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Blood, 1 May 2006, Vol. 107, No. 9, pp. 3564-3571. Prepublished online as a Blood First Edition Paper on January 10, 2006; DOI 10.1182/blood-2005-07-2961. This Article Full Text Full Text (PDF) All Versions of this Article: 2005-07-2961v1 107/9/3564    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Huang, Y. Articles by Luo, Y. Search for Related Content PubMed PubMed Citation Articles by Huang, Y. Articles by Luo, Y. Related Collections Hemostasis, Thrombosis, and Vascular Biology Cell Adhesion and Motility Cytoskeleton Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY The angiogenic function of nucleolin is mediated by vascular endothelial growth factor and nonmuscle myosin Yujie Huang, Hubing Shi, Hao Zhou, Xiaomin Song, Shaopeng Yuan, and Yongzhang Luo From the Laboratory of Protein Chemistry, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing, China. Nucleolin, originally described as a nuclear protein, was recently found to be expressed on the surface of endothelial cells during angiogenic. However, the functions of cell-surface nucleolin in angiogenic remain mysterious. Here we report that upon endothelial cells adhering to extracellular matrix components, vascular endothelial growth factor (VEGF) mobilizes nucleolin from nucleus to cell surface. Functional blockage or down-regulation of the expression of cell-surface nucleolin in endothelial cells significantly inhibits the migration of endothelial cells and prevents capillary-tubule formation. Moreover, nonmuscle myosin heavy chain 9 (MyH9), an actin-based motor protein, is identified as a nucleolin-binding protein. Subsequent studies reveal that MyH9 serves as a physical linker between nucleolin and cytoskeleton, thus modulating the translocation of nucleolin. Knocking down endogenous MyH9, specifically inhibiting myosin activity, or overexpressing functional deficient MyH9 disrupts the organization of cell-surface nucleolin and inhibits its angiogenic function. These studies indicate that VEGF, extracellular matrix, and intracellular motor protein MyH9 are all essential for the novel function of nucleolin in angiogenic. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: V. Stepanova, T. Lebedeva, A. Kuo, S. Yarovoi, S. Tkachuk, S. Zaitsev, K. Bdeir, I. Dumler, M. S. Marks, Y. Parfyonova, et al. Nuclear translocation of urokinase-type plasminogen activator Blood, July 1, 2008; 112(1): 100 - 110. [Abstract] [Full Text] [PDF] Y. Teng, A. C. Girvan, L. K. Casson, W. M. Pierce Jr., M. Qian, S. D. Thomas, and P. J. Bates AS1411 Alters the Localization of a Complex Containing Protein Arginine Methyltransferase 5 and Nucleolin Cancer Res., November 1, 2007; 67(21): 10491 - 10500. [Abstract] [Full Text] [PDF] H. Shi, Y. Huang, H. Zhou, X. Song, S. Yuan, Y. Fu, and Y. Luo Nucleolin is a receptor that mediates antiangiogenic and antitumor activity of endostatin Blood, October 15, 2007; 110(8): 2899 - 2906. [Abstract] [Full Text] [PDF] M. Xie, I. Kobayashi, T. Kiyoshima, H. Yamaza, J.-y. Honda, K. Takahashi, N. Enoki, A. Akamine, and H. Sakai Functional Implication of Nucleolin in the Mouse First Molar Development J. Biol. Chem., August 10, 2007; 282(32): 23275 - 23283. [Abstract] [Full Text] [PDF] C. R. Ireson and L. R. Kelland Discovery and development of anticancer aptamers Mol. Cancer Ther., December 1, 2006; 5(12): 2957 - 2962. [Abstract] [Full Text] [PDF]

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