A folded synthetic peptide analog of NDF (NDF5), which has the 52 amin
o acid EGF-like domain of NDF alpha 2, has been characterized. The fol
ded peptide stimulates tyrosine phosphorylation of Her2, Her3 and Her4
in breast cancer cells and competes with low affinity with full-lengt
h NDF alpha 2 for binding to the cells, while the linear one does not.
NDF5 also induces morphologic changes in breast cancer cells. After s
everal days treatment with NDF5 or NDF alpha 2, Here-transfected MCF7
cells (Her2/MCF7) became similar morphologically to non-transfected MC
F7. The biological activity of NDF5 is between 1/10 and 1/100 that of
NDF alpha 2. This suggests that other motifs, such as the Ig and space
r domains may be important elements in conferring full activity. (C) 1
995 Academic Press, Inc.