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Urokinaseâ deficient and urokinase receptorâ deficient mice have impaired neutrophil antimicrobial activation in vitro
dc.contributor.authorGyetko, Margaret R.
dc.contributor.authorAizenberg, David
dc.contributor.authorMayo‐bond, Laura
dc.date.accessioned2018-02-05T16:32:29Z
dc.date.available2018-02-05T16:32:29Z
dc.date.issued2004-09
dc.identifier.citationGyetko, Margaret R.; Aizenberg, David; Mayo‐bond, Laura (2004). "Urokinaseâ deficient and urokinase receptorâ deficient mice have impaired neutrophil antimicrobial activation in vitro." Journal of Leukocyte Biology 76(3): 648-656.
dc.identifier.issn0741-5400
dc.identifier.issn1938-3673
dc.identifier.urihttps://hdl.handle.net/2027.42/141382
dc.publisherCold Spring Harbor Laboratory
dc.publisherWiley Periodicals, Inc.
dc.subject.otherinflammation
dc.subject.othercellular activation
dc.subject.otherphagocytosis
dc.subject.othertransgenic/knockout
dc.titleUrokinaseâ deficient and urokinase receptorâ deficient mice have impaired neutrophil antimicrobial activation in vitro
dc.typeArticleen_US
dc.rights.robotsIndexNoFollow
dc.subject.hlbsecondlevelMicrobiology and Immunology
dc.subject.hlbtoplevelHealth Sciences
dc.description.peerreviewedPeer Reviewed
dc.contributor.affiliationumPulmonary and Critical Care Medicine Division, Department of Internal Medicine, Ann Arbor Veterans Affairs Medical Center and University of Michigan Medical Center, Ann Arbor
dc.description.bitstreamurlhttps://deepblue.lib.umich.edu/bitstream/2027.42/141382/1/jlb0648.pdf
dc.identifier.doi10.1189/jlb.0104023
dc.identifier.sourceJournal of Leukocyte Biology
dc.identifier.citedreferenceWelch, H., Maridonneauâ Parini, I. ( 1997 ) Lyn and Fgr are activated in distinct membrane fractions of human granulocytic cells. Oncogene 15, 2021 â 2029.
dc.identifier.citedreferenceWolfson, M., McPhail, L. C., Nasrallah, V. N., Snyderman, R. ( 1985 ) Phorbol myristate acetate mediates redistribution of protein kinase C in human neutrophils: Potential role in the activation of the respiratory burst enzyme. J. Immunol. 135, 2057 â 2062.
dc.identifier.citedreferenceHampton, M. B., Kettle, A. J., Winterbourn, C. C. ( 1998 ) Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing. Blood 92, 3007 â 3017.
dc.identifier.citedreferenceWinkelstein, J. A., Marino, M. C., Johnston, R. B. J., Boyle, J., Curnutte, J., Gallin, J. I., Malech, H. L., Holland, S. M., Ochs, H. ( 2000 ) Chronic granulomatous disease. Report on a national registry of 368 patients. Medicine (Baltimore) 79, 155 â 169.
dc.identifier.citedreferenceSegal, B. H., Leto, T. L., Gallin, J. I., Malech, H. L., Holland, S. M. G. ( 2000 ) Genetic, biochemical, and clinical features of chronic granulomatous disease. Medicine (Baltimore) 79, 170 â 200.
dc.identifier.citedreferenceSegal, B. H., Holland, S. M. ( 2000 ) Primary phagocytic disorders of childhood. Pediatr. Clin. North Am. 47, 1311 â 1338.
dc.identifier.citedreferenceMoscai, A., Jakus, S., Vantus, T., Berton, G., Lowell, C. A., Ligeti, E. ( 2000 ) Kinase pathways in chemoattractantâ induced degranulation of neutrophils: The role of p38 mitogenâ activated protein kinase activated by Src family kinases. J. Immunol. 164, 4321 â 4331.
dc.identifier.citedreferenceGutkind, J. S., Robbins, K. C. ( 1989 ) Translocation of the FGR proteinâ tyrosine kinase as a consequence of neutrophil activation. Proc. Natl. Acad. Sci. USA 86, 8783 â 8787.
dc.identifier.citedreferenceMöhn, H., Le Cabec, V., Fischer, S., Maridonneauâ Parini, I. ( 1995 ) The srcâ family proteinâ tyrosine kinase p59hck is located on the secretory granules in human neutrophils and translocates towards the phagosome during cell activation. Biochem. J. 309, 657 â 665.
dc.identifier.citedreferenceKonakova, M., Hucho, F., Schleuning, W.â D. ( 1998 ) Downstream targets of urokinaseâ type plasminogenâ activatorâ mediated signal transduction. Eur. J. Biochem. 253, 421 â 429.
dc.identifier.citedreferenceBusso, N., Masur, S. K., Lazega, D., Waxman, S., Ossowski, L. ( 1994 ) Induction of cell migration by proâ urokinase binding to its receptor: possible mechanism for signal transduction in human epithelial cells. J. Cell Biol. 126, 259 â 270.
dc.identifier.citedreferenceDel Rosso, M., Anichini, E., Pedersen, N., Blasi, F., Fibbi, G., Pucci, M., Ruggiero, M. ( 1993 ) Urokinaseâ urokinase receptor interaction: nonâ mitogenic signal transduction in human epidermal cells. Biochem. Biophys. Res. Commun. 190, 347 â 352.
dc.identifier.citedreferenceDumler, I., Weis, A., Mayboroda, O. A., Maasch, C., Jerke, U., Haller, H., Gulba, D. C. ( 1998 ) The Jak/Stat pathway and urokinase receptor signaling in human aortic vascular smooth muscle cells. J. Biol. Chem. 273, 315 â 321.
dc.identifier.citedreferenceDumler, I., Petri, T., Schleuning, W. D. ( 1993 ) Interaction of urokinaseâ type plasminogen activator (uâ PA) with its cellular receptor (uPAR) induces phosphorylation on tyrosine of a 38 kDa protein. FEBS Lett. 322, 37 â 40.
dc.identifier.citedreferenceAbraham, E. A., Gyetko, M. R., Kuhn, K., Arcaroli, J., Strassheim, D., Park, J. S., Shetty, S., Idell, S. ( 2003 ) Urokinaseâ type plasminogen activator potentiates lipopolysaccharideâ induced neutrophil activation. J. Immunol. 170, 5644 â 5651.
dc.identifier.citedreferenceEstreicher, A., Wohlwend, A., Belin, D., Schleuning, W.â D., Vassalli, J.â D. ( 1989 ) Characterization of the cellular binding site for the urokinaseâ type plasminogen activator. J. Biol. Chem. 263, 1180 â 1189.
dc.identifier.citedreferenceBhat, G. J., Gunaje, J. J., Idell, S. ( 1999 ) Urokinaseâ type plasminogen activator induces tyrosine phosphorylation of a 78â kDa protein in Hâ 157 cells. Am. J. Physiol. 277, L301 â L309.
dc.identifier.citedreferencePluskota, E., Soloviev, D. A., Bdeir, K., Cines, D. B., Plow, E. F. ( 2004 ) Integrin {alpha}M{beta}2 Orchestrates and Accelerates Plasminogen Activation and Fibrinolysis by Neutrophils. J. Biol. Chem. 279, 18063 â 18072.
dc.identifier.citedreferenceVaday, G. G., Lider, O. ( 2000 ) Extracellular matrix moieties, cytokines, and enzymes: dynamic effects on immune cell behavior and inflammation. J. Leukoc. Biol. 67, 149 â 159.
dc.identifier.citedreferenceRobson, S. C., Saunders, R., Kirsch, R. E. ( 1990 ) Monocyteâ macrophage release of ILâ 1 is inhibited by typeâ 1 plasminogen activator inhibitors. J. Clin. Lab. Immunol. 33, 83 â 90.
dc.identifier.citedreferenceMatsushima, K., Taguchi, M., Kovacs, E. J., Young, H. A., Oppenheim, J. J. ( 1986 ) Intracellular localization of human monocyte associated interleukinâ 1 (ILâ 1) activity and release of biologically active ILâ 1 from monocytes by trypsin and plasmin. J. Immunol. 136, 2883 â 2891.
dc.identifier.citedreferenceWilkinson, P., Haston, W. ( 1988 ) Chemotaxis: An overview. Methods Enzymol. 162, 3 â 16.
dc.identifier.citedreferenceLauffenburger, D. ( 1991 ) Models for receptorâ mediated cell phenomena: Adhesion and migration. Annu. Rev. Biophys. Biophys. Chem. 20, 387 â 414.
dc.identifier.citedreferenceDanø, K., Andreasen, P., Grondahlâ Hansen, J., Kristensen, P., Nielsen, L., Skriver, L. ( 1985 ) Plaminogen activators, tissue degradation, and cancer. Adv. Cancer Res. 44, 139 â 265.
dc.identifier.citedreferenceHuber, A. R., Ellis, S., Johnson, K. J., Dixit, V. M., Varani, J. ( 1992 ) Monocyte diapedesis through an in vitro vessel wall construct: Inhibition with monoclonal antibodies to thrombospondin. J. Leukoc. Biol. 52, 524 â 528.
dc.identifier.citedreferenceKirchmeimer, J. C., Wojta, J., Christ, G., Hienert, G., Binder, B. R. ( 1988 ) Mitogenic effect of urokinase on malignant and unaffected adjacent human renal cells. Carcinogenesis 9, 2121 â 2123.
dc.identifier.citedreferenceLiotta, L. A., Goldfarb, R. H., Brundange, R., Siegal, G. P., Terranova, V., Garbisa, S. ( 1981 ) Effect of plasminogen activator (urokinase), plasmin, and thrombin on glycoprotein and collagenous components of basement membrane. Cancer Res. 41, 4629 â 4636.
dc.identifier.citedreferenceVassalli, J., Sappino, A., Belin, D. ( 1991 ) The plasminogen activator/plasmin system. J. Clin. Invest. 88, 1067 â 1072.
dc.identifier.citedreferenceEstreicher, A., Mühlhause, J., Carpentier, J., Orci, L., Vassalli, J. ( 1990 ) The receptor for urokinase type plasminogen activator polarizes expression of the protease to the leading edge of migrating monocytes and promotes degradation of enzyme inhibitor complexes. J. Cell Biol. 111, 783 â 792.
dc.identifier.citedreferenceSenior, R., Shapiro, S. ( 1992 ) Introduction: The matrix metalloproteinase family. Am. J. Respir. Cell Mol. Biol. 7, 119 â 127.
dc.identifier.citedreferenceWerb, Z., Mainardi, C. L., Vater, C. A., Harris, E. D. ( 1977 ) Endogenous activation of latent collagenase by synovial cells: Evidence for a role for plasminogen activator. N. Engl. J. Med. 296, 1017 â 1021.
dc.identifier.citedreferenceGyetko, M. R., Todd, R. F., III Wilkinson, C. C., Sitrin, R. G. ( 1994 ) The urokinase receptor is required for human monocyte chemotaxis in vitro. J. Clin. Invest. 93, 1380 â 1387.
dc.identifier.citedreferenceGyetko, M. R., Sitrin, R. G., Fuller, J. A., Todd, R. F., III Petty, H., Standiford, T. J. ( 1995 ) Function of the urokinase receptor (CD87) in neutrophil chemotaxis. J. Leukoc. Biol. 58, 533 â 538.
dc.identifier.citedreferenceSitrin, R. G., Todd, R. F., III Petty, H. R., Brock, T. G., Shollenberger, S. B., Albrecht, E., Gyetko, M. R. ( 1996 ) The urokinase receptor (CD87) facilitates CD11b/CD18â mediated adhesion of human monocytes. J. Clin. Invest. 97, 1942 â 1951.
dc.identifier.citedreferenceGyetko, M. R., Sud, S., Kendall, T., Fuller, J. A., Newstead, M. W., Standiford, T. ( 2000 ) Urokinase receptorâ deficient transgenic mice have impaired neutrophil recruitment in response to pulmonary pseudomonas infection. J. Immunol. 165, 1513 â 1519.
dc.identifier.citedreferenceCarmeliet, P., Schoonjans, L., Kieckens, L., Ream, B., Degen, J., Bronson, R., De Vos, R., van den Oord, J. J., Collen, D., Mulligan, R. C. ( 1994 ) Physiological consequences of loss of plasminogen activator gene function in mice. Nature 368, 419 â 424.
dc.identifier.citedreferenceDewerchin, M., Nuffelen, A. V., Wallays, G., Bouche, A., Moons, L., Carmeliet, P., Mulligan, R. C., Collen, D. ( 1996 ) Generation and characterization of urokinase receptorâ deficient mice. J. Clin. Invest. 97, 870 â 878.
dc.identifier.citedreferenceGyetko, M. R., Chen, G.â H., McDonald, R. A., Goodman, R., Huffnagle, G. B., Wilkinson, C. C., Fuller, J. A., Toews, G. B. ( 1996 ) Urokinase is required for the pulmonary inflammatory response to Cryptococcus neoformans: A murine transgenic model. J. Clin. Invest. 97, 1818 â 1826.
dc.identifier.citedreferenceKubo, H., Morgenstern, D., Quinlan, W. M., Ward, P. A., Dinauer, M. C., Doershuk, C. M. ( 1996 ) Preservation of complementâ induced lung injury in mice with deficiency of NADPH oxidase. J. Clin. Invest. 97, 2680 â 2684.
dc.identifier.citedreferenceTraynor, T. R., Kuziel, W. A., Toews, G. B., Huffnagle, G. B. ( 2000 ) CCR2 expression determines T1 versus T2 polarization during pulmonary Cryptococcus neoformans infection. J. Immunol. 164, 2021 â 2027.
dc.identifier.citedreferenceHattori, N., Sisson, T. H., Xu, Y., Simon, R. H. ( 1999 ) Adenovirusâ mediated transfer of urokinaseâ type plasminogen activator genes to lung cells in vitro and in vivo. Hum. Gene Ther. 10, 215 â 222.
dc.identifier.citedreferenceMayo, L. A., Curnutte, J. T. ( 1990 ) Kinetic microplate assay for superoxide production by neutrophils and other phagocytic cells. Methods Enzymol. 186, 567 â 575.
dc.identifier.citedreferenceHarlow, E., Lane, D. ( 1988 ) Antibodies: A Laboratory Manual; Cold Spring Harbor Laboratory, New York.
dc.identifier.citedreferenceSorensen, O., Borregaard, N. ( 1999 ) Methods for quantitation of human neutrophil proteins, a survey. J. Immunol. Methods 232, 179 â 190.
dc.identifier.citedreferenceCarr, R. ( 2000 ) Neutrophil productiona dn funciton in newborn infants. Br. J. Haematol. 110, 18 â 28.
dc.identifier.citedreferenceTodd, R. F. I., Arnaout, M. A., Rosin, R. E., Crowley, C. A., Peters, W. A. ( 1984 ) Subcellular localization of the large subunit of Mo1 (Mo1 alpha; formerly gp 110), a surface glycoprotein associated with neutrophil adhesion. J. Clin. Invest. 74, 1280 â 1290.
dc.identifier.citedreferenceTodd, R. F. I., Freyer, D. R. ( 1988 ) The CD11/CD18 leukocyte glycoprotein deficience. Hematol. Oncol. Clin. North Am. 2, 13 â 31.
dc.identifier.citedreferenceMay, A. E., Kanse, S. M., Lund, L. R., Gisler, R. H., Imhof, B. A., Preissner, K. T. ( 1998 ) Urokinase receptor (CD87) regulates leukocyte recruitment via β2 integrins in vivo. J. Exp. Med. 188, 1029 â 1037.
dc.identifier.citedreferenceWang, N., Planus, E., Pouchelet, M., Fredberg, J. J., Barlovatzâ Meimon, G. ( 1995 ) Urokinase receptor mediates mechanical force transfer across the cell surface. Am. J. Physiol. 268, C1062 â C1066.
dc.identifier.citedreferenceCao, D., Mizukami, I. F., Garniâ Wagner, B. A., Kindzelskii, A. L., Todd, R. F., III Boxer, L. A., Petty, H. R. ( 1995 ) Human urokinaseâ type plasminogen activator primes neutrophils for superoxide anion release. J. Immunol. 154, 1817 â 1829.
dc.identifier.citedreferencePlesner, T., Ploug, M., Ellis, V., Ronne, E., Høyerâ Hansen, G., Wittrup, M., Pedersen, T. L., Tscherning, T., Danø, K., Hansen, N. E. ( 1994 ) The receptor for urokinaseâ type plasminogen activator and urokinase is translocated from two distinct intracellular compartments to the plasma membrane on stimulation of human neutrophils. Blood 83, 808 â 815.
dc.identifier.citedreferencePedersen, T., Plesner, T., Horn, T., Hoyerâ Hansen, G., Sorensen, S., Hansen, N. E. ( 2000 ) Subcellular distribution of urokinase and urokinase receptor in human neutrophils determined by immunoelectron microscopy. Ultrastruct. Pathol. 24, 175 â 182.
dc.identifier.citedreferenceHolmes, B., Page, A. R., Good, R. A. ( 1967 ) Studies of the metabolic activity of leukocytes from patients with a genetic abnormality of phagocyte function. J. Clin. Invest. 49, 1422 â 1432.
dc.identifier.citedreferenceShepard, V. L. ( 1986 ) The role of the respiratory burst of phagocytes in host defense. Semin. Respir. Infect. 1, 99 â 106.
dc.identifier.citedreferenceSmith, C. D., Cox, C. C., Snyderman, R. ( 1986 ) Receptorâ coupled activation of phosphoinositideâ specific phospholipase C by an N protein. Science 232, 97 â 100.
dc.identifier.citedreferenceNishizuka, Y. ( 1984 ) The role of protein kinase C in cell surface signal transduction and tumor promotion. Nature 308, 693 â 698.
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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