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Cell. 1990 Jun 29;61(7):1339-47.

Intermolecular association of the p185neu protein and EGF receptor modulates EGF receptor function.

Author information

1
Department of Pathology, University of Pennsylvania School of Medicine, Philadelphia 19104-6082.

Abstract

We have used cross-linking reagents on cell lines expressing both p185neu and EGFR. The lysates of the cells were precipitated with anti-p185neu or anti-EGFR antibodies. These precipitates included a high molecular weight complex that was identified as an EGFR-p185neu heterodimer. Heterodimerization was found to be induced by exposure to EGR. The EGFR of these cells displayed three affinity states for EGF: low (Kd, approximately 10(-9) M), high (Kd, 10(-9) to 10(-10) M), and very high (Kd, 10(-11) M), as determined by Scatchard analyses. Relatively small levels of EGF had a dramatic biological effect on cells expressing very high affinity EGFR. The very high affinity EGFR disappeared after the cells were treated with anti-p185neu monoclonal antibodies that selectively down-regulated p185neu. EGF and TPA had differential effects on down-modulation of the EGFR in cells that express either one or both species of receptor proteins.

PMID:
1973074
DOI:
10.1016/0092-8674(90)90697-d
[Indexed for MEDLINE]

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