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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Characterization of a breast cancer cell differentiation factor that specifically activates the HER4/p180erbB4 receptor.

We recently reported the molecular cloning of HER4/p180erbB4, a new member of the epidermal growth factor receptor family, as well as its activation by a partially purified ligand (Plowman, G. D., Culouscou, J.-M., Whitney, G. S., Green, J. M., Carlton, G. W., Foy, L., Neubauer, M. G., and Shoyab, M. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 1746-1750). In this report we describe the purification to homogeneity of a 45-kDa protein ( p45) that induces the differentiation of MDA-MB-453 human breast cancer cells and stimulates the tyrosine phosphorylation of p180erbB4, the HER4-encoded protein. Hydrophobic interaction, ion-exchange, heparin, and size exclusion chromatographies were used to purify this p180erbB4 activator to homogeneity. N-terminal amino acid sequencing suggests that p45 is related to heregulin, a recently reported ligand for p185erbB2. Binding and cross-linking experiments demonstrated that p45 specifically binds to cells expressing recombinant p180erbB4 and not cells expressing recombinant p185erbB2.[1]

References

  1. Characterization of a breast cancer cell differentiation factor that specifically activates the HER4/p180erbB4 receptor. Culouscou, J.M., Plowman, G.D., Carlton, G.W., Green, J.M., Shoyab, M. J. Biol. Chem. (1993) [Pubmed]
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