caa a22 4500 397557736 CHVBK 20180308164807.0 cr unu---uuuuu 161202e199605 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021325 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021325 Structural and Functional Characterization of a Novel Tumor-Derived Rat Galectin-1 Having Transforming Growth Factor (TGF) Activity: The Relationship between Intramolecular Disulfide Bridges and TGF Activity [Elektronische Daten] [Kazuko Yamaoka, Arnd Ingendoh, Satoshi Tsubuki, Yoshitaka Nagai, Yutaka Sanai] Previously we demonstrated that overexpression of a β-galactoside binding protein, galectin-1, caused the transformation of BALB3T3 fibroblast cells [Yamaoka, K., Ohno, S., Kawasaki, H., and Suzuki, K. (1991) Biochem. Biophys. Res;. Commun. 179, 272-279]. We have now studied the structure-function relationships between the sugar-binding activity and the mitogenic activity of galectin-1 purified from an avian sarcoma virus-transformed rat NKK cell line, 77N1. The purified galectin-1 (t-galectin-1) had potent mitogenic activity in BALB3T3 cells, but no sugar-binding activity. Treatment of t-galectin-1 with 2-mercap-toethanol decreased its mitogenic activity, but resulted in the appearance of a sugar binding activity. Chemical modification of sulfhydryl groups in purified t-galectin-1 with [14C]-iodoacetamide suggested the presence of intramolecular disulfide bonds. MALDI-TOF mass spectrometric analysis of the native and reduced forms of the tryptic peptides from t-galectin-1 showed that t-galectin-1 has two intramolecular disulfide bonds (Cys2-Cysl6 and'Cys42-Cys60). These studies suggest that these intramolecular disulfide bonds of t-galectin-1 are essential for its mitogenic activity and that the different activities may be regulated by structural changes caused by intramolecular disulfide bond-breakage. © by the Journal of Biochemistry Regular Papers nationallicence BALB3T3 nationallicence disulfide bond nationallicence galectin nationallicence MALDI-TOF nationallicence transforming growth factor nationallicence Yamaoka Kazuko Department of Biochemical Cell Research and Department of Molecular Biology, The Tokyo Metropolitan Institute of Medical Science Honkomagome, Bunkyo-ku, Tokyo 113 aut Ingendoh Arnd Finnigan MAT Inc Hatsudai, Shibuya-ku, Tokyo 151. aut Tsubuki Satoshi Finnigan MAT Inc Hatsudai, Shibuya-ku, Tokyo 151. aut Nagai Yoshitaka Mitsubishi Kasei Institute of Life Sciences 11 Minamiooya, Machida, Tokyo 194 aut Sanai Yutaka Department of Biochemical Cell Research and Department of Molecular Biology, The Tokyo Metropolitan Institute of Medical Science Honkomagome, Bunkyo-ku, Tokyo 113 aut The Journal of Biochemistry Oxford University Press 119/5(1996-05), 878-886 0021-924X 119:5<878 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021325 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021325 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Yamaoka Kazuko Department of Biochemical Cell Research and Department of Molecular Biology, The Tokyo Metropolitan Institute of Medical Science Honkomagome, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Ingendoh Arnd Finnigan MAT Inc Hatsudai, Shibuya-ku, Tokyo 151 aut NATIONALLICENCE 700 1- Tsubuki Satoshi Finnigan MAT Inc Hatsudai, Shibuya-ku, Tokyo 151 aut NATIONALLICENCE 700 1- Nagai Yoshitaka Mitsubishi Kasei Institute of Life Sciences 11 Minamiooya, Machida, Tokyo 194 aut NATIONALLICENCE 700 1- Sanai Yutaka Department of Biochemical Cell Research and Department of Molecular Biology, The Tokyo Metropolitan Institute of Medical Science Honkomagome, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/5(1996-05), 878-886 0021-924X 119:5<878 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