Membrane-bound proteinase 3 and PAR2 mediate phagocytosis of non-opsonized bacteria in human neutrophils

Molecular Immunology

Volumn 48, Issue 15-16, 2011, Pages 1966-1974

  Kim, Yong C ^a   Shin, Ji E ^a   Lee, Sung H ^a,b   Chung, Woo Jae ^a,c   Lee, Yoon Sik ^a   Choi, Bong K ^a   Choi, Youngnim ^a  

^a Seoul National University   (South Korea)

^b Dankook University   (South Korea)

^c LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

Bacteria; Neutrophils; PAR2; Phagocytosis; PR3

Indexed keywords

GLYCOSYLPHOSPHATIDYLINOSITOL; MEMBRANE BOUND PROTEINASE 3; MYELOBLASTIN; OPSONIN; PROTEIN ANTIBODY; PROTEINASE ACTIVATED RECEPTOR 2; UNCLASSIFIED DRUG;

AFFINITY CHROMATOGRAPHY; ARTICLE; BINDING KINETICS; CALCIUM TRANSPORT; CELL MEMBRANE; CONTROLLED STUDY; ENZYME ACTIVITY; FUSOBACTERIUM NUCLEATUM; HUMAN; HUMAN CELL; INHIBITION KINETICS; MASS SPECTROMETRY; NEUTROPHIL; NONHUMAN; PHAGOCYTOSIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PORPHYROMONAS GINGIVALIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PSEUDOMONAS AERUGINOSA; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SIGNAL TRANSDUCTION; STREPTOCOCCUS SANGUINIS; WESTERN BLOTTING;

BLOTTING, WESTERN; CALCIUM SIGNALING; CELL SEPARATION; FLOW CYTOMETRY; HL-60 CELLS; HUMANS; MEMBRANE PROTEINS; MYELOBLASTIN; NEUTROPHIL ACTIVATION; NEUTROPHILS; PHAGOCYTOSIS; RECEPTOR, PAR-2; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; STREPTOCOCCUS SANGUIS;

STREPTOCOCCUS SANGUINIS;

EID: 80051951092     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2011.05.026     Document Type: Article

References (34)

1. Bréchard S., Tschirhart E.J. Regulation of superoxide production in neutrophils: role of calcium influx. J. Leukoc. Biol. 2008, 84:1223-1237.
2. Campbell E.J., Campbell M.A., Owen C.A. Bioactive proteinase 3 on the cell surface of human neutrophils: quantification, catalytic activity, and susceptibility to inhibition. J. Immunol. 2000, 165:3366-3374.
3. Carrassi A., Antibodyati S., Santarelli G., Vogel G. Periodontitis in a patient with chronic neutropenia. J. Periodontol. 1989, 60:352-357.
4. Cianciola U., Genco R.J., Patters M.R., McKenna J., Van-Oss C.J. Defective polymorphonuclear leukocyte function in a human periodontal disease. Nature 1977, 265:445-447.
5. Chen T., Bolland S., Chen I., Parker J., Pantelic M., Grunert F., Zimmerman W. The CGM1a (CEACAM3/CD66d)-mediated phagocytic pathway of Neisseria gonorrhoeae expressing opacity proteins is also the pathway to cell death. J. Biol. Chem. 2001, 276:17413-17419.
6. Csernok E., Ai M., Gross W.L., Wicklein D., Petersen A., Lindner B., Lamprecht P., Holle J.U., Hellmich B. Wegener autoantigen induces maturation of dendritic cells and licenses them for Th1 priming via the protease-activated receptor-2 pathway. Blood 2006, 107:4440-4448.
7. Delcourt-Debruyne E.M., Boutigny H.R., Hildebrand H.F. Features of severe periodontal disease in a teenager with Chédiak-Higashi syndrome. J. Periodontol. 2000, 71:816-824.
8. Déry O., Thoma M.S., Wong H., Grady E.F., Bunnett N.W. Trafficking of proteinase-activated receptor-2 and beta-arrestin-1 tagged with green fluorescent protein. beta-Arrestin-dependent endocytosis of a proteinase receptor. J. Biol. Chem. 1999, 274:18524-18535.
9. Dixon D.R., Bainbridge B.W., Darveau R.P. Modulation of the innate immune response within the periodontium. Periodontol. 2000 2004, 35:53-74.
10. Falk R.J., Terrell R.S., Charles L.A., Jennette J.C. Anti-neutrophil cytoplasmic autoantibodies induce neutrophils to degranulate and produce oxygen radicals in vitro. Proc. Natl. Acad. Sci. U.S.A. 1990, 87:4115-4119.
11. Fridlich R., David A., Aviram I. Membrane proteinase 3 and its interactions within microdomains of neutrophil membranes. J. Cell. Biochem. 2006, 99:117-125.
12. Inaloz H.S., Harman M., Akdeniz S., Inaloz S.S., Isik A.G. Atypical familial Papillon-Lefèvre syndrome. J. Eur. Acad. Dermatol. Venereol. 2001, 15:48-50.
13. Jensen O.N., Mortensen P., Vorm O., Mann M. Automation of matrix-assisted laser desorption/ionization mass spectrometry using fuzzy logic feedback control. Anal. Chem. 1997, 69:1706-1714.
14. Ji S., Hyun J., Park E., Lee B.L., Kim K.K., Choi Y. Susceptibility of various oral bacteria to antimicrobial peptides and phagocytosis by neutrophils. J. Periodontal. Res. 2007, 42:410-419.
15. Kettritz R., Jennette J.C., Falk R.J. Crosslinking of ANCA-antigens stimulates superoxide release by human neutrophils. J. Am. Soc. Nephrol. 1997, 8:386-394.
16. Kim Y.G., Lee C.S., Chung W.J., Kim E.M., Shin D.S., Rhim J.H., Lee Y.S., Kim B.G., Chung J. Screening of LPS-specific peptides from a phage display library using epoxy beads. Biochem. Biophys. Res. Commun. 2005, 329:312-317.
17. Klarenbach S.W., Chipiuk A., Nelson R.C., Hollenberg M.D., Murray A.G. Differential actions of PAR2 and PAR1 in stimulating human endothelial cell exocytosis and permeantibodyility: the role of Rho-GTPases. Circ. Res. 2003, 92:272-278.
18. Ludemann J., Utecht B., Gross W.L. Anti-neutrophil cytoplasm antibodies in Wegener's granulomatosis recognize an elastinolytic enzyme. J. Exp. Med. 1990, 171:357-362.
19. Moraes T.J., Martin R., Plumb J.D., Vachon E., Cameron C.M., Danesh A., Kelvin D.J., Ruf W., Downey G.P. Role of PAR2 in murine pulmonary pseudomonal infection. Am. J. Physiol. Lung. Cell. Mol. Physiol. 2008, 294:L368-L377.
20. Nishihara T., Koseki T. Microbial etiology of periodontitis. Periodontol. 2000 2004, 36:14-26.
21. Perez H.D., Kelly E., Elfman F., Armitage G., Winkler J. Defective polymorphonuclear leukocyte formyl peptide receptor(s) in juvenile periodontitis. J. Clin. Invest. 1991, 87:971-976.
22. Rantibodyer-Durlacher J.E., Epstein J.B., Rantibodyer J., van Dissel J.T., van Winkelhoff A.J., Guiot H.F., van der Velden U. Periodontal infection in cancer patients treated with high-dose chemotherapy. Support. Care Cancer 2002, 10:466-473.
23. Russell F.A., McDougall J.J. Proteinase activated receptor (PAR) involvement in mediating arthritis pain and inflammation. Inflamm. Res. 2009, 58:119-126.
24. Schmitter T., Agerer F., Peterson L., Munzner P., Hauck C.R. Granulocyte CEACAM3 is a phagocytic receptor of the innate immune system that mediates recognition and elimination of human-specific pathogens. J. Exp. Med. 2004, 199:35-46.
25. Seasholtz T.M., Majumdar M., Brown J.H. Rho as a mediator of G protein-coupled receptor signaling. Mol. Pharmacol. 1999, 55:949-956.
26. Shin J., Ji S., Choi Y. Antibodyility of oral bacteria to induce tissue-destructive molecules from human neutrophils. Oral Dis. 2008, 14:327-334.
27. Stuart L.M., Ezekowitz R.A. Phagocytosis: elegant complexity. Immunity 2005, 22:539-550.
28. Swanson J.A. Shaping cups into phagosomes and macropinosomes. Nat. Rev. Mol. Cell Biol. 2008, 9:639-649.
29. Tarlowe M.H., Kannan K.B., Itagaki K., Adams J.M., Livingston D.H., Hauser C.J. Inflammatory chemoreceptor cross-talk suppresses leukotriene B4 receptor 1-mediated neutrophil calcium mobilization and chemotaxis after trauma. J. Immunol. 2003, 171:2066-2073.
30. Uehara A., Sugawara Y., Sasano T., Takada H., Sugawara S. Proinflammatory cytokines induce proteinase 3 as membrane-bound and secretory forms in human oral epithelial cells and antibodies to proteinase 3 activate the cells through protease-activated receptor-2. J. Immunol. 2004, 173:4179-4189.
31. van Rossum A.P., Rarok A.A., Huitema M.G., Fassina G., Limburg P.C., Kallenberg C.G. Constitutive membrane expression of proteinase 3 (PR3) and neutrophil activation by anti-PR3 antibodies. J. Leukoc. Biol. 2004, 76:1162-1170.
32. von Vietinghoff S., Tunnemann G., Eulenberg C., Wellner M., Cardoso M.C., Luft F.C., Kettritz R. NB1 mediates surface expression of the ANCA antigen proteinase 3 on human neutrophils. Blood 2007, 109:4487-4493.
33. Vouret-Craviari V., Grall D., Van Obberghen-Schilling E. Modulation of Rho GTPase activity in endothelial cells by selective proteinase-activated receptor (PAR) agonists. J. Thromb. Haemost. 2003, 1:1103-1111.
34. Zimmer M., Medcalf R.L., Fink T.M., Mattmann C., Lichter P., Jenne D.E. Three human elastase-like genes coordinately expressed in the myelomonocyte lineage are organized as a single genetic locus on 19pter. Proc. Natl. Acad. Sci. U.S.A. 1992, 89:8215-8219.