Monoclonal anti-epidermal growth factor receptor antibodies which are inhibitors of epidermal growth factor binding and antagonists of epidermal growth factor binding and antagonists of epidermal growth factor-stimulated tyrosine protein kinase activity.

Gill, Gordon N.; Kawamoto, Tomoyuki; Cochet, Claude; Le, Anh D.; Sato, Jun; Masui, Hideo; McLeod, Chris; Mendelsohn, John

doi:10.1016/s0021-9258(17)42857-2

Cited by 418 publications

(48 citation statements)

References 28 publications

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“…The EGF receptorblocking monoclonal antibody 225 (MAb 225) was kindly provided by Dr. J. Mendelsohn. The biological and biochemical characteristics of MAb 225 have been described (Gill et al, 1984).…”

Section: Methodsmentioning

confidence: 99%

EGF-related peptides are involved in the proliferation and survival of MDA-MB-468 human breast carcinoma cells

et al. 1999

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Section: Methodsmentioning

confidence: 99%

EGF-related peptides are involved in the proliferation and survival of MDA-MB-468 human breast carcinoma cells

et al. 1999

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“…This antibody fragment, although not completely specific, as it is known to bind blood group-A carbohydrate antigens (Gooi et al, 1983), did not impede growth factor binding and therefore later enabled us to follow oligomerization after binding. The initial oligomeric state was also investigated using FRET measurements on donor-and acceptor-conjugated Fab fragments of the monoclonal anti-EGFR antibody 225, which exclusively binds to the EGF binding site and therefore prevents EGR binding (Gill et al, 1984). The donor fluorescence lifetimes of a 1:2 mixture of donor Al-Fab 29.1 and acceptor Er-Fab 29.1-bound A431 cells when compared with those from cells bound with a 1:2 mixture of Al-Fab 29.1 and unlabeled Fab 29.1, showed a decrease of 0.21 ns (bars 12 and 13 in Fig.…”

Section: High-affinity Egfrs Are Constitutive Oligomers In A431 Cellsmentioning

confidence: 99%

Preformed Oligomeric Epidermal Growth Factor Receptors Undergo an Ectodomain Structure Change during Signaling

Martin-Fernandez

Clarke

Tobin

et al. 2002

Biophysical Journal

109

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Fluorescence resonance energy transfer (FRET) was used to reveal aspects of the mechanism of signal transduction by epidermal growth factor receptors (EGFR). The superpositions of epidermal growth factor (EGF), transforming growth factor-alpha (TGFalpha) and an antibody fragment (29.1) to the carbohydrate extremity of the receptor's ectodomain as measured by FRET, show that 14% of EGFRs in A431 cells are oligomerized before growth factor binding. After binding growth factor and signaling, these oligomers dissociate before releasing growth factor. Time courses of the FRET-derived distances between constitutively oligomerized EGFRs during signal transduction show a transient structural change in the extracellular domain, which occurs simultaneously with the production of intracellular Ca2+ signals. The FRET measurements also show a slow increase in oligomerization of EGFR monomers after growth factor binding. The structural change found in the extracellular domain of oligomeric EGFRs is similar to that shown by others for EPO, Neu, Fas, and tumor necrosis factor receptors, and may therefore be a common property of the transduction of the receptor-mediated signals.

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“…aEGFR binds to A431, HeLa cells, and other human cells. It inhibits ligand binding to receptor and acts as an antagonist of EGF-stimulated tyrosine kinase activity (Gill et al, 1984;Kawamoto et al, 1984). The antibody was used at 1 µg per ml in these experiments.…”

Section: Blocking By Aegfrmentioning

confidence: 99%

Endogenous EGF-Family Growth Factors are Necessary for the Progression from the G1 to S Phase in Human Keratinocytes

Kobayashi

Hashimoto²,

Okumura³

et al. 1998

Journal of Investigative Dermatology

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Recently several endogenous epidermal growth factor (EGF)-family growth factors (transforming growth factor-alpha, amphiregulin, and heparin-binding EGF-like growth factor) have been identified in human keratinocytes. These factors are known to play an important role in the regulation of cell proliferation. Here we show that the interaction between these factors and EGF receptor are key factors in the progression from the G1 phase to the S phase (the G1/S progression) in human keratinocytes. In this study, human keratinocytes were cultured in serum-free MCDB153 medium and then partially synchronized by isoleucine deprivation. After synchronization, the number of S phase cells increased and reached a maximum after 18-24 h. The immediate addition of anti-EGF receptor blocking antibody (1 microg per ml) to synchronized cells decreased S phase cells by 42.5% compared with untreated keratinocytes at 18 h. By contrast, the addition of anti-EGF receptor antibodies at 12 h or later did not alter the percentage of S phase cells. Northern blot analysis of synchronized cells demonstrated that mRNA expression of transforming growth factor-alpha, amphiregulin, heparin-binding EGF-like growth factor, and EGF receptor reached a maximum within 0.5-3 h after synchronization, when many cells initiated progression from the G1 to the S phase. The results show that anti-EGF receptor antibodies block the G1/S progression and the rapid increase of mRNA expression of endogenous EGF-family growth factors and EGF receptor during G1/S progression. These findings indicate that growth factor binding and EGF receptor activation are involved in the G1/S cell cycle progression of human keratinocytes.

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Monoclonal anti-epidermal growth factor receptor antibodies which are inhibitors of epidermal growth factor binding and antagonists of epidermal growth factor binding and antagonists of epidermal growth factor-stimulated tyrosine protein kinase activity.

Cited by 418 publications

References 28 publications

EGF-related peptides are involved in the proliferation and survival of MDA-MB-468 human breast carcinoma cells

EGF-related peptides are involved in the proliferation and survival of MDA-MB-468 human breast carcinoma cells

Preformed Oligomeric Epidermal Growth Factor Receptors Undergo an Ectodomain Structure Change during Signaling

Endogenous EGF-Family Growth Factors are Necessary for the Progression from the G1 to S Phase in Human Keratinocytes

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