Open AccessInterference of E2‐2‐mediated effect in endothelial cells by FAM96B through its limited expression of E2‐2
Author(s) -
Yang Weiwen,
Itoh Fumiko,
Ohya Hirotoshi,
Kishimoto Fukiko,
Tanaka Aya,
Nakano Naoko,
Itoh Susumu,
Kato Mitsuyasu
Publication year - 2011
Publication title -
cancer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 141
eISSN - 1349-7006
pISSN - 1347-9032
DOI - 10.1111/j.1349-7006.2011.02022.x
Subject(s) - ectopic expression , regulator , endogeny , microbiology and biotechnology , biology , chemistry , endocrinology , cell culture , biochemistry , genetics , gene
The basic helix–loop–helix protein E2‐2 is known to play a role in quiescence of endothelial cells (ECs). However, it is unclear how the activity of E2‐2 is controlled in the cells. In this study, we identified FAM96B as an interaction partner of E2‐2. FAM96B interfered with E2‐2‐mediated effects on luciferase reporter activities. Furthermore, the suppression of vascular endothelial growth factor receptor 2 promoter activity by E2‐2 was rescued by the expression of FAM96B in a dose‐dependent manner. Interestingly, FAM96B decreased the expression of ectopic and endogenous E2‐2 proteins. Mutational analysis revealed that the middle region of FAM96B is required for the limited expression of E2‐2 protein. When FAM96B was expressed in ECs, the EC migration, proliferation, and tube formation were potentiated. Taken together, these findings suggest that FAM96B acts as a regulator of E2‐2 through the control of its protein expression. ( Cancer Sci 2011; 102: 1808–1814)