Targeted therapy of human glioblastoma via delivery of a toxin through a peptide directed to cell surface nucleolin

2017 ◽  
Vol 233 (5) ◽  
pp. 4091-4105 ◽  
Author(s):  
Anne-Chloé Dhez ◽  
Elisabetta Benedetti ◽  
Andrea Antonosante ◽  
Gloria Panella ◽  
Brigida Ranieri ◽  
...  
Keyword(s):  
Targeted Therapy ◽  
Cell Surface ◽  
Human Glioblastoma ◽  
Surface Nucleolin ◽  
Cell Surface Nucleolin

scholarly journals Pre-B acute lymphoblastic leukemia expresses cell surface nucleolin as a 9-O-acetylated sialoglycoprotein

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Eun Ji Joo ◽  
Brian R Wasik ◽  
Colin Parrish ◽  
Helicia Paz ◽  
Martina Mϋhlenhoff ◽  
...  
Keyword(s):  
Acute Lymphoblastic Leukemia ◽  
Cell Surface ◽  
Lymphoblastic Leukemia ◽  
Surface Nucleolin ◽  
Cell Surface Nucleolin

Abstract 1476: Cell surface nucleolin acts as a specific receptor of Tipα, a carcinogenic factor released fromH. pylori

2010 ◽  
Author(s):  
Masami Suganuma ◽  
Tatsuro Watanabe ◽  
Hideaki Tsuge ◽  
Kazuo Hirano ◽  
Masatoshi Beppu ◽  
...  
Keyword(s):  
Cell Surface ◽  
Specific Receptor ◽  
Surface Nucleolin ◽  
Cell Surface Nucleolin

Cell surface nucleolin antagonist causes endothelial cell apoptosis and normalization of tumor vasculature

Angiogenesis ◽  
2009 ◽  
Vol 12 (1) ◽  
pp. 91-100 ◽  
Author(s):  
Valentina Fogal ◽  
Kazuki N. Sugahara ◽  
Erkki Ruoslahti ◽  
Sven Christian
Keyword(s):  
Endothelial Cell ◽  
Cell Surface ◽  
Cell Apoptosis ◽  
Tumor Vasculature ◽  
Endothelial Cell Apoptosis ◽  
Surface Nucleolin ◽  
Cell Surface Nucleolin

Nucleolin is a receptor that mediates antiangiogenic and antitumor activity of endostatin

Blood ◽  
2007 ◽  
Vol 110 (8) ◽  
pp. 2899-2906 ◽  
Author(s):  
Hubing Shi ◽  
Yujie Huang ◽  
Hao Zhou ◽  
Xiaomin Song ◽  
Shaopeng Yuan ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Cell Surface ◽  
Neutralizing Antibody ◽  
Cell Nuclei ◽  
Antitumor Activities ◽  
Surface Nucleolin ◽  
Tumor Environment ◽  
Cell Surface Nucleolin ◽  
Functional Receptor

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.

Cell surface nucleolin is crucial in the activation of the CXCL12/CXCR4 signaling pathway

Tumor Biology ◽  
2013 ◽  
Vol 35 (1) ◽  
pp. 333-338 ◽  
Author(s):  
Xiangshan Yang ◽  
Zhongfa Xu ◽  
Daotang Li ◽  
Shaomei Cheng ◽  
Kaixi Fan ◽  
...  
Keyword(s):  
Cell Surface ◽  
Signaling Pathway ◽  
Cxcr4 Signaling ◽  
Surface Nucleolin ◽  
Cell Surface Nucleolin

scholarly journals Cell Surface Nucleolin Serves as Receptor for DNA Nanoparticles Composed of Pegylated Polylysine and DNA

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

The angiogenic function of nucleolin is mediated by vascular endothelial growth factor and nonmuscle myosin

Blood ◽  
2006 ◽  
Vol 107 (9) ◽  
pp. 3564-3571 ◽  
Author(s):  
Yujie Huang ◽  
Hubing Shi ◽  
Hao Zhou ◽  
Xiaomin Song ◽  
Shaopeng Yuan ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Vascular Endothelial Growth Factor ◽  
Endothelial Cells ◽  
Growth Factor ◽  
Cell Surface ◽  
Vascular Endothelial ◽  
Nonmuscle Myosin ◽  
Surface Nucleolin ◽  
Cell Surface Nucleolin ◽  
Endothelial Growth Factor

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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