Küng W, David F, Langen H, Weyer K A, Schlaeger E J, Lahm H W, Silber E, Mueller H, Eppenberger U
Department of Research, University Clinics, Kantonsspital Basel, Switzerland.
Biochem Biophys Res Commun. 1994 Aug 15;202(3):1357-65. doi: 10.1006/bbrc.1994.2080.
A 52 kDa peptide growth factor secreted by the estrogen receptor (ER)-negative human breast cancer cell line MDA-MB-231 was purified to homogeneity. It induced transient membrane ruffling, lamellipodia formation, cell motility and proliferation exclusively of ER-positive human breast cancer cells. Partial sequencing revealed a high homology to the protein family of heregulins. However, the obtained amino acid sequences of the new factor were not completely identical to any of the members of the heregulin family. This finding together with the observation that the successful purification protocol was significantly different from that used to isolate other members of the heregulin family indicate the isolation of a novel heregulin-like proliferation factor for ER-positive human breast cancer cells.