TY - JOUR
T1 - α-Actinin-2, a cytoskeletal protein, binds to angiogenin
AU - Hu, Huajun
AU - Gao, Xiangwei
AU - Sun, Yishan
AU - Zhou, Jiliang
AU - Yang, Min
AU - Xu, Zhengping
N1 - Funding Information:
This work was supported by the National Natural Science Foundation of China (Grant No. 30171035) and the Scientific Research Foundation for the Returned Overseas Chinese Scholars, Ministry of Education, China.
PY - 2005/4/8
Y1 - 2005/4/8
N2 - Angiogenin is an angiogenic factor which is involved in tumorigenesis. However, no particular intracellular protein is known to interact directly with angiogenin. In the present study, we reported the identification of α-actinin-2, an actin-crosslinking protein, as a potential angiogenin-interacting partner by yeast two-hybrid screening. This interaction was confirmed by different approaches. First, angiogenin was pulled down together with His-tagged α-actinin-2 by Ni2+-agarose resins. Second, α-actinin-2 was coimmunoprecipitated with angiogenin by anti-angiogenin monoclonal antibody. Third, the in vivo interaction of these two proteins was revealed by fluorescence resonance energy transfer analysis. Since members of α-actinin family play pivotal roles in cell proliferation, migration, and invasion, the interaction between α-actinin-2 and angiogenin may underline one possible mechanism of angiogenin in angiogenesis. Our finding presents the first evidence of an interaction of a cytosolic protein with angiogenin, which might be a novel interference target for anti-angiogenesis and anti-tumor therapy.
AB - Angiogenin is an angiogenic factor which is involved in tumorigenesis. However, no particular intracellular protein is known to interact directly with angiogenin. In the present study, we reported the identification of α-actinin-2, an actin-crosslinking protein, as a potential angiogenin-interacting partner by yeast two-hybrid screening. This interaction was confirmed by different approaches. First, angiogenin was pulled down together with His-tagged α-actinin-2 by Ni2+-agarose resins. Second, α-actinin-2 was coimmunoprecipitated with angiogenin by anti-angiogenin monoclonal antibody. Third, the in vivo interaction of these two proteins was revealed by fluorescence resonance energy transfer analysis. Since members of α-actinin family play pivotal roles in cell proliferation, migration, and invasion, the interaction between α-actinin-2 and angiogenin may underline one possible mechanism of angiogenin in angiogenesis. Our finding presents the first evidence of an interaction of a cytosolic protein with angiogenin, which might be a novel interference target for anti-angiogenesis and anti-tumor therapy.
KW - Angiogenesis
KW - Angiogenin
KW - Protein interaction
KW - α-Actinin-2
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U2 - 10.1016/j.bbrc.2005.01.158
DO - 10.1016/j.bbrc.2005.01.158
M3 - Article
C2 - 15737636
AN - SCOPUS:14644391548
SN - 0006-291X
VL - 329
SP - 661
EP - 667
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -