scholarly journals Radioiodine-labeled anti-epidermal growth factor receptor binding bovine serum albumin-polycaprolactone for targeting imaging of glioblastoma

2017 ◽  
Vol 38 (5) ◽  
pp. 2919-2926 ◽  
Author(s):  
Chengxia Li ◽  
Jian Tan ◽  
Jin Chang ◽  
Wei Li ◽  
Zhongyun Liu ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Receptor Binding ◽  
Bovine Serum ◽  
Growth Factor Receptor ◽  
Epidermal Growth

scholarly journals Growth Factor Receptor Binding Protein 2-mediated Recruitment of the RING Domain of Cbl to the Epidermal Growth Factor Receptor Is Essential and Sufficient to Support Receptor Endocytosis

2005 ◽  
Vol 16 (3) ◽  
pp. 1268-1281 ◽  
Author(s):  
Fangtian Huang ◽  
Alexander Sorkin
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Receptor Binding ◽  
Binding Protein ◽  
Growth Factor Receptor ◽  
Ring Domain ◽  
Receptor Endocytosis ◽  
Epidermal Growth ◽  
Receptor Binding Protein

Knockdown of growth factor receptor binding protein 2 (Grb2) by RNA interference strongly inhibits clathrin-mediated endocytosis of the epidermal growth factor receptor (EGFR). To gain insights into the function of Grb2 in EGFR endocytosis, we have generated cell lines in which endogenous Grb2 was replaced by yellow fluorescent protein (YFP)-tagged Grb2 expressed at the physiological level. In these cells, Grb2-YFP fully reversed the inhibitory effect of Grb2 knockdown on EGFR endocytosis and, moreover, trafficked together with EGFR during endocytosis. Overexpression of Grb2-binding protein c-Cbl did not restore endocytosis in Grb2-depleted cells. However, EGFR endocytosis was rescued in Grb2-depleted cells by chimeric proteins consisting of the Src homology (SH) 2 domain of Grb2 fused to c-Cbl. The “knockdown and rescue” analysis revealed that the expression of Cbl-Grb2/SH2 fusions containing RING finger domain of Cbl restores normal ubiquitylation and internalization of the EGFR in the absence of Grb2, consistent with the important role of the RING domain in EGFR endocytosis. In contrast, the carboxy-terminal domain of Cbl, when attached to Grb2 SH2 domain, had 4 times smaller endocytosis-rescue effect compared with the RING-containing chimeras. Together, the data suggest that the interaction of Cbl carboxy terminus with CIN85 has a minor and a redundant role in EGFR internalization. We concluded that Grb2-mediated recruitment of the functional RING domain of Cbl to the EGFR is essential and sufficient to support receptor endocytosis.

scholarly journals Quantitation of the Effect of ErbB2 on Epidermal Growth Factor Receptor Binding and Dimerization

2012 ◽  
Vol 287 (37) ◽  
pp. 31116-31125 ◽  
Author(s):  
Yu Li ◽  
Jennifer Macdonald-Obermann ◽  
Corey Westfall ◽  
David Piwnica-Worms ◽  
Linda J. Pike
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Receptor Binding ◽  
Growth Factor Receptor ◽  
Epidermal Growth

Characterization of a monoclonal antibody directed against the epidermal growth factor receptor binding site

1991 ◽  
Vol 34 (1) ◽  
pp. 37-42 ◽  
Author(s):  
Rita Pellegrini ◽  
Filippo Centis ◽  
Stefania Martignone ◽  
Antonio Mastroianni ◽  
Elda Tagliabue ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Binding Site ◽  
Receptor Binding ◽  
Growth Factor Receptor ◽  
Receptor Binding Site ◽  
Epidermal Growth
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