Identification and characterization of follistatin as a novel angiogenin-binding protein.
Angiogenin enhances tumorigenesis. However, the mechanisms of angiogenin-induced angiogenesis and cancer cell proliferation remain elusive. In this study, follistatin was identified as a binding partner of angiogenin by a yeast two-hybrid screen and confirmed by a pull-down experiment. The interaction of fluorescently tagged angiogenin and follistatin was monitored in real time by a laser confocal microscope and shown to localize at the sub-nuclear region of HeLa cells. Additional yeast two-hybrid analysis revealed that domains 2 and 3 of follistatin were the minimal structure requirement for angiogenin binding. These findings provide new clues for further studies on the mechanisms of angiogenin-induced angiogenesis or cancer cell growth.
Gao
Xiangwei
X
Research Center for Environmental Genomics, Zhejiang University School of Medicine, 388 Yuhangtang Road, Hangzhou 310058, China.
Hu
Huajun
H
Zhu
Junqiao
J
Xu
Zhengping
Z
D002467:Cell Nucleus / Q000378:metabolism; D031541:Fluorescence Resonance Energy Transfer; D038681:Follistatin / Q000235:genetics / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D011485:Protein Binding; D012259:Ribonuclease, Pancreatic / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D020798:Two-Hybrid System Techniques
D038681:Follistatin; C046366:angiogenin; D012259:Ribonuclease, Pancreatic