A role for urokinase in mediating phorbol ester induced macrophagelike maturation and adhesion of u937 and other myeloid cells

A. R. Nusrat*, A. Mazar, J. Henkin, H. A. Chapman

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    3 Scopus citations

    Abstract

    The phorbol ester, phorbol myristate acetate (PMA), induces myeloid cells to differentiate towards the macrophage lineage. Polyclonal antibodies to the urokinase plasminogen activator (u-PA) interfere with this process as defined by the inability of U937 cells to adhere on tissue culture surfaces. This block in differentiation is overcome by a 21 amino acid synthetic peptide from the u-PA growth factor domain which has residues of the receptor binding sequence. Moreover, a 40 amino acid peptide from the u-PA growth factor domain is more potent and enhances by 4-fold the PMA stimulated adhesion of a similar cell line, HL60. These observations indicate that the growth factor domain of u-PA plays an important role in PMA mediated myeloid cell differentiation and adhesion.

    Original languageEnglish (US)
    Pages (from-to)71-75
    Number of pages5
    JournalFibrinolysis and Proteolysis
    Volume6
    Issue numberSUPPL. 1
    DOIs
    StatePublished - Jan 1992

    ASJC Scopus subject areas

    • Hematology

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