Abstract
A peptide mitogen for cultured osteoblast-like cells was purified from aerum-free conditioned culture medium of a human prostatic cancer cell line, PC-3. Based on amino acid sequencing and estimated molecular weight, this peptide was identified as an NH2-terminal fragment of urokinase-type plasminogen activator (uPA). Recombinant high molecular weight (HMW) uPA and the NH2-terminal growth factor domain (GFD) of uPA, but not low molecular weight (LMW) uPA (lacking the NH2-terminal region) stimulated [3H]thymidine incorporation and proliferation in osteoblast-like cells, and specific, competitive binding sites for HMW, but not LMW, uPA were demonstrable. These studies demonstrate the production of a mitogenic NH2-terminal fragment of uPA by a human prostatic cancer cell line which may be of importance in the pathogenesis of osteoblastic metastases.
Original language | English (US) |
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Pages (from-to) | 1058-1064 |
Number of pages | 7 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 173 |
Issue number | 3 |
DOIs | |
State | Published - Dec 31 1990 |
Funding
We thank I. Bolivar, F. Dumas and B. Gibbs for technical assistance and D. Allen for secreterial assistance. This work was supported by National Institute of Health Grant ROI CA 37126 and by Medical Research Council of Canada Grants MT-5775 and MT-10630.
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology