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A soluble form of the urokinase plasminogen activator receptor (suPAR) can bind to hematopoietic cells

dc.contributor.authorMizukami, Ikuko F.
dc.contributor.authorTodd, Robert F.
dc.date.accessioned2018-02-05T16:48:31Z
dc.date.available2018-02-05T16:48:31Z
dc.date.issued1998-08
dc.identifier.citationMizukami, Ikuko F.; Todd, Robert F. (1998). "A soluble form of the urokinase plasminogen activator receptor (suPAR) can bind to hematopoietic cells." Journal of Leukocyte Biology 64(2): 203-213.
dc.identifier.issn0741-5400
dc.identifier.issn1938-3673
dc.identifier.urihttps://hdl.handle.net/2027.42/142227
dc.description.abstractThe receptor for urokinase plasminogen activator (uPAR; CD87) is a 50‐ to 65‐kDa glycosylphosphatidylinositol (GPI)‐anchored glycoprotein expressed by leukocytes and tumor cells where it facilitates uPA‐dependent, plasmin‐mediated pericellular proteolysis during cellular invasion. Because uPAR is inducibly shed into culture supernatants and human body fluids, we tested the hypothesis that soluble uPAR (suPAR) can bind to the plasma membrane of hematopoietic cells where it might modulate their invasive phenotype. As measured by flow cytometry, recombinant biotinylated‐suPAR (B‐suPAR) bound in a specific fashion to THP‐1 leukemia cells and blood PMNs and monocytes (but not to lymphocytes). B‐suPAR also demonstrated specific binding to a variety of leukemic lines, including cells that are positive or negative for membrane uPAR expression. Binding of B‐suPAR to THP‐1 cells was enhanced four‐ to sevenfold by 24‐h exposure of cells to PMA or by coincubation with uPA ligand (but not its isolated catalytic and binding fragments). Conversely, binding of B‐suPAR to PMNs was unaffected by brief exposure to fMLP, and was inhibited by coincubation with uPA. B‐suPAR binding to PMA‐differentiated THP‐1 cells in the presence of uPA was further enhanced by acid washing (removing endogenous uPA) but was partially inhibited by treatment of cells with trypsin. Pretreatment of PMA‐differentiated THP‐1 cells and unstimulated PMNs with soluble sugars, calcium chelators, and antibodies specific for integrins or extracellular matrix proteins failed to consistently block the binding of B‐suPAR. Whereas the binding of suPAR did not measurably affect cell‐associated plasmin activation, suPAR did competitively inhibit the binding of exogenous uPA to membrane‐associated uPAR. These observations support the hypothesis that suPAR can bind specifically to trypsin‐sensitive receptors expressed by certain normal and neoplastic hematopoietic cells where its binding is variably influenced by uPA ligand. J. Leukoc. Biol. 64: 203–213; 1998.
dc.publisherWiley Periodicals, Inc.
dc.subject.othersoluble receptor
dc.subject.otherbinding
dc.titleA soluble form of the urokinase plasminogen activator receptor (suPAR) can bind to hematopoietic cells
dc.typeArticleen_US
dc.rights.robotsIndexNoFollow
dc.subject.hlbsecondlevelMicrobiology and Immunology
dc.subject.hlbtoplevelHealth Sciences
dc.description.peerreviewedPeer Reviewed
dc.contributor.affiliationumDivision of Hematology/Oncology, Department of Internal Medicine, and the University of Michigan Comprehensive Cancer Center, Ann Arbor
dc.description.bitstreamurlhttps://deepblue.lib.umich.edu/bitstream/2027.42/142227/1/jlb0203.pdf
dc.identifier.doi10.1002/jlb.64.2.203
dc.identifier.sourceJournal of Leukocyte Biology
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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