculty Of Pharmaceutical Sciences Tokyo University Of Science
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Kamiya Sadahiro
Department Of Analytical Chemistry Faculty Of Pharmaceutical Sciences Science University Of Tokyo
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Ohwaki Toshiyuki
Department Of Patho-physiology Faculty Of Pharmaceutical Sciences Science University Of Tokyo
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Katayama Takashi
Department Of Patho-physiology Faculty Of Pharmaceutical Sciences Science University Of Tokyo
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Fukai Fumio
Department Of Molecular Patho-physiology Faculty Of Pharmaceutical Science
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Katayama Takashi
Department of Chemical Engineering, Faculty of Engineering Science, Osaka University
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