Cathepsin D, a lysosomal aspartic proteinase, is secreted in the form
of enzymatically inactive precursor in some cancer cells. This precurs
or, called procathepsin D, was found to exhibit growth factor activity
toward breast cancer cell lines and this activity was later shown to
be mediated by its activation peptide. In the present investigation we
have used human procathepsin D and a synthetic 44 amino acid peptide
corresponding to the activation peptide of procathepsin D to test its
growth factor activity for human prostate cancer-derived cell lines PC
3, DU145 and LNCaP. We have tested the level of proliferation of these
cell lines depending on the presence of either procathepsin or activa
tion peptide in the medium. In parallel, we have also measured the tim
e dependency of this growth and established the optimal dose of activa
tion peptide. These findings represent the first experimental data sho
wing the direct effects of procathepsin D on prostate cancer cells. (C
) 1998 Elsevier Science Ireland Ltd. All rights reserved.