Nishioka Tomoko, Sakumi Kunihiko, Miura Tomofumi, Tahara Kazuki, Horie Hidenori, Kadoya Toshihiko, Nakabeppu Yusaku
Division of Neurofunctional Genomics, Medical Institute of Bioregulation, Kyushu University, and CREST, Japan Science and Technology Corporation, Maidashi, Higashi-ku, Fukuoka 812-8582.
J Biochem. 2002 May;131(5):653-61. doi: 10.1093/oxfordjournals.jbchem.a003148.
In this study, we established rat 3Y1 embryo cell lines expressing FosB and DeltaFosB as fusion proteins (ER-FosB, ER-DeltaFosB) with the ligand-binding domain of human estrogen receptor (ER). The binding of estrogen to the fusion proteins resulted in their nuclear translocation. After estrogen administration, exponentially growing cells expressing ER-DeltaFosB, and to a lesser extent ER-FosB, underwent morphological alteration from the flat fibroblastic shape to an extended bipolar shape, and ceased proliferating. Such morphological alteration was also induced in quiescent cells expressing ER-DeltaFosB and ER-FosB after one round of cell division triggered by estrogen administration. The cells expressing ER-DeltaFosB changed shape frequently, and the content of F-actin in the cytoplasm detected by binding of Alexa 488-phalloidin significantly decreased after the morphological alteration. By two-dimensional gel electrophoresis analysis of cellular proteins from the cells expressing ER-DeltaFosB, we identified several proteins whose expression either increased or decreased after estrogen administration. Two of these proteins were identified from their amino acid sequences as novel processed form of galectin-1.