Secretory leukocyte protease inhibitor: A macrophage product induced by and antagonistic to bacterial lipopolysaccharide

Cell

Volumn 88, Issue 3, 1997, Pages 417-426

  Jin, Fen Yu ^a   Nathan, Carl ^a   Radzioch, Danuta ^b   Ding, Aihao ^a  

^a WEILL CORNELL MEDICAL COLLEGE   (United States)

^b MCGILL UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIUM LIPOPOLYSACCHARIDE; GAMMA INTERFERON; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; SECRETORY LEUKOCYTE PROTEINASE INHIBITOR; SERINE PROTEINASE INHIBITOR; TUMOR NECROSIS FACTOR ALPHA;

ANIMAL CELL; ARTICLE; CELL LINE; CONTROLLED STUDY; GENETIC TRANSFECTION; GRAM NEGATIVE INFECTION; HOST RESISTANCE; MACROPHAGE; MOUSE; NEUTROPHIL; NONHUMAN; PHAGOCYTOSIS; PHENOTYPE; PRIORITY JOURNAL; PROTEINASE INHIBITION;

ANIMALIA; BACTERIA (MICROORGANISMS); NEGIBACTERIA;

EID: 0030941175     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81880-2     Document Type: Article

References (68)

1. Abbinante-Nissen, J.M., Simpson, L.G., and Leikauf, G.D. (1993). Neutrophil elastase increases secretory leukocyte protease inhibitor transcript levels in airway epithelial cells. Am. J. Physiol. 265, L286-L292.
2. Abbinante-Nissen, J.M., Simpson, L.G., and Leikauf, G.D. (1995). Corticosteroids increase secretory leukocyte protease inhibitor transcript levels in airway epithelial cells. Am. J. Physiol. 268, L601-L606.
3. Abe, T., Kobayashi, N., Yoshimura, K., Trapnell, B.C., Kim, H., Hubbard, R.C., Brewer, M.T., Thompson, R.C., and Crystal, R.G. (1991). Expression of the secretory leukoprotease inhibitor gene in epithelial cells. J. Clin. Invest. 87, 2207-2215.
4. Beeson, P.B. (1947). Tolerance to bacterial pyrogens. J. Exp. Med. 86, 29-44.
5. Beutler, B., Krochin, N., Milsark, I.W., Luedke, C., and Cerami, A. (1986a). Control of cachectin (tumor necrosis factor) synthesis: mechanisms of endotoxin resistance. Science 232, 977-980.
6. d (endotoxin resistance) phenotype. J. Exp. Med. 164, 1791-1796.
7. Blasi, E., Radzioch, D., Durum, S.K., and Varesio, L. (1987). A murine macrophage cell line, immortalized by v-raf and v-myc oncogenes, exhibits normal macrophage functions. Eur. J. Immunol. 17, 1491-1498.
8. Bogdan, C., Vodovotz, Y., and Nathan, C. (1991). Macrophage deactivation by interleukin 10. J. Exp. Med. 174, 1549-1555.
9. Bohm, B., Aigner, T., Kinne, R., and Burkhardt, H. (1992). The serine-protease inhibitor of cartilage matrix is not a chondrocytic gene product. Eur. J. Biochem. 207, 773-779.
10. Bone, R.C. (1991). The pathogenesis of sepsis. Ann. Intern. Med. 115, 457-469.
11. Brandtzaeg, P., Osnes, L., Ovstebo, R., Joo, G.B., Westvik, A.B., and Kierulf, P. (1996). Net inflammatory capacity of human septic shock plasma evaluated by a monocyte-based target cell assay: identification of interleukin-10 as a major functional deactivator of human monocytes. J. Exp. Med. 184, 51-60.
12. Costa, T.E., Franke, R.R., Sanchez, M., Misulovin, Z., and Nussenzweig, M.C. (1992). Functional reconstitution of an immunoglobulin antigen receptor in T cells. J. Exp. Med. 175, 1669-1676.
13. Coutinho, A., Gronowicz, E., and Sultzer, B.M. (1975). Genetic control of B-cell responses. I. Selective unresponsiveness to lipopolysaccharide. Scand. J. Immunol. 4, 139-143.
14. Cox, G., Grandino, L., Blasi, E., Radzioch, D., Mathieson, B.J., and Varesio, L. (1989) Heterogeneity of hematopoietic cells immortalized by v-myc/v-raf recombinant retrovirus infection of bone marrow or fetal liver. J. Natl. Cancer Inst. 81, 1492-1496.
15. Deng, G., Curriden, S.A., Wang, S., Rosenberg, S., and Loskutoff, D.J. (1996). Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release? J. Cell Biol. 134, 1563-1571.
16. De Water, R., Willems, L.N., Van Muijen, G.N., Franken, C., Fransen, J.A., Dijkman, J.H., and Kramps, J.A. (1986). Ultrastructural localization of bronchial antileukoprotease in central and peripheral human airways by a gold-labeling technique using monoclonal antibodies. Am. Rev. Respir. Dis. 133, 882-890.
17. Ding, A.H., and Nathan, C.F. (1987). Trace levels of bacterial lipopolysaccharide prevent interferon-gamma or tumor necrosis factor-alpha from enhancing mouse peritoneal macrophage respiratory burst capacity. J. Immunol. 139, 1971-1977.
18. Ding, A., Wright, S.D., and Nathan, C. (1987). Activation of mouse peritoneal macrophages by monoclonal antibodies to Mac-1 (complement receptor type 3). J. Exp. Med. 165, 733-749.
19. Ding, A., Nathan, C.F., Graycar, J., Derynck, R., Stuehr, D.J., and Srimal, S. (1990). Macrophage deactivating factor and transforming growth factors-beta 1, -beta2 and -beta 3 inhibit induction of macrophage nitrogen oxide synthesis by IFN-gamma. J. Immunol. 145, 940-944.
20. d) mice respond to bacterial lipopolysaccharide by activating NF-kappa B. J. Leukoc. Biol. 57, 174-179.
21. Drenth, J., Low, B.W., Richardson, J.S., and Wright, C.S. (1980). The toxin-agglutinin fold. A new group of small protein structures organized around a four-disulfide core. J. Biol. Chem. 255, 2652-2655.
22. Eisenberg, S.P., Hale, K.K., Heimdal, P., and Thompson, R.C. (1990). Location of the protease-inhibitory region of secretory leukocyte protease inhibitor. J. Biol. Chem. 265, 7976-7981.
23. Fink, E., Nettelbeck, R., and Fritz, H. (1986). Inhibition of mast cell chymase by eglin c and antileukoprotease (HUSI-I). Indications for potential biological functions of these inhibitors. Biol. Chem. Hoppe Seyler 367, 567-571.
24. Grutter, M.G., Fendrich, G., Huber, R., and Bode, W. (1988). The 2.5 A X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine alpha-chymotrypsin. EMBO J. 7, 345-351.
25. Heinzel, R., Appelhans, H., Gassen, G., Seemuller, U., Machleidt, W., Fritz, H., and Steffens, G. (1986). Molecular cloning and expression of cDNA for human antileukoprotease from cervix uterus. Eur. J. Biochem. 160, 61-67.
26. Helmig, R., Uldbjerg, N., and Ohlsson, K. (1995). Secretory leukocyte protease inhibitor in the cervical mucus and in the fetal membranes. Eur. J. Obstet. Gynecol. Reprod. Biol. 59, 95-101.
27. Hogan, M.M., and Vogel, S.N. (1988). Inhibition of macrophage tumoricidal activity by glucocorticoids. J. Immunol. 140, 513-519.
28. Hutchison, D.C. (1987). The role of proteases and antiproteases in bronchial secretions. Eur. J. Respir. Dis. Suppl. 153, 78-85.
29. Ingalls, R.R., and Golenbock, D.T. (1995). CD11c/CD18, a transmembrane signaling receptor for lipopolysaccharide. J. Exp. Med. 181, 1473-1479.
30. 2+ in human neutrophils and HUVEC cells. Biochem. Biophys. Res. Commun. 207, 324-330.
31. Kramps, J.A., Te Boekhorst, A.H., Fransen, J.A., Ginsel, L.A., and Dijkman, J.H. (1989). Antileukoprotease is associated with elastin fibers in the extracellular matrix of the human lung. An immunoelectron microscopic study. Am. Rev. Respir. Dis. 140, 471-476.
32. Ku, G.S., Quigley, J.P., and Sultzer, B.M. (1981). Time-dependent inhibition of tuberculin-induced lymphocyte DNA synthesis by a serine protease inhibitor. J. Immunol. 126, 2209-2214.
33. Kuus-Reichel, K., and Ulevitch, R.J. (1986). Partial restoration of the lipopolysaccharide-induced proliferative response in splenic B cells from C3H/HeJ mice. J. Immunol. 137, 472-477.
34. Lee, C.H., Igarashi, Y., Hohman, R.J., Kaulbach, H., White, M.V., and Kaliner, M.A. (1993). Distribution of secretory leukoprotease inhibitor in the human nasal airway. Am. Rev. Respir. Dis. 147, 710-716.
35. Liang, P., and Pardee, A.B. (1992). Differential display of eukaryotic messenger RNA by means of the polymerase chain reaction. Science 257, 967-971.
36. Liang, P., Averboukh, L., and Pardee, A.B. (1993). Distribution and cloning of eukaryotic mRNAs by means of differential display: refinements and optimization. Nucleic Acids Res. 21, 3269-3275.
37. Lucey, E.C., Stone, P.J., Ciccolella, D.E., Breuer, R., Christensen, T.G., Thompson, R.C., and Snider, G.L. (1990). Recombinant human secretory leukocyte-protease inhibitor: in vitro properties, and amelioration of human neutrophil elastase-induced emphysema and secretory cell metaplasia in the hamster. J. Lab. Clin. Med. 115, 224-232.
38. Maruyama, M., Hay, J.G., Yoshimura, K., Chu, C.S., and Crystal, R.G. (1994). Modulation of secretory leukoprotease inhibitor gene expression in human bronchial epithelial cells by phorbol ester. J. Clin. Invest. 94, 368-375.
39. McNeely, T.B., Dealy, M., Dripps, D.J., Orenstein, J.M., Eisenberg, S.P., and Wahl, S.M. (1995). Secretory leukocyte protease inhibitor: a human saliva protein exhibiting anti-human immunodeficiency virus 1 activity in vitro. J. Clin. Invest. 96, 456-464.
40. Nathan, C.F. (1987). Secretory products of macrophages. J. Clin. Invest. 79, 319-326.
41. Ohlsson, K., Bergenfeldt, M., and Bjork, P. (1988). Functional studies of human secretory leukocyte protease inhibitor. Adv. Exp. Med. Biol. 240, 123-131.
42. Ohlsson, K., Bjartell, A., and Lilja, H. (1995). Secretory leucocyte protease inhibitor in the male genital tract: PSA-induced proteolytic processing in human semen and tissue localization. J. Androl. 16, 64-74.
43. Parker, M.M., and Parrillo, J.E. (1983). Septic shock. Hemodynamics and pathogenesis. J. Am. Med. Assoc. 250, 3324-3327.
44. Pearse, R.N., Feinman, R., and Ravetch, J.V. (1991) Characterization of the promoter of the human gene encoding the high-affinity IgG receptor: transcriptional induction by γ-interferon is mediated through common DNA response elements. Proc. Natl. Acad. Sci. USA 88, 11305-11309.
45. Randow, F., Syrbe, U., Meisel, C., Krausch, D., Zuckermann, H., Platzer, C., and Volk, H.D. (1995). Mechanism of endotoxin desensitization: involvement of interleukin 10 and transforming growth factor beta. J. Exp. Med. 181, 1887-1892.
46. Rosenstreich, D.L., and Glode, L.M. (1975). Difference in B cell mitogen responsiveness between closely related strains of mice. J. Immunol. 115, 777-780.
47. Rudolphus, A., Stolk, J., Dijkman, J.H., and Kramps, J.A. (1993). Inhibition of lipopolysaccharide-induced pulmonary emphysema by intratracheally instilled recombinant secretory leukocyte proteinase inhibitor. Am. Rev. Respir. Dis. 147, 442-447.
48. Sallenave, J.M., Silva, A., Marsden, M.E., and Ryle, A.P. (1993). Secretion of mucus proteinase inhibitor and elafin by Clara cell and type II pneumocyte cell lines. Am. J. Respir. Cell Mol. Biol. 8, 126-133.
49. Sallenave, J.M., Shulmann, J., Crossley, J., Jordana, M., and Gauldie, J. (1994). Regulation of secretory leukocyte proteinase inhibitor (SLPI) and elastase-specific inhibitor (ESI/elafin) in human airway epithelial cells by cytokines and neutrophilic enzymes. Am. J. Respir. Cell Mol. Biol. 11, 733-741.
50. Seemuller, U., Arnhold, M., Fritz, H., Wiedenmann, K., Machleidt, W., Heinzel, R., Appelhans, H., Gassen, H.G., and Lottspeich, F. (1986). The acid-stable proteinase inhibitor of human mucous secretions (HUSI-I, antileukoprotease). Complete amino acid sequence as revealed by protein and cDNA sequencing and structural homology to whey proteins and Red Sea turtle proteinase inhibitor. FEBS Lett. 199, 43-48.
51. 3 binding to vitronectin. Nature 383, 441-443.
52. Stetler, G., Brewer, M.T., and Thompson, R.C. (1986). Isolation and sequence of a human gene encoding a potent inhibitor of leukocyte proteases. Nucleic Acids Res. 14, 7883-7896.
53. Stolk, J., Heinzel-Wieland, R., Saunders, D., Dijkman, J.H., and Steffens, G. (1993). Potency of an oxidation-resistant mutant of secretory leukocyte proteinase inhibitor in lipopolysaccharide-induced emphysema in hamsters. Pulm. Pharmacol. 6, 33-39.
54. Sultzer, B.M. (1968). Genetic control of leucocyte responses to endotoxin. Nature 219, 1253-1254.
55. Sultzer, B.M. (1976). Genetic analysis of lymphocyte activation by lipopolysaccharide Endotoxin. Infect. Immun. 13, 1579-1584.
56. Sultzer, B.M., Castagna, R., Bandekar, J., and Wong, P. (1993). Lipopolysaccharide nonresponder cells: the C3H/HeJ defect. Immunobiology 187, 257-271.
57. Sweet, M.J., and Hume, D.A. (1996). Endotoxin signal transduction in macrophages. J. Leukoc. Biol. 60, 8-26.
58. Tegner, H. (1978). Quantitation of human granulocyte protease inhibitors in non-purulent bronchial lavage fluid. Acta Otolaryngol. 85, 282-289.
59. Thompson, R.C., and Ohlsson, K. (1986). Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. Proc. Natl. Acad. Sci. USA 83, 6692-6696.
60. Tobias, P.S., Soldau, K., and Ulevitch, R.J. (1986). Isolation of a lipopolysaccharide-binding acute phase reactant from rabbit serum. J. Exp. Med. 164, 777-793.
61. Tomova, S., Cutruzzola, F., Barra, D., Amiconi, G., Ascenzi, P., Carugo, K.D., Menegatti, E., Sarti, P., Schnebli, H.P., and Bolognesi, M. (1994). Selective oxidation of methionyl residues in the human recombinant secretory leukocyte proteinase inhibitor. Effect on the inhibitor binding properties. J. Mol. Recognit. 7, 31-37.
62. Ulevitch, R.J., and Tobias, P.S. (1995). Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin. Annu. Rev. Immunol. 13, 437-457.
63. Watson, J., Kelly, K., Largen, M., and Taylor, B.A. (1978). The genetic mapping of a defective LPS response gene in C3H/HeJ mice. J. Immunol. 120, 422-424.
64. Wright, S.D., and Jong, M.T. (1986). Adhesion-promoting receptors on human macrophages recognize Escherichia coli by binding to lipopolysaccharide. J. Exp. Med. 164, 1876-1888.
65. Wright, S.D., Ramos, R.A., Tobias, P.S., Ulevitch, R.J., and Mathison, J.C. (1990). CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding protein. Science 249, 1431-1433.
66. Xie, Q.W., Cho, H.J., Calaycay, J., Mumford, R.A., Swiderek, K.M., Lee, T.D., Ding, A., Troso, T., and Nathan, C. (1992). Cloning and characterization of inducible nitric oxide synthase from mouse macrophages. Science 256, 225-228.
67. Xie, Q.W., Kashiwabara, Y., and Nathan, C. (1994). Role of transcription factor NF-kappa B/Rel in induction of nitric oxide synthase. J. Biol. Chem. 269, 4705-4708.
68. Yurochko, A.D., Liu, D.Y., Eierman, D., and Haskill, S. (1992). Integrins as a primary signal transduction molecule regulating monocyte immediate-early gene induction. Proc. Natl. Acad. Sci. USA 89, 9034-9038.