Identification and characterization of follistatin as a novel angiogenin-binding protein

被引：39

作者：

Gao, Xiangwei ^{[1
,2
]}

Hu, Huajun

Zhu, Junqiao ^{[1
,2
]}

Xu, Zhengping ^{[1
,2
]}

机构：

[1] Zhejiang Univ, Sch Med, Bioelectromagnet Lab, Hangzhou 310058, Peoples R China

[2] Zhejiang Univ, Sch Med, Res Ctr Environm Genom, Hangzhou 310058, Peoples R China

来源：

FEBS LETTERS | 2007年 / 581卷 / 28期

基金：

中国国家自然科学基金;

关键词：

angiogenin; tumorigenesis; follistatin; protein interaction;

D O I：

10.1016/j.febslet.2007.10.059

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

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. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

收藏

页码：5505 / 5510

页数：6

相关论文

共 23 条

[1]

Follistatins neutralize activin bioactivity by inhibition of activin binding to its type II receptors [J].

deWinter, JP ;

tenDijke, P ;

deVries, CJM ;

vanAchterberg, TAE ;

Sugino, H ;

deWaele, P ;

Huylebroeck, D ;

Verschueren, K ;

vandenEijndenvanRaaij, AJM .

MOLECULAR AND CELLULAR ENDOCRINOLOGY, 1996, 116 (01) :105-114

[2]

STRUCTURAL CHARACTERIZATION OF FOLLISTATIN - A NOVEL FOLLICLE-STIMULATING-HORMONE RELEASE-INHIBITING POLYPEPTIDE FROM THE GONAD [J].

ESCH, FS ;

SHIMASAKI, S ;

MERCADO, M ;

COOKSEY, K ;

LING, N ;

YING, S ;

UENO, N ;

GUILLEMIN, R .

MOLECULAR ENDOCRINOLOGY, 1987, 1 (11) :849-855

[3]

ISOLATION AND CHARACTERIZATION OF ANGIOGENIN, AN ANGIOGENIC PROTEIN FROM HUMAN CARCINOMA-CELLS [J].

FETT, JW ;

STRYDOM, DJ ;

LOBB, RR ;

ALDERMAN, EM ;

BETHUNE, JL ;

RIORDAN, JF ;

VALLEE, BL .

BIOCHEMISTRY, 1985, 24 (20) :5480-5486

[4]

Subnuclear organelles: new insights into form and function [J].

Handwerger, KE ;

Gall, JG .

TRENDS IN CELL BIOLOGY, 2006, 16 (01) :19-26

[5]

Structural basis for the inhibition of activin signalling by follistatin [J].

Harrington, AE ;

Morris-Triggs, SA ;

Ruotolo, BT ;

Robinson, CV ;

Ohnuma, S ;

Hyvönen, M .

EMBO JOURNAL, 2006, 25 (05) :1035-1045

[6]

A novel role of follistatin, an activin-binding protein, in the inhibition of activin action in rat pituitary cells - Endocytotic degradation of actin and its acceleration by follistatin associated with cell-surface heparan sulfate [J].

Hashimoto, O ;

Nakamura, T ;

Shoji, H ;

Shimasaki, S ;

Hayashi, Y ;

Sugino, H .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (21) :13835-13842

[7]

Expression of receptors for human angiogenin in vascular smooth muscle cells [J].

Hatzi, E ;

Badet, J .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1999, 260 (03) :825-832

[8]

FOLLISTATIN, AN ANTAGONIST OF ACTIVIN, IS EXPRESSED IN THE SPEMANN ORGANIZER AND DISPLAYS DIRECT NEURALIZING ACTIVITY [J].

HEMMATIBRIVANLOU, A ;

KELLY, OG ;

MELTON, DA .

CELL, 1994, 77 (02) :283-295

[9]

α-actinin-2, a cytoskeletal protein, binds to angiogenin [J].

Hu, HJ ;

Gao, XW ;

Sun, YS ;

Zhou, JL ;

Yang, M ;

Xu, ZP .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2005, 329 (02) :661-667

[10]

Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo [J].

Iemura, S ;

Yamamoto, TS ;

Takagi, C ;

Uchiyama, H ;

Natsume, T ;

Shimasaki, S ;

Sugino, H ;

Ueno, N .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (16) :9337-9342