scholarly journals Cell surface nucleolin as active bait for nanomedicine in cancer therapy: a promising option

2021 ◽  
Author(s):  
Benedetta Ferrara ◽  
Sabrina Belbekhouche ◽  
Damien Habert ◽  
Claire Houpe ◽  
Benoit Vallée ◽  
...  
2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Eun Ji Joo ◽  
Brian R Wasik ◽  
Colin Parrish ◽  
Helicia Paz ◽  
Martina Mϋhlenhoff ◽  
...  

2010 ◽  
Author(s):  
Masami Suganuma ◽  
Tatsuro Watanabe ◽  
Hideaki Tsuge ◽  
Kazuo Hirano ◽  
Masatoshi Beppu ◽  
...  

Angiogenesis ◽  
2009 ◽  
Vol 12 (1) ◽  
pp. 91-100 ◽  
Author(s):  
Valentina Fogal ◽  
Kazuki N. Sugahara ◽  
Erkki Ruoslahti ◽  
Sven Christian

Blood ◽  
2007 ◽  
Vol 110 (8) ◽  
pp. 2899-2906 ◽  
Author(s):  
Hubing Shi ◽  
Yujie Huang ◽  
Hao Zhou ◽  
Xiaomin Song ◽  
Shaopeng Yuan ◽  
...  

AbstractThe exact molecular mechanism of how endostatin inhibits angiogenesis and tumor growth remains uncharacterized. Here, we report that endostatin specifically binds to the cell surface nucleolin with high affinity. Blockage of nucleolin by a neutralizing antibody or knockdown of nucleolin by the RNA interference results in loss of antiendothelial activities of endostatin. Importantly, a neutralizing antinucleolin antibody abrogates the antiangiogenic and antitumor activities of endostatin in vivo. Nucleolin and endostatin are colocalized on the cell surface of endothelial cells of angiogenic blood vessels in the tumor environment. Finally, we found that endostatin is internalized and transported into cell nuclei of endothelial cell via nucleolin. In the nucleus, the phosphorylation of nucleolin, which is critical for cell proliferation, can be inhibited by endostatin. Our studies demonstrate that nucleolin is a novel functional receptor for endostatin, and mediates the antiangiogenic and antitumor activities of endostatin. These findings also provide mechanistic insights of how endostatin specifically inhibits proliferating endothelial cell growth and angiogenesis.


Tumor Biology ◽  
2013 ◽  
Vol 35 (1) ◽  
pp. 333-338 ◽  
Author(s):  
Xiangshan Yang ◽  
Zhongfa Xu ◽  
Daotang Li ◽  
Shaomei Cheng ◽  
Kaixi Fan ◽  
...  

2008 ◽  
Vol 16 (2) ◽  
pp. 333-342 ◽  
Author(s):  
Xuguang Chen ◽  
Dianne M Kube ◽  
Mark J Cooper ◽  
Pamela B Davis

Blood ◽  
2006 ◽  
Vol 107 (9) ◽  
pp. 3564-3571 ◽  
Author(s):  
Yujie Huang ◽  
Hubing Shi ◽  
Hao Zhou ◽  
Xiaomin Song ◽  
Shaopeng Yuan ◽  
...  

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.


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