caa a22 4500 397557523 CHVBK 20180308164807.0 cr unu---uuuuu 161202e199604 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021285 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021285 A 31-kDa Recombinant Fibronectin Cell-Binding Domain Fragment: Its Binding to Receptor, Cell Adhesive Activity, and Fusion Proteins [Elektronische Daten] [Kimikazu Hashino, Yasuko Uemori, Fusao Kimizuka, Ikunoshin Kato, Koiti Titanif] The binding of fibronectin to fibronectin receptor was studied using a recombinant 31-kDa cell-binding domain fragment of fibronectin (C279), which consisted of three type HI repeats (Ill8-III9-III10). Fibronectin receptor in several cell lysates was bound to a column of C279- immobilized Sepharose HP and obtained in a highly purified form by elution with a synthetic peptide, GRGDSP. α5β1-Integrin was detected in the GRGDSP-eluted fraction by immunoblotting. The cell-adhesive activity of C279 was inhibited by GRGDSP peptide, an anti-integrin β1, subunit antibody, and an anti-integrin α5, subunit antibody. The cell adhesion of fusion proteins of the 31-kDa fragment with biologically interesting polypep-tides (heparin-binding domain of fibronectin, and basic fibroblast growth factor) was also studied. In the presence of an anti-integrin α5 subunit antibody, human fibrosarcoma HT-1080 cells attached to the fusion protein containing fibroblast growth factor, giving rise to changes the morphology of the attached cells. The cell adhesion of C279 was inhibited by GRGDSP peptide but that of the fusion protein with the heparin-binding domain of fibronectin was not completely inhibited by the peptide. These results suggest that these biologically interesting polypeptides contribute to the cell adhesion of the fusion proteins. © by the Journal of Biochemistry Regular Papers nationallicence cell adhesion nationallicence fibroblast growth factor nationallicence fibronectin nationallicence fibronectin receptor nationallicence integrin nationallicence Hashino Kimikazu Biotechnology Research Laboratories, Takara Shuzo Co., Ltd. 3-4-1 Seta, Otsu, Shiga 520-21 aut Uemori Yasuko Biotechnology Research Laboratories, Takara Shuzo Co., Ltd. 3-4-1 Seta, Otsu, Shiga 520-21 aut Kimizuka Fusao Biotechnology Research Laboratories, Takara Shuzo Co., Ltd. 3-4-1 Seta, Otsu, Shiga 520-21 aut Kato Ikunoshin Biotechnology Research Laboratories, Takara Shuzo Co., Ltd. 3-4-1 Seta, Otsu, Shiga 520-21 aut Titanif Koiti Institute for Comprehensive Medical Science, Fujita Health University Toyoake, Aichi 470-11 aut The Journal of Biochemistry Oxford University Press 119/4(1996-04), 604-609 0021-924X 119:4<604 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021285 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021285 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Hashino Kimikazu Biotechnology Research Laboratories, Takara Shuzo Co., Ltd. 3-4-1 Seta, Otsu, Shiga 520-21 aut NATIONALLICENCE 700 1- Uemori Yasuko Biotechnology Research Laboratories, Takara Shuzo Co., Ltd. 3-4-1 Seta, Otsu, Shiga 520-21 aut NATIONALLICENCE 700 1- Kimizuka Fusao Biotechnology Research Laboratories, Takara Shuzo Co., Ltd. 3-4-1 Seta, Otsu, Shiga 520-21 aut NATIONALLICENCE 700 1- Kato Ikunoshin Biotechnology Research Laboratories, Takara Shuzo Co., Ltd. 3-4-1 Seta, Otsu, Shiga 520-21 aut NATIONALLICENCE 700 1- Titanif Koiti Institute for Comprehensive Medical Science, Fujita Health University Toyoake, Aichi 470-11 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/4(1996-04), 604-609 0021-924X 119:4<604 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford