2002
DOI: 10.1016/s1535-6108(02)00097-1
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Targeting ligand-activated ErbB2 signaling inhibits breast and prostate tumor growth

Abstract: ErbB2 is a ligand-less member of the ErbB receptor family that functions as a coreceptor with EGFR, ErbB3, and ErbB4. Here, we describe an approach to target ErbB2's role as a coreceptor using a monoclonal antibody, 2C4, which sterically hinders ErbB2's recruitment into ErbB ligand complexes. Inhibition of ligand-dependent ErbB2 signaling by 2C4 occurs in both low- and high-ErbB2-expressing systems. Since the ErbB3 receptor contains an inactive tyrosine kinase domain, 2C4 is very effective in blocking hereguli… Show more

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Cited by 802 publications
(600 citation statements)
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References 55 publications
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“…The anti-ErbB1 antibody cetuximab inhibits ligandmediated phosphorylation of ErbB1 by directly competing with ligand binding to ErbB1 (Prewett et al, 1998). The anti-ErbB2 mAb pertuzumab sterically hinders recruitment of ErbB2 into ErbB/ligand complexes An isoform-specific anti-ErbB4 antibody M Hollmén et al affecting the formation and activation of ErbB2-containing dimers (Agus et al, 2002;Franklin et al, 2004). However, our preliminary in vitro experiments with recombinant proteins suggest that mAb 1479 does not compete with NRG binding to ErbB4 or interfere with NRG-induced ErbB4 dimerization.…”
Section: Discussionmentioning
confidence: 68%
“…The anti-ErbB1 antibody cetuximab inhibits ligandmediated phosphorylation of ErbB1 by directly competing with ligand binding to ErbB1 (Prewett et al, 1998). The anti-ErbB2 mAb pertuzumab sterically hinders recruitment of ErbB2 into ErbB/ligand complexes An isoform-specific anti-ErbB4 antibody M Hollmén et al affecting the formation and activation of ErbB2-containing dimers (Agus et al, 2002;Franklin et al, 2004). However, our preliminary in vitro experiments with recombinant proteins suggest that mAb 1479 does not compete with NRG binding to ErbB4 or interfere with NRG-induced ErbB4 dimerization.…”
Section: Discussionmentioning
confidence: 68%
“…Blots were reprobed for b-actin to account for loading differences. (Agus et al, 2002;Mendoza et al, 2002) and further implies that NHEK lack the formation of such heterodimers in response to EGF.…”
Section: Results Egfr Is the Major Her/erbb Receptor In Primary Humanmentioning
confidence: 99%
“…PCR reactions for each template were run in triplicate using 1 mg of total RNA per sample. The sequences of the primer/ probe sets for the HER-kinase axis were described previously (Agus et al, 2002). Standard curves were constructed for each genespecific primer pair using 10 -1000 ng of total RNA prepared from CWR22R xenografts.…”
Section: Rna Extraction and Real-time Quantitative Rt-pcrmentioning
confidence: 99%
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“…But convincing evidence in support of this hypothesis has not yet emerged. In pulldown assays, trastuzumab does not inhibit HER2-HER3 interaction (Agus et al, 2002), and in fluorescence resonance energy transfer (FRET)-based assays trastuzumab also does not inhibit HER2 interaction with EGFR or HER3 (Diermeier et al, 2005). In a different model using truncated HER proteins fusing them to b-galactosidase fragments in an enzyme complementation assay, trastuzumab was reported to inhibit EGFR-HER2 interaction but not HER2-HER3 interactions (Wehrman et al, 2006).…”
Section: Mechanism Of Action Of Trastuzumab -Her2 Signalingmentioning
confidence: 99%