Key points are not available for this paper at this time.
Human neutrophil-specific CD177 (NB1 and PRV-1) has been reported to be up-regulated in a number of inflammatory settings, including bacterial infection and granulocyte-colony-stimulating factor application. Little is known about its function. By flow cytometry and immunoprecipitation studies, we identified platelet endothelial cell adhesion molecule-1 (PECAM-1) as a binding partner of CD177. Real-time protein-protein analysis using surface plasmon resonance confirmed a cation-dependent, specific interaction between CD177 and the heterophilic domains of PECAM-1. Monoclonal antibodies against CD177 and against PECAM-1 domain 6 inhibited adhesion of U937 cells stably expressing CD177 to immobilized PECAM-1. Transendothelial migration of human neutrophils was also inhibited by these antibodies. Our findings provide direct evidence that neutrophil-specific CD177 is a heterophilic binding partner of PECAM-1. This interaction may constitute a new pathway that participates in neutrophil transmigration. Human neutrophil-specific CD177 (NB1 and PRV-1) has been reported to be up-regulated in a number of inflammatory settings, including bacterial infection and granulocyte-colony-stimulating factor application. Little is known about its function. By flow cytometry and immunoprecipitation studies, we identified platelet endothelial cell adhesion molecule-1 (PECAM-1) as a binding partner of CD177. Real-time protein-protein analysis using surface plasmon resonance confirmed a cation-dependent, specific interaction between CD177 and the heterophilic domains of PECAM-1. Monoclonal antibodies against CD177 and against PECAM-1 domain 6 inhibited adhesion of U937 cells stably expressing CD177 to immobilized PECAM-1. Transendothelial migration of human neutrophils was also inhibited by these antibodies. Our findings provide direct evidence that neutrophil-specific CD177 is a heterophilic binding partner of PECAM-1. This interaction may constitute a new pathway that participates in neutrophil transmigration. CD177 (NB1 and PRV-1) is a 58- to 64-kDa glycosylphosphatidylinositol-anchored glycoprotein expressed exclusively by neutrophils, neutrophilic metamyelocytes, and myelocytes, but not by any other blood cells (1Stroncek D.F. Skubitz K.M. McCullough J.J. Blood. 1990; 75: 744-755Crossref PubMed Google Scholar, 2Stroncek D.F. Shankar R.A. Noren P.A. Herr G.P. Clement L.T. Transfusion. 1996; 36: 168-174Crossref PubMed Scopus (39) Google Scholar). We and others elucidated its primary structure by sequencing the NB1 and PRV-1 genes, which later turned out to be two alleles of a single CD177 gene (3Kissel K. Santoso S. Hofmann C. Stroncek D. Bux J. Eur. J. Immunol. 2001; 31: 1301-1309Crossref PubMed Scopus (75) Google Scholar, 4Temerinac S. Klippel S. Strunck E. Roder S. Lubbert M. Lange W. Azemar M. Meinhardt G. Schaefer H.E. Pahl H.L. Blood. 2000; 95: 2569-2576Crossref PubMed Google Scholar, 5Caruccio L. Bettinotti M. rector-Myska A.E. Arthur D.C. Stroncek D. Transfusion. 2006; 46: 441-447Crossref PubMed Scopus (30) Google Scholar). The surface expression of CD177 is unique in that only a subpopulation of neutrophils expresses this protein on the cell surface, with the mean size of the CD177-positive subpopulation ranging from 45% to 65% (2Stroncek D.F. Shankar R.A. Noren P.A. Herr G.P. Clement L.T. Transfusion. 1996; 36: 168-174Crossref PubMed Scopus (39) Google Scholar, 6Matsuo K. Lin A. Procter J.L. Clement L. Stroncek D. Transfusion. 2000; 40: 654-662Crossref PubMed Scopus (63) Google Scholar). CD177 has been well studied as a target antigen in immunemediated disorders. During pregnancy, women with a CD177 null phenotype are prone to produce alloantibodies against CD177 that cross the placenta, react with fetal neutrophils, and cause neutropenia of the newborn. This mechanism let to the initial discovery of the NB1 antigen in 1971 (7Lalezari P. Murphy G.B. Allen Jr., F.H. J. Clin. Invest. 1971; 50: 1108-1115Crossref PubMed Scopus (116) Google Scholar). Alloantibodies to CD177, present in blood products obtained from immunized donors, have also been implicated as mediators of transfusion-related acute lung injury (8Sachs U.J. Hattar K. Weissmann N. Bohle R.M. Weiss T. Sibelius U. Bux J. Blood. 2006; 107: 1217-1219Crossref PubMed Scopus (133) Google Scholar). Although well characterized as an immunotarget, the function of CD177 is largely unknown. It has been reported that CD177 is up-regulated on the neutrophil surface upon stimulation, including during severe bacterial infections, and following granulocyte-colony-stimulating factor treatment (9Gohring K. Wolff J. Doppl W. Schmidt K.L. Fenchel K. Pralle H. Sibelius U. Bux J. Br. J. Haematol. 2004; 126: 252-254Crossref PubMed Scopus (58) Google Scholar). In addition, antibody-mediated clustering of CD177 primes the N-formyl-methionyl-leucyl-phenylalanine (fMLP) 3The abbreviations used are: fMLP, N-formyl-methionyl-leucyl-phenylalanine; HUVEC, human umbilical vein endothelial cell; mAb, monoclonal antibody; sr, soluble recombinant; SPR, surface plasmon resonance; IL, interleukin; BCECF, 2′,7′-bis-(2-carboxyethyl)-5-(and-6-)carboxyfluorescein; JAM, junctional adhesion molecule; PECAM-1, platelet endothelial cell adhesion molecule-1; PBS, phosphate-buffered saline; BSA, bovine serum albumin. 3The abbreviations used are: fMLP, N-formyl-methionyl-leucyl-phenylalanine; HUVEC, human umbilical vein endothelial cell; mAb, monoclonal antibody; sr, soluble recombinant; SPR, surface plasmon resonance; IL, interleukin; BCECF, 2′,7′-bis-(2-carboxyethyl)-5-(and-6-)carboxyfluorescein; JAM, junctional adhesion molecule; PECAM-1, platelet endothelial cell adhesion molecule-1; PBS, phosphate-buffered saline; BSA, bovine serum albumin.-activated respiratory burst reaction of the neutrophil (8Sachs U.J. Hattar K. Weissmann N. Bohle R.M. Weiss T. Sibelius U. Bux J. Blood. 2006; 107: 1217-1219Crossref PubMed Scopus (133) Google Scholar). Taken together, these observations make it reasonable to suppose that CD177 may be involved in processes of neutrophil-mediated host defense. One preliminary study suggests a participation of CD177 in neutrophil-endothelial cell interaction (10Stroncek D.F. Herr G.P. Plachta L.B. J. Lab. Clin. Med. 1994; 123: 247-255PubMed Google Scholar). The latter observation is in line with the fact that CD177, as a member of the leukocyte antigen-6 superfamily, shares a similar structure with the urokinase plasminogen activator receptor (11Plesner T. Behrendt N. Ploug M. Stem Cells. 1997; 15: 398-408Crossref PubMed Scopus (145) Google Scholar). Urokinase plasminogen activator receptor is expressed on numerous cell types and plays an important role in cell-extra-cellular matrix and cell-cell interaction by binding of vitronectin, and by regulating β1 and β2 integrin-dependent adhesion of leukocytes (12Chavakis T. Kanse S.M. May A.E. Preissner K.T. Biochem. Soc. Trans. 2002; 30: 168-173Crossref PubMed Google Scholar). Our understanding of the role that CD177 might similarly play in mediating neutrophil-endothelial cell interactions is limited, however, by lack of an identifiable counter-receptor on the endothelial cell surface. A complex molecular crosstalk is known to be responsible for the interaction between neutrophils and endothelial cells (13McIntyre T.M. Prescott S.M. Weyrich A.S. Zimmerman G.A. Curr. Opin. Hematol. 2003; 10: 150-158Crossref PubMed Scopus (139) Google Scholar, 14Kakkar A.K. Lefer D.J. Curr. Opin. Pharmacol. 2004; 4: 154-158Crossref PubMed Scopus (82) Google Scholar). Whereas the initiating step of rolling and subsequent firm leukocyte adhesion have been well characterized (15McEver R.P. Thromb. Haemost. 2001; 86: 746-756Crossref PubMed Scopus (360) Google Scholar), less is known about the mechanisms that mediate the migration of leukocytes through the endothelium. A number of adhesion molecules have been implicated in this process, including β2 integrins, ICAM-1 (intercellular adhesion molecule-1), junctional adhesion molecules (JAMs), CD99, and platelet endothelial cell adhesion molecule-1 (PECAM-1) (16Muller W.A. Trends Immunol. 2003; 24: 327-334PubMed Scopus (0) Google Scholar, 17Shaw S.K. Ma S. Kim M.B. Rao R.M. Hartman C.U. Froio R.M. Yang L. Jones T. Liu Y. Nusrat A. Parkos C.A. Luscinskas F.W. J. Exp. Med. 2004; 200: 1571-1580Crossref PubMed Scopus (189) Google Scholar). PECAM-1 is a constitutively expressed, abundant component of endothelial cell junctions at all levels of the vascular tree (18Muller W.A. Ratti C.M. McDonnell S.L. Cohn Z.A. J. Exp. Med. 1989; 170: 399-414Crossref PubMed Scopus (289) Google Scholar, 19Albelda S.M. Oliver P.D. Romer L.H. Buck C.A. J. Cell Biol. 1990; 110: 1227-1237Crossref PubMed Scopus (330) Google Scholar). Homophilic PECAM-1-PECAM-1 interaction as part of a sensing and activating process of neutrophils plays a central role in leukocyte migration (20Dangerfield J. Larbi K.Y. Huang M.T. Dewar A. Nourshargh S. J. Exp. Med. 2002; 196: 1201-1211Crossref PubMed Scopus (180) Google Scholar). In addition, a number of heterophilic binding partners for PECAM-1 have been described, including CD38, αvβ3, and glycosaminoglycans (21Deaglio S. Morra M. Mallone R. Ausiello C.M. Prager E. Garbarino G. Dianzani U. Stockinger H. Malavasi F. J. Immunol. 1998; 160: 395-402PubMed Google Scholar, 22Piali L. Hammel P. Uherek C. Bachmann F. Gisler R.H. Dunon D. Imhof B.A. J. Cell Biol. 1995; 130: 451-460Crossref PubMed Scopus (340) Google Scholar, 23DeLisser H.M. Yan H.C. Newman P.J. Muller W.A. Buck C.A. Albelda S.M. J. Biol. Chem. 1993; 268: 16037-16046Abstract Full Text PDF PubMed Google Scholar), but the relevance of these partners in leukocyte transmigration is currently not well established (24Sun Q.H. Paddock C. Visentin G.P. Zukowski M.M. Muller W.A. Newman P.J. J. Biol. Chem. 1998; 273: 11483-11490Abstract Full Text Full Text PDF PubMed Scopus (25) Google Scholar, 25Sun Q.H. DeLisser H.M. Zukowski M.M. Paddock C. Albelda S.M. Newman P.J. J. Biol. Chem. 1996; 271: 11090-11098Abstract Full Text Full Text PDF PubMed Scopus (156) Google Scholar, 26Thompson R.D. Wakelin M.W. Larbi K.Y. Dewar A. Asimakopoulos G. Horton M.A. Nakada M.T. Nourshargh S. J. Immunol. 2000; 165: 426-434Crossref PubMed Scopus (75) Google Scholar, 27Luu N.T. Rainger G.E. Buckley C.D. Nash G.B. J. Vasc. Res. 2003; 40: 467-479Crossref PubMed Scopus (40) Google Scholar). In this study, we demonstrate that neutrophil-specific CD177 can directly bind PECAM-1 and that CD177 and PECAM-1 constitute a heterophilic ligand pair with contribution to neutrophil-endothelial cell interactions. Cells—U937 cells obtained from and in and cell from and in Cell with fetal serum and Cell Human umbilical vein endothelial cells from umbilical and as T. T. R. K. U.J. Preissner K.T. Santoso S. J. Biol. Chem. 2004; Full Text Full Text PDF PubMed Scopus Google Scholar). in with Cell Monoclonal against CD177 was by D. Stroncek of specific for CD177 was from against the two domains of PECAM-1 was and characterized in H. Q.H. Santoso S. Blood. 2000; PubMed Google Scholar). and domains and 6 of PECAM-1, have been (24Sun Q.H. Paddock C. Visentin G.P. Zukowski M.M. Muller W.A. Newman P.J. J. Biol. Chem. 1998; 273: 11483-11490Abstract Full Text Full Text PDF PubMed Scopus (25) Google Scholar, H.C. DeLisser H.M. Romer L. Albelda S.M. Cell 1995; PubMed Scopus Google Scholar). and against and from specific for was in S. U.J. H. M. A. Preissner K.T. T. J. Exp. Med. 2002; 196: PubMed Scopus Google Scholar). antibodies are of for PECAM-1 from cells has been A. Oliver Paddock C. Yan H.C. DeLisser H.M. Albelda S.M. Newman P.J. J. Biol. Chem. 1994; Full Text PDF PubMed Google Scholar). by protein as was from of CD177 (3Kissel K. Santoso S. Hofmann C. Stroncek D. Bux J. Eur. J. Immunol. 2001; 31: 1301-1309Crossref PubMed Scopus (75) Google was by using and of of CD177 with of of in a of was for of for at for at and for at In the the was at a of for and to The was from a by using the of by and by using CD177 and as A from was by analysis on an of cells in and with of CD177 in of by the of cells with of Cell from cell by In with of at with PBS, with in for at of of was and the was for at and protein was with of and as was with of and was on an at protein was from of and by the of a protein protein was on by and by of to by of with for and with cells with of for at with in and with of cells in of for flow cytometry analysis with of at with and with for at of of protein and the was for at and with of endothelial cell for at protein was by the of against PECAM-1, and at for of was for at antibodies on an as of the CD177 with of and in of as S. U.J. A. H. Blood. 2002; PubMed Scopus Google Scholar). with cell at of of with of protein for at of cell to the and at with immunoprecipitation by for at on and with and a with the was with against endothelial cell with and the of CD177 in U937 Cell cells in fetal serum and of of cell was with of CD177 in (3Kissel K. Santoso S. Hofmann C. Stroncek D. Bux J. Eur. J. Immunol. 2001; 31: 1301-1309Crossref PubMed Scopus (75) Google using for on cells in of The cells and for expression by the of expressing CD177 identified by flow cytometry analysis using as of for CD177 expression by flow cytometry as (9Gohring K. Wolff J. Doppl W. Schmidt K.L. Fenchel K. Pralle H. Sibelius U. Bux J. Br. J. Haematol. 2004; 126: 252-254Crossref PubMed Scopus (58) Google Scholar). from blood by and was by flow cytometry using cells The size of the subpopulation was from the the of on protein surface as and with for at cells for at in the of was as using and of CD177 from Human obtained from by a U.J. A. T. G. W. Transfusion. 2006; 46: PubMed Scopus Google Scholar). to all of human granulocyte-colony-stimulating factor as by the in of and for at Cell of for on to cells in of of of for Cell for at at and for by as (3Kissel K. Santoso S. Hofmann C. Stroncek D. Bux J. Eur. J. Immunol. 2001; 31: 1301-1309Crossref PubMed Scopus (75) Google Scholar). CD177 protein was against PBS, and the of was by through protein as a was from platelet by The and of was by and and protein was by of at protein interaction between PECAM-1 and CD177 was in with a surface plasmon resonance on a in to a of was directly immobilized on a as by the of of CD177 as at a flow of at as In CD177 to studies, of was in was The was with Cell adhesion to was as T. Kanse S.M. F. W. R.A. Preissner K.T. Blood. 2000; PubMed Google Scholar). with of as in and with U937 cells with of The for in the in and the at for studies, cells with specific for CD177 and PECAM-1 and with of CD177 during the adhesion the the and adhesion was using a transmigration using with an size with on to the and for in a and The of was the of the transmigration in the with the was with of neutrophils was with of as of of cells cells with was to the on of the endothelial for at the number of cells in the was using a as and of the binding partner of CD177, we established stably cells soluble of and by the of a protein The protein was by to its and by to the of CD177 and the with specific for CD177, as well as with and In the not any reaction demonstrate that CD177 and of protein are of to of the protein with was by flow cytometry with as a and a specific reaction with only was that endothelial cells a binding partner for CD177. the binding partner of CD177, an antigen was using protein immobilized on protein was with against endothelial in a reaction was with reaction was with against and against that PECAM-1 may the binding partner of CD177. was with surface to this cell with and to protein by using a In to with and a specific with a of The was and with against endothelial cell to the specific for PECAM-1 was a was In reaction was with against and In the of with the specific reaction of not Real-time of CD177 and PECAM-1 study the direct protein-protein interaction between CD177 and soluble PECAM-1 a analysis by was and by and was immobilized the surface, and the binding of CD177 at was in binding of CD177 to immobilized PECAM-1 was In the interaction between CD177 and immobilized was to the the and of CD177 binding was and the of the binding of PECAM-1, against domains and was in the which was to with the PECAM-1 binding T. T. R. K. U.J. Preissner K.T. Santoso S. J. Biol. Chem. 2004; Full Text Full Text PDF PubMed Scopus Google Scholar), to immobilized PECAM-1 on the analysis of immobilized PECAM-1 and CD177 by on a the of in for and of CD177. was directly immobilized on a with a flow of at The the binding of against PECAM-1 in two and analysis of heterophilic interaction in the of and and of a CD177 in as of heterophilic binding by CD177 was in the of against CD177 and for at as heterophilic interaction has been reported to be on W.A. Newman P.J. DeLisser H.M. Albelda S.M. J. Exp. Med. PubMed Scopus (139) Google and binding have been to domain 6 of PECAM-1 M.T. Newman P.J. 1997; 36: PubMed Scopus Google Scholar), we the binding between CD177 and PECAM-1 might be by the of in of the binding of CD177 to PECAM-1 In the the of which the binding of urokinase plasminogen activator receptor to and T. May A.E. Preissner K.T. Kanse S.M. Blood. PubMed Google Scholar), not have any on interaction In the of the interaction between PECAM-1 and CD177 was the of for the heterophilic to the of heterophilic with and in to the interaction to specific for the a to this binding that and bind on CD177 demonstrate that CD177 can directly and with PECAM-1. between CD177 and PECAM-1 Cell the heterophilic interaction of CD177 with PECAM-1 to mediate cell we cells expressing CD177. by flow cytometry that CD177 CD177 of PECAM-1 expression was in In U937 cells PECAM-1, but not CD177, on surface. This observation was confirmed by the adhesion of U937 cells and and U937 cells and be cells an in which to study interactions of PECAM-1, and heterophilic interactions between PECAM-1 and CD177, study cell we and U937 cells to to immobilized in cell types to immobilized PECAM-1. The adhesion of U937 cells to immobilized PECAM-1 be inhibited by against the domain of PECAM-1, which with the interaction of PECAM-1, but not by and specific for the and domains of PECAM-1, CD177 with the adhesion of U937 The was U937 cells The adhesion of these cells and to PECAM-1 was inhibited by CD177, as well as by but not by in the adhesion of U937 cells to immobilized by β2 and by β1 not not that the of CD177 on U937 cells adhesion to PECAM-1. that the interaction between CD177 and the heterophilic domains of PECAM-1 can in interactions between neutrophils and endothelial The of CD177 in demonstrate the participation of CD177 in neutrophil we the of two important and on CD177 surface of neutrophils for with the surface expression of CD177 as by mean to In PECAM-1 surface expression was in the of to obtained with which the surface expression of CD177 by to and PECAM-1 surface expression to from a we the migration of neutrophils through endothelial cells the and of neutrophil migration was with specific for CD177 and against the domain of PECAM-1. In was to with neutrophil transmigration A monoclonal against the domain of PECAM-1 which is known to with the migration of neutrophil transmigration heterophilic interaction with PECAM-1 and can be in the of against CD177 against a heterophilic domain of PECAM-1. this heterophilic interaction is involved in to the CD177-positive and neutrophils in we the size of neutrophil subpopulation of transmigration by neutrophils that and which in the of the transmigration Whereas to transmigration of all neutrophils CD177-positive and the of CD177-positive neutrophils to of the of cells that not In the of CD177-positive neutrophils which through the was of all cells CD177-positive neutrophils to Taken together, that the heterophilic interaction between CD177 and PECAM-1 participates in migration of and the of neutrophils to of infection by a process that a number of surface molecules on the and the CD177 is a surface glycoprotein that up-regulated during bacterial (9Gohring K. Wolff J. Doppl W. Schmidt K.L. Fenchel K. Pralle H. Sibelius U. Bux J. Br. J. Haematol. 2004; 126: 252-254Crossref PubMed Scopus (58) Google Scholar). In the present study we CD177 participates in neutrophil we demonstrate heterophilic binding between neutrophil-specific CD177 and PECAM-1 that to interactions between neutrophils and endothelial cells in the of inflammatory cell a protein was to bind to endothelial that the endothelial partner for was a protein of which was identified as PECAM-1. In SPR, the CD177 protein to PECAM-1 in a with a of This heterophilic interaction was on and be by against CD177. In to the interaction of PECAM-1, which is on domains and of the the heterophilic CD177 interaction was to be by domain 6 also domain of PECAM-1. It has been established that PECAM-1 can mediate cell adhesion L. Hammel P. Uherek C. Bachmann F. Gisler R.H. Dunon D. Imhof B.A. J. Cell Biol. 1995; 130: 451-460Crossref PubMed Scopus (340) Google Scholar, 23DeLisser H.M. Yan H.C. Newman P.J. 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Res. 2003; 40: 467-479Crossref PubMed Scopus (40) Google Scholar). In CD177 is expressed on neutrophils, and of CD177 and the heterophilic domains of PECAM-1 with the transmigration of human The pathway a new adhesion pathway that leukocyte transmigration. neutrophils be to this a subpopulation of 45% to 65% of all Our that this at in to and the relevance of the transmigration pathway in is not by the present study and It has been that neutrophils as an unique surface as a subpopulation with in S. M. L. M. H. T. J. Biol. PubMed Scopus Google Scholar). a specific of neutrophil CD177 has been during bacterial infections, upon treatment with granulocyte-colony-stimulating and during as well as in (9Gohring K. Wolff J. Doppl W. Schmidt K.L. Fenchel K. Pralle H. Sibelius U. Bux J. Br. J. Haematol. 2004; 126: 252-254Crossref PubMed Scopus (58) Google Scholar, K. M. Bux J. Transfusion. 2006; 46: PubMed Scopus Google Scholar, L. Bettinotti M. K. Stroncek D. Transfusion. 2003; PubMed Scopus Google Scholar). This that the pathway be In the findings of the present study provide evidence that neutrophil-specific CD177 is a heterophilic binding partner of PECAM-1. This interaction leukocyte transmigration for a subpopulation of it a new to understanding of cell in host defense. The of and Hofmann is We for for In addition, we Bux and for
Sachs et al. (Wed,) studied this question.