An amino-terminal fragment of urokinase isolated from a prostate cancer cell line (PC-3) is mitogenic for osteoblast-like cells

Shafast A. Rabbani, Johanne Desjardins, Alexander W. Bell, Denis Banville, Andrew Mazar, Jack Henkin, David Goltzman*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    173 Scopus citations

    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 languageEnglish (US)
    Pages (from-to)1058-1064
    Number of pages7
    JournalBiochemical and Biophysical Research Communications
    Volume173
    Issue number3
    DOIs
    StatePublished - Dec 31 1990

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

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