메뉴 건너뛰기




Volumn 272, Issue 3 16-3, 1997, Pages

Cytokines regulate membrane-bound leukocyte elastase on neutrophils: A novel mechanism for effector activity

Author keywords

interleukin 8; N formyl leucyl methionyl phenylalanine; platelet activating factor; tumor necrosis factor

Indexed keywords

CYTOKINE; FORMYLMETHIONYLLEUCYLPHENYLALANINE; INTERLEUKIN 8; LEUKOCYTE ELASTASE; THROMBOCYTE ACTIVATING FACTOR; TUMOR NECROSIS FACTOR ALPHA;

EID: 0030948848     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1997.272.3.l385     Document Type: Article
Times cited : (110)

References (36)
  • 1
    • 0001862846 scopus 로고
    • Interleukin-8 and related chemotactic cytokines
    • edited by J. I. Gallin, I. M. Goldstein, and R. Snyderman. New York: Raven
    • Baggiolini, M., B. Dewald, and A. Walz. Interleukin-8 and related chemotactic cytokines. In: Inflammation. Basic Principles and Clinical Correlates, edited by J. I. Gallin, I. M. Goldstein, and R. Snyderman. New York: Raven, 1992, p. 247-263.
    • (1992) Inflammation. Basic Principles and Clinical Correlates , pp. 247-263
    • Baggiolini, M.1    Dewald, B.2    Walz, A.3
  • 2
    • 0026524163 scopus 로고
    • Priming of human neutrophil functions by tumor necrosis factor: Enhancement of superoxide anion generation, degranulation, and chemotaxis to chemoattractants C5a and f-met-leu-phe
    • Bajaj, M. S., R. R. Kew, R. O. Webster, and T. M. Hyers. Priming of human neutrophil functions by tumor necrosis factor: enhancement of superoxide anion generation, degranulation, and chemotaxis to chemoattractants C5a and f-met-leu-phe. Inflammation 16: 241-250, 1992.
    • (1992) Inflammation , vol.16 , pp. 241-250
    • Bajaj, M.S.1    Kew, R.R.2    Webster, R.O.3    Hyers, T.M.4
  • 3
    • 0023886316 scopus 로고
    • 1-proteinase inhibitor is a neutrophil chemoattractant after proteolytic inactivation by macrophage elastase
    • 1-proteinase inhibitor is a neutrophil chemoattractant after proteolytic inactivation by macrophage elastase. J. Biol. Chem. 263: 4481-4484, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4481-4484
    • Banda, M.J.1    Rice, A.G.2    Griffin, G.L.3    Senior, R.M.4
  • 4
    • 0028521143 scopus 로고
    • Comparison of properties of membrane bound versus soluble forms of human leukocyte elastase and cathepsin G
    • Bangalore, N., and J. Travis. Comparison of properties of membrane bound versus soluble forms of human leukocyte elastase and cathepsin G. Biol. Chem. Hoppe-Seyler 375: 659-666, 1994.
    • (1994) Biol. Chem. Hoppe-Seyler , vol.375 , pp. 659-666
    • Bangalore, N.1    Travis, J.2
  • 6
    • 0027686133 scopus 로고
    • Release of interleukin-8, interleukin-6, and colony-stimulating factors by upper airway epithelial cells: Implications for cystic fibrosis
    • Bedard, M., C. D. McClure, N. L. Schiller, C. Francoeur, A. Cantin, and M. Denis. Release of interleukin-8, interleukin-6, and colony-stimulating factors by upper airway epithelial cells: implications for cystic fibrosis. Am. J. Respir. Cell Mol. Biol. 9: 455-462, 1993.
    • (1993) Am. J. Respir. Cell Mol. Biol. , vol.9 , pp. 455-462
    • Bedard, M.1    McClure, C.D.2    Schiller, N.L.3    Francoeur, C.4    Cantin, A.5    Denis, M.6
  • 7
    • 0002016013 scopus 로고
    • Elastases: Catalytic and biological properties
    • edited by R. P. Mecham. Orlando, FL: Academic
    • Bieth, J. G. Elastases: catalytic and biological properties. In: Biology of Extracellular Matrix: Regulation of Matrix Accumulation, edited by R. P. Mecham. Orlando, FL: Academic, 1986, p. 217-320.
    • (1986) Biology of Extracellular Matrix: Regulation of Matrix Accumulation , pp. 217-320
    • Bieth, J.G.1
  • 8
    • 0014385564 scopus 로고
    • Isolation of mononuclear cells and granulocytes from human blood: Isolation of mononuclear cells by one centrifugation and of granulocytes by combining centrifugation and sedimentation at 1 g
    • Boyum, A. Isolation of mononuclear cells and granulocytes from human blood: isolation of mononuclear cells by one centrifugation and of granulocytes by combining centrifugation and sedimentation at 1 g. Scand. J. Clin. Lab. Invest. 21, Suppl. 97: 77-89, 1963.
    • (1963) Scand. J. Clin. Lab. Invest. , vol.21 , Issue.97 SUPPL. , pp. 77-89
    • Boyum, A.1
  • 9
    • 0028586814 scopus 로고
    • Involvement of a serine protease in the synthesis of platelet-activating factor by endothelial cells stimulated by tumor necrosis factor-α or interleukin-1α
    • Bussolino, F., M. Arese, L. Silvestro, R. Soldi, E. Benfenati, F. Sanavio, M. Aglietta, A. Bosia, and G. Camussi. Involvement of a serine protease in the synthesis of platelet-activating factor by endothelial cells stimulated by tumor necrosis factor-α or interleukin-1α. Eur. Respir. J. 24: 3131-3139, 1994.
    • (1994) Eur. Respir. J. , vol.24 , pp. 3131-3139
    • Bussolino, F.1    Arese, M.2    Silvestro, L.3    Soldi, R.4    Benfenati, E.5    Sanavio, F.6    Aglietta, M.7    Bosia, A.8    Camussi, G.9
  • 10
    • 0023840318 scopus 로고
    • Pericellular proteolysis by neutrophils in the presence of proteinase inhibitors: Effects of substrate opsonization
    • Campbell, E. J., and M. A. Campbell. Pericellular proteolysis by neutrophils in the presence of proteinase inhibitors: effects of substrate opsonization. J. Cell Biol. 106: 667-676, 1988.
    • (1988) J. Cell Biol. , vol.106 , pp. 667-676
    • Campbell, E.J.1    Campbell, M.A.2
  • 11
    • 0024430531 scopus 로고
    • Elastase and cathepsin G of human monocytes. Quantification of cellular content, release in response to stimuli, and heterogeneity in elastase-mediated proteolytic activity
    • Campbell, E. J., E. K. Silverman, and M. A. Campbell. Elastase and cathepsin G of human monocytes. Quantification of cellular content, release in response to stimuli, and heterogeneity in elastase-mediated proteolytic activity. J. Immunol. 143: 2961-2968, 1989.
    • (1989) J. Immunol. , vol.143 , pp. 2961-2968
    • Campbell, E.J.1    Silverman, E.K.2    Campbell, M.A.3
  • 12
    • 0002032398 scopus 로고
    • Role of interleukin-1 and tumor necrosis factor in systemic responses to infection and inflammation
    • edited by J. I. Gallin, I. M. Goldstein, and R. Snyderman. New York: Raven
    • Dinarello, C. A. Role of interleukin-1 and tumor necrosis factor in systemic responses to infection and inflammation. In: Inflammation: Basic Principles and Clinical Correlates, edited by J. I. Gallin, I. M. Goldstein, and R. Snyderman. New York: Raven, 1992, p. 211-232.
    • (1992) Inflammation: Basic Principles and Clinical Correlates , pp. 211-232
    • Dinarello, C.A.1
  • 13
    • 84941832880 scopus 로고
    • 1-proteinase inhibitor-elastase uptake by polymorphonuclear leukocytes and evidence of an elastase-specific receptor
    • 1-proteinase inhibitor-elastase uptake by polymorphonuclear leukocytes and evidence of an elastase-specific receptor. J. Clin. Chem. Clin. Biochem. 24: 299-308, 1986.
    • (1986) J. Clin. Chem. Clin. Biochem. , vol.24 , pp. 299-308
    • Dwenger, A.1    Tost, P.2
  • 14
    • 0015184089 scopus 로고
    • The immunologic release of constituents from neutrophil leukocytes
    • Henson, P. M. The immunologic release of constituents from neutrophil leukocytes. J. Immunol. 107: 1547-1557, 1971.
    • (1971) J. Immunol. , vol.107 , pp. 1547-1557
    • Henson, P.M.1
  • 16
    • 0018341904 scopus 로고
    • A rapid procedure for the large scale purification of elastase and cathepsin G from human sputum
    • Martodam, R. R., R. J. Baugh, D. Y. Twumasi, and I. E. Liener. A rapid procedure for the large scale purification of elastase and cathepsin G from human sputum. Prep. Biochem. 9: 15-31, 1979.
    • (1979) Prep. Biochem. , vol.9 , pp. 15-31
    • Martodam, R.R.1    Baugh, R.J.2    Twumasi, D.Y.3    Liener, I.E.4
  • 17
    • 0020576190 scopus 로고
    • A comparison of the binding and fate of internalized neutrophil elastase in human monocytes and alveolar macrophages
    • McGowan, S. E., R. D. Arbeit, P. J. Stone, and G. L. Snider. A comparison of the binding and fate of internalized neutrophil elastase in human monocytes and alveolar macrophages. Am. Rev. Respir. Dis. 128: 688-694, 1983.
    • (1983) Am. Rev. Respir. Dis. , vol.128 , pp. 688-694
    • McGowan, S.E.1    Arbeit, R.D.2    Stone, P.J.3    Snider, G.L.4
  • 18
    • 0026681802 scopus 로고
    • Neutrophil elastase in respiratory epithelial lining fluid of individuals with cystic fibrosis induces interleukin-8 gene expression in a human bronchial epithelial cell line
    • Nakamura, H., K. Yoshimura, N. G. McElvaney, and R. G. Crystal. Neutrophil elastase in respiratory epithelial lining fluid of individuals with cystic fibrosis induces interleukin-8 gene expression in a human bronchial epithelial cell line. J. Clin. Invest. 89: 1478-1484, 1992.
    • (1992) J. Clin. Invest. , vol.89 , pp. 1478-1484
    • Nakamura, H.1    Yoshimura, K.2    McElvaney, N.G.3    Crystal, R.G.4
  • 19
    • 0018345813 scopus 로고
    • Digestion of the fifth component of complement by leukocyte enzymes: Sequential generation of chemotactic activities for leukocytes and for tumor cells
    • Orr, F. W., J. Varani, D. L. Kreutzer, R. M. Senior, and P. A. Ward. Digestion of the fifth component of complement by leukocyte enzymes: sequential generation of chemotactic activities for leukocytes and for tumor cells. Am. J. Pathol. 94: 75-83, 1979.
    • (1979) Am. J. Pathol. , vol.94 , pp. 75-83
    • Orr, F.W.1    Varani, J.2    Kreutzer, D.L.3    Senior, R.M.4    Ward, P.A.5
  • 20
    • 0029443042 scopus 로고
    • Neutrophil proteinases and matrix degradation. the cell biology of pericellular proteolysis
    • Owen, C. A., and E. J. Campbell. Neutrophil proteinases and matrix degradation. The cell biology of pericellular proteolysis. Semin. Cell Biol. 6: 367-376, 1995.
    • (1995) Semin. Cell Biol. , vol.6 , pp. 367-376
    • Owen, C.A.1    Campbell, E.J.2
  • 21
    • 0028575729 scopus 로고
    • Monocytes recruited to sites of inflammation express a distinctive pro-inflammatory (P) phenotype
    • Lung Cell. Mol. Physiol. 11
    • Owen, C. A., M. A. Campbell, S. S. Boukedes, and E. J. Campbell. Monocytes recruited to sites of inflammation express a distinctive pro-inflammatory (P) phenotype. Am. J. Physiol. 267 (Lung Cell. Mol. Physiol. 11): L786-L796, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Owen, C.A.1    Campbell, M.A.2    Boukedes, S.S.3    Campbell, E.J.4
  • 22
    • 0028802595 scopus 로고
    • Inducible binding of cathepsin G to the cell surface of neutrophils: A mechanism for mediating extracellular proteolytic activity of cathepsin G
    • Owen, C. A., M. A. Campbell, S. S. Boukedes, and E. J. Campbell. Inducible binding of cathepsin G to the cell surface of neutrophils: a mechanism for mediating extracellular proteolytic activity of cathepsin G. J. Immunol. 155: 5803-5810, 1995.
    • (1995) J. Immunol. , vol.155 , pp. 5803-5810
    • Owen, C.A.1    Campbell, M.A.2    Boukedes, S.S.3    Campbell, E.J.4
  • 23
    • 0028607459 scopus 로고
    • A discrete subpopulation of human monocytes expresses a neutrophil-like pro-inflammatory (P) phenotype
    • Lung Cell. Mol. Physiol. 11
    • Owen, C. A., M. A. Campbell, S. S. Boukedes, R. A. Stockley, and E. J. Campbell. A discrete subpopulation of human monocytes expresses a neutrophil-like pro-inflammatory (P) phenotype. Am. J. Physiol. 267 (Lung Cell. Mol. Physiol. 11): L775-L785, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Owen, C.A.1    Campbell, M.A.2    Boukedes, S.S.3    Stockley, R.A.4    Campbell, E.J.5
  • 24
    • 0028865394 scopus 로고
    • Cell-surface-bound elastase and cathepsin G on human neutrophils. A novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases
    • Owen, C. A., M. A. Campbell, P. L. Sannes, S. S. Boukedes, and E. J. Campbell. Cell-surface-bound elastase and cathepsin G on human neutrophils. A novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases. J. Cell Biol. 131: 775-789, 1995.
    • (1995) J. Cell Biol. , vol.131 , pp. 775-789
    • Owen, C.A.1    Campbell, M.A.2    Sannes, P.L.3    Boukedes, S.S.4    Campbell, E.J.5
  • 25
    • 0026056106 scopus 로고
    • Human neutrophil elastase releases a ligand-binding fragment from the 75-kDa tumor necrosis factor (TNF) receptor
    • Porteu, F., M. Brockhaus, D. Wallach, H. Engelmann, and C. F. Nathan. Human neutrophil elastase releases a ligand-binding fragment from the 75-kDa tumor necrosis factor (TNF) receptor. J. Biol. Chem. 266: 18846-18853, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18846-18853
    • Porteu, F.1    Brockhaus, M.2    Wallach, D.3    Engelmann, H.4    Nathan, C.F.5
  • 26
    • 0017326665 scopus 로고
    • Reaction of serine proteases with aza-amino acid and aza-peptide derivatives
    • Powers, J. C., and B. F. Gupton. Reaction of serine proteases with aza-amino acid and aza-peptide derivatives. Methods Enzymol. 46: 208-216, 1977.
    • (1977) Methods Enzymol. , vol.46 , pp. 208-216
    • Powers, J.C.1    Gupton, B.F.2
  • 27
    • 0027155816 scopus 로고
    • Enhancement of cathepsin G-induced platelet activation by leukocyte elastase: Consequence for the neutrophil-mediated platelet activation
    • Renesto, P., and M. Ghignard. Enhancement of cathepsin G-induced platelet activation by leukocyte elastase: consequence for the neutrophil-mediated platelet activation. Blood 82: 139-144, 1993.
    • (1993) Blood , vol.82 , pp. 139-144
    • Renesto, P.1    Ghignard, M.2
  • 29
    • 0026755667 scopus 로고
    • Detection of extracellular neutrophil elastase in hamster lungs after intratracheal instillation of E. coli lipopolysaccharide using a fluorogenic, elastase-specific, synthetic substrate
    • Rudolphus, A., J. Stolk, C. Van Twisk, C. J. F. van Noorden, J. H. Dijkman, and J. A. Kramps. Detection of extracellular neutrophil elastase in hamster lungs after intratracheal instillation of E. coli lipopolysaccharide using a fluorogenic, elastase-specific, synthetic substrate. Am. J. Pathol. 141: 153-160, 1992.
    • (1992) Am. J. Pathol. , vol.141 , pp. 153-160
    • Rudolphus, A.1    Stolk, J.2    Van Twisk, C.3    Van Noorden, C.J.F.4    Dijkman, J.H.5    Kramps, J.A.6
  • 30
    • 0027142981 scopus 로고
    • Regulation of cytokine secretion by cystic fibrosis airway epithelial cells
    • Ruef, C., D. M. Jefferson, S. E. Schlegel-Haueter, and S. Suter. Regulation of cytokine secretion by cystic fibrosis airway epithelial cells. Eur. Respir. J. 6: 1429-1436, 1993.
    • (1993) Eur. Respir. J. , vol.6 , pp. 1429-1436
    • Ruef, C.1    Jefferson, D.M.2    Schlegel-Haueter, S.E.3    Suter, S.4
  • 31
    • 2542641284 scopus 로고
    • Differential release of elastase and chymotrypsin from polymorphonuclear leukocytes
    • edited by K. Havemann and A. Janoff. Baltimore, MD: Urban & Schwarzenberg
    • Schmidt, W. Differential release of elastase and chymotrypsin from polymorphonuclear leukocytes. In: Neutral Proteases of Polymorphonuclear Leukocytes, edited by K. Havemann and A. Janoff. Baltimore, MD: Urban & Schwarzenberg, 1978, p. 77-81.
    • (1978) Neutral Proteases of Polymorphonuclear Leukocytes , pp. 77-81
    • Schmidt, W.1
  • 32
    • 0025732513 scopus 로고
    • Cathepsin-G and leukocyte elastase inactivate human tumor necrosis factor and lymphotoxin
    • Scuderi, P., P. A. Nez, M. L. Duerr, B. J. Wong, and C. M. Valdez. Cathepsin-G and leukocyte elastase inactivate human tumor necrosis factor and lymphotoxin. Cell. Immunol. 135: 299-313, 1991.
    • (1991) Cell. Immunol. , vol.135 , pp. 299-313
    • Scuderi, P.1    Nez, P.A.2    Duerr, M.L.3    Wong, B.J.4    Valdez, C.M.5
  • 33
    • 0017687920 scopus 로고
    • Limited degradation of third component (C3) of human complement by human leukocyte elastase (HLE): Partial characterization of C3 fragments
    • Taylor, J. C., I. P. Crawford, and T. E. Hugli. Limited degradation of third component (C3) of human complement by human leukocyte elastase (HLE): partial characterization of C3 fragments. Biochemistry 16: 3390-3396, 1977.
    • (1977) Biochemistry , vol.16 , pp. 3390-3396
    • Taylor, J.C.1    Crawford, I.P.2    Hugli, T.E.3
  • 34
    • 0025790451 scopus 로고
    • Inactivation of recombinant human tumor necrosis factor-α by proteolytic enzymes released from stimulated human neutrophils
    • Van Kessel, K. P. M., J. A. G. Van Strijp, and J. Verhoef. Inactivation of recombinant human tumor necrosis factor-α by proteolytic enzymes released from stimulated human neutrophils. J. Immunol. 147: 3862-3868, 1991.
    • (1991) J. Immunol. , vol.147 , pp. 3862-3868
    • Van Kessel, K.P.M.1    Van Strijp, J.A.G.2    Verhoef, J.3
  • 35
    • 0023924297 scopus 로고
    • Platelet-activating factor primes neutrophil responses to agonists: Role in promoting neutrophil-mediated endothelial damage
    • Vercellotti, G. M., H. Q. Yin, K. S. Gustafson, R. D. Nelson, and H. S. Jacob. Platelet-activating factor primes neutrophil responses to agonists: role in promoting neutrophil-mediated endothelial damage. Blood 71: 1100-1107, 1988.
    • (1988) Blood , vol.71 , pp. 1100-1107
    • Vercellotti, G.M.1    Yin, H.Q.2    Gustafson, K.S.3    Nelson, R.D.4    Jacob, H.S.5
  • 36
    • 0001168910 scopus 로고
    • Platelet-activating factor. a fluid-phase and cell-associated mediator of inflammation
    • edited by J. I. Gallin, I. M. Goldstein, and R. Snyderman. New York: Raven
    • Zimmerman, G. A., S. M. Prescott, and T. M. McIntyre. Platelet-activating factor. A fluid-phase and cell-associated mediator of inflammation. In: Inflammation. Basic Principles and Clinical Correlates, edited by J. I. Gallin, I. M. Goldstein, and R. Snyderman. New York: Raven, 1992, p. 149-176.
    • (1992) Inflammation. Basic Principles and Clinical Correlates , pp. 149-176
    • Zimmerman, G.A.1    Prescott, S.M.2    McIntyre, T.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.