메뉴 건너뛰기




Volumn 2, Issue 3, 2006, Pages 263-277

A pulmonary perspective on GASPIDs: Granule-Associated serine peptidases of immune defense

Author keywords

Cathepsin G; Chymase; Factor D; Granzyme; Neutrophil elastase; Tyrptase

Indexed keywords

ADIPSIN; BETA TRYPTASE; CATHEPSIN G; CHYMASE; COMPLEMENT FACTOR D; GRANULE ASSOCIATED SERINE PEPTIDASE OF IMMUNE DEFENSE; GRANULOCYTE ANTIBODY; GRANZYME A; GRANZYME B; LEUKOCYTE ELASTASE; MYELOBLASTIN; PEPTIDASE; TRYPTASE; UNCLASSIFIED DRUG;

EID: 33747707534     PISSN: 1573398X     EISSN: None     Source Type: Journal    
DOI: 10.2174/157339806778019024     Document Type: Review
Times cited : (13)

References (144)
  • 3
    • 0025212267 scopus 로고
    • Different mouse mast cell populations express various combinations of at least six distinct mast cell serine proteases
    • Reynolds DS, Stevens RL, Lane WS, Carr MH, Austen KF, Serafin WE. Different mouse mast cell populations express various combinations of at least six distinct mast cell serine proteases. Proc Natl Acad Sci USA 1990; 87: 3230-4.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3230-3234
    • Reynolds, D.S.1    Stevens, R.L.2    Lane, W.S.3    Carr, M.H.4    Austen, K.F.5    Serafin, W.E.6
  • 4
    • 0028046879 scopus 로고
    • Genes for mast-cell serine protease and their molecular evolution
    • Huang R, Hellman L. Genes for mast-cell serine protease and their molecular evolution. Immunogenetics 1994; 40: 397-414.
    • (1994) Immunogenetics , vol.40 , pp. 397-414
    • Huang, R.1    Hellman, L.2
  • 5
    • 0039649450 scopus 로고    scopus 로고
    • Secretory granule proteases in rat mast cells. Cloning of 10 different serine proteases and a carboxypeptidase A from various rat mast cell populations
    • Lutzelschwab C, Pejler G, Aveskogh M, Hellman L. Secretory granule proteases in rat mast cells. Cloning of 10 different serine proteases and a carboxypeptidase A from various rat mast cell populations. J Exp Med 1997; 185: 13-29.
    • (1997) J Exp Med , vol.185 , pp. 13-29
    • Lutzelschwab, C.1    Pejler, G.2    Aveskogh, M.3    Hellman, L.4
  • 6
    • 0036034837 scopus 로고    scopus 로고
    • New developments in the genetics and activation of mast cell proteases
    • Caughey GH. New developments in the genetics and activation of mast cell proteases. Mol Immunol 2002; 38: 1353-7.
    • (2002) Mol Immunol , vol.38 , pp. 1353-1357
    • Caughey, G.H.1
  • 7
    • 0347445722 scopus 로고    scopus 로고
    • A genomic analysis of rat proteases and protease inhibitors
    • Puente XS, Lopez-Otin C. A genomic analysis of rat proteases and protease inhibitors. Genome Res 2004; 14: 609-22.
    • (2004) Genome Res , vol.14 , pp. 609-622
    • Puente, X.S.1    Lopez-Otin, C.2
  • 8
    • 0034659960 scopus 로고    scopus 로고
    • Characterization of human γ-tryptases, novel members of the chromosome 16p mast cell tryptase and prostasin gene families
    • Caughey GH, Raymond WW, Blount JL et al. Characterization of human γ-tryptases, novel members of the chromosome 16p mast cell tryptase and prostasin gene families. J Immunol 2000; 164: 6566-75.
    • (2000) J Immunol , vol.164 , pp. 6566-6575
    • Caughey, G.H.1    Raymond, W.W.2    Blount, J.L.3
  • 9
    • 13544256359 scopus 로고    scopus 로고
    • Mastin is a gelatinolytic mast cell peptidase resembling a mini-proteasome
    • Raymond WW, Sommerhoff CP, Caughey GH. Mastin is a gelatinolytic mast cell peptidase resembling a mini-proteasome. Arch Biochem Biophys 2005; 435: 311-22.
    • (2005) Arch Biochem Biophys , vol.435 , pp. 311-322
    • Raymond, W.W.1    Sommerhoff, C.P.2    Caughey, G.H.3
  • 10
    • 0024299058 scopus 로고
    • Purification and characterization of dog mastocytoma chymase. Identification of an octapeptide conserved in chymotryptic leukocyte proteases
    • Caughey GH, Viro NF, Lazarus SC, Nadel JA. Purification and characterization of dog mastocytoma chymase. Identification of an octapeptide conserved in chymotryptic leukocyte proteases. Biochim Biophys Acta 1988; 952: 142-9.
    • (1988) Biochim Biophys Acta , vol.952 , pp. 142-149
    • Caughey, G.H.1    Viro, N.F.2    Lazarus, S.C.3    Nadel, J.A.4
  • 12
    • 0141957399 scopus 로고    scopus 로고
    • A despecialization step underlying evolution of a family of serine proteases
    • Wouters MA, Liu K, Riek P, Husain A. A despecialization step underlying evolution of a family of serine proteases. Mol Cell 2003; 12: 343-54.
    • (2003) Mol Cell , vol.12 , pp. 343-354
    • Wouters, M.A.1    Liu, K.2    Riek, P.3    Husain, A.4
  • 13
    • 0024465841 scopus 로고
    • Isolation and complete structure of the lymphocyte serine protease granzyme G, a novel member of the granzyme multigene family in murine cytolytic T lymphocytes. Evolutionary origin of lymphocyte proteases
    • Jenne DE, Masson D, Zimmer M, Haefliger J-A, Li W-H, Tschopp J. Isolation and complete structure of the lymphocyte serine protease granzyme G, a novel member of the granzyme multigene family in murine cytolytic T lymphocytes. Evolutionary origin of lymphocyte proteases. Biochemistry 1989; 28: 7953-61.
    • (1989) Biochemistry , vol.28 , pp. 7953-7961
    • Jenne, D.E.1    Masson, D.2    Zimmer, M.3    Haefliger, J.-A.4    Li, W.-H.5    Tschopp, J.6
  • 15
    • 0033525211 scopus 로고    scopus 로고
    • Characterization of genes encoding known and novel human mast cell tryptases on chromosome 16p13.3
    • Pallaoro M, Fejzo MS, Shayesteh L, Blount JL, Caughey GH. Characterization of genes encoding known and novel human mast cell tryptases on chromosome 16p13.3. J Biol Chem 1999; 274: 3355-62.
    • (1999) J Biol Chem , vol.274 , pp. 3355-3362
    • Pallaoro, M.1    Fejzo, M.S.2    Shayesteh, L.3    Blount, J.L.4    Caughey, G.H.5
  • 17
    • 0027415378 scopus 로고
    • The human mast cell chymase gene (CMA1): Mapping to the cathepsin G /granzyme gene cluster and lineage-restricted expression
    • Caughey GH, Schaumberg TH, Zerweck EH, et al. The human mast cell chymase gene (CMA1): mapping to the cathepsin G/granzyme gene cluster and lineage-restricted expression. Genomics 1993; 15: 614-20.
    • (1993) Genomics , vol.15 , pp. 614-620
    • Caughey, G.H.1    Schaumberg, T.H.2    Zerweck, E.H.3
  • 18
    • 0033538454 scopus 로고    scopus 로고
    • Human tryptases α and β/II are functionally distinct due, in part, to a single amino acid difference in one of the surface loops that forms the substrate-binding cleft
    • Huang C, Li L, Krilis SA, et al. Human tryptases α and β/II are functionally distinct due, in part, to a single amino acid difference in one of the surface loops that forms the substrate-binding cleft. J Biol Chem 1999; 274: 19670-6.
    • (1999) J Biol Chem , vol.274 , pp. 19670-19676
    • Huang, C.1    Li, L.2    Krilis, S.A.3
  • 19
    • 0036385841 scopus 로고    scopus 로고
    • The crystal structure of human α1-tryptase reveals a blocked substrate-binding region
    • Marquardt U, Zettl F, Huber R, Bode W, Sommerhoff C. The crystal structure of human α1-tryptase reveals a blocked substrate-binding region. J Mol Biol 2002; 321: 491-502.
    • (2002) J Mol Biol , vol.321 , pp. 491-502
    • Marquardt, U.1    Zettl, F.2    Huber, R.3    Bode, W.4    Sommerhoff, C.5
  • 20
    • 0036446159 scopus 로고    scopus 로고
    • Rodent alpha-chymases are elastase-like proteases
    • Kunori Y, Koizumi M, Masegi T, et al. Rodent alpha-chymases are elastase-like proteases. Eur J Biochem 2002; 269: 5921-30.
    • (2002) Eur J Biochem , vol.269 , pp. 5921-5930
    • Kunori, Y.1    Koizumi, M.2    Masegi, T.3
  • 21
    • 0141960165 scopus 로고    scopus 로고
    • Extended substrate specificity of rat mast cell protease 5, a rodent α-chymase with elastase-like primary specificity
    • Karlson U, Pejler G, Tomasini-Johansson B, Hellman L. Extended substrate specificity of rat mast cell protease 5, a rodent α-chymase with elastase-like primary specificity. J Biol Chem 2003; 278: 39625-31.
    • (2003) J Biol Chem , vol.278 , pp. 39625-39631
    • Karlson, U.1    Pejler, G.2    Tomasini-Johansson, B.3    Hellman, L.4
  • 22
    • 0025835534 scopus 로고
    • Structure, chromosomal assignment, and deduced amino acid sequence of a human gene for mast cell chymase
    • Caughey GH, Zerweck EH, Vanderslice P. Structure, chromosomal assignment, and deduced amino acid sequence of a human gene for mast cell chymase. J Biol Chem 1991; 266: 12956-63.
    • (1991) J Biol Chem , vol.266 , pp. 12956-12963
    • Caughey, G.H.1    Zerweck, E.H.2    Vanderslice, P.3
  • 25
    • 1642576098 scopus 로고    scopus 로고
    • Mouse chromosome 17A3.3 contains 13 genes that encode functional tryptic-like serine proteases with distinct tissue and cell expression patterns
    • Wong GW, Yasuda S, Morokawa N, Li L, Stevens RL. Mouse chromosome 17A3.3 contains 13 genes that encode functional tryptic-like serine proteases with distinct tissue and cell expression patterns. J Biol Chem 2004; 279: 2438-52.
    • (2004) J Biol Chem , vol.279 , pp. 2438-2452
    • Wong, G.W.1    Yasuda, S.2    Morokawa, N.3    Li, L.4    Stevens, R.L.5
  • 26
    • 0000317053 scopus 로고
    • Chloroacyl esters as histochemical substrates
    • Gomori G. Chloroacyl esters as histochemical substrates. J Histochem Cytochem 1953; 1: 469-70.
    • (1953) J Histochem Cytochem , vol.1 , pp. 469-470
    • Gomori, G.1
  • 27
    • 0000452039 scopus 로고
    • Histochemical demonstration of a species-specific trypsin-like enzyme in mast cells
    • Glenner GG, Cohen LA. Histochemical demonstration of a species-specific trypsin-like enzyme in mast cells. Nature 1960; 185: 846-7.
    • (1960) Nature , vol.185 , pp. 846-847
    • Glenner, G.G.1    Cohen, L.A.2
  • 28
    • 0037432314 scopus 로고    scopus 로고
    • Structure of human pro-chymase: A model for the activating transition of granule-associated proteases
    • Reiling KY, Krucinski J, Miercke LJ, Raymond WW, Caughey GH, Stroud RM. Structure of human pro-chymase: a model for the activating transition of granule-associated proteases. Biochemistry 2003; 42: 2616-24.
    • (2003) Biochemistry , vol.42 , pp. 2616-2624
    • Reiling, K.Y.1    Krucinski, J.2    Miercke, L.J.3    Raymond, W.W.4    Caughey, G.H.5    Stroud, R.M.6
  • 29
    • 0032546934 scopus 로고    scopus 로고
    • Regulated expression, processing, and secretion of dog mast cell dipeptidyl peptidase I
    • Wolters PJ, Raymond WW, Blount JL, Caughey GH. Regulated expression, processing, and secretion of dog mast cell dipeptidyl peptidase I. J Biol Chem 1998; 273: 15514-20.
    • (1998) J Biol Chem , vol.273 , pp. 15514-15520
    • Wolters, P.J.1    Raymond, W.W.2    Blount, J.L.3    Caughey, G.H.4
  • 30
    • 0034088336 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I cleaves matrix-associated proteins and is expressed mainly by mast cells in normal dog airways
    • Wolters PJ, Laig-Webster M, Caughey GH. Dipeptidyl peptidase I cleaves matrix-associated proteins and is expressed mainly by mast cells in normal dog airways. Am J Respir Cell Mol Biol 2000; 22: 183-90.
    • (2000) Am J Respir Cell Mol Biol , vol.22 , pp. 183-190
    • Wolters, P.J.1    Laig-Webster, M.2    Caughey, G.H.3
  • 31
    • 0027518670 scopus 로고
    • Generation of active myeloid and lymphoid granule serine proteases requires processing by the granule thiol protease dipeptidyl peptidase I
    • McGuire MJ, Lipsky PE, Thiele DL. Generation of active myeloid and lymphoid granule serine proteases requires processing by the granule thiol protease dipeptidyl peptidase I. J Biol Chem 1993; 268: 2458-67.
    • (1993) J Biol Chem , vol.268 , pp. 2458-2467
    • McGuire, M.J.1    Lipsky, P.E.2    Thiele, D.L.3
  • 32
    • 0033587689 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo
    • Pham CT, Ley TJ. Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo. Proc Natl Acad Sci USA 1999; 96: 8627-32.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8627-8632
    • Pham, C.T.1    Ley, T.J.2
  • 33
    • 0035947568 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I is essential for activation of mast cell chymases, but not tryptases, in mice
    • Wolters PJ, Pham CT, Muilenburg DJ, Ley TJ, Caughey GH. Dipeptidyl peptidase I is essential for activation of mast cell chymases, but not tryptases, in mice. J Biol Chem 2001; 276: 18551-6.
    • (2001) J Biol Chem , vol.276 , pp. 18551-18556
    • Wolters, P.J.1    Pham, C.T.2    Muilenburg, D.J.3    Ley, T.J.4    Caughey, G.H.5
  • 34
    • 0036168150 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I activates neutrophil-derived serine proteases and regulates the development of acute experimental arthritis
    • Adkison AM, Raptis SZ, Kelley DG, Pham CT. Dipeptidyl peptidase I activates neutrophil-derived serine proteases and regulates the development of acute experimental arthritis. J Clin Invest 2002; 109: 363-71.
    • (2002) J Clin Invest , vol.109 , pp. 363-371
    • Adkison, A.M.1    Raptis, S.Z.2    Kelley, D.G.3    Pham, C.T.4
  • 35
    • 0033455594 scopus 로고    scopus 로고
    • Mutations of the cathepsin C gene are responsible for Papillon-Lefevre syndrome
    • Hart TC, Hart PS, Bowden DW, et al. Mutations of the cathepsin C gene are responsible for Papillon-Lefevre syndrome. J Med Genet 1999; 36: 881-7.
    • (1999) J Med Genet , vol.36 , pp. 881-887
    • Hart, T.C.1    Hart, P.S.2    Bowden, D.W.3
  • 36
    • 4444343709 scopus 로고    scopus 로고
    • Loss-of-function mutations in cathepsin C in two families with Papillon-Lefevre syndrome are associated with deficiency of serine proteinases in PMNs
    • de Haar SF, Jansen DC, Schoenmaker T, De Vree H, Everts V, Beertsen W. Loss-of-function mutations in cathepsin C in two families with Papillon-Lefevre syndrome are associated with deficiency of serine proteinases in PMNs. Hum Mutat 2004; 23: 524.
    • (2004) Hum Mutat , vol.23 , pp. 524
    • de Haar, S.F.1    Jansen, D.C.2    Schoenmaker, T.3    De Vree, H.4    Everts, V.5    Beertsen, W.6
  • 37
    • 10344234724 scopus 로고    scopus 로고
    • Papillon-Lefevre syndrome: Correlating the molecular, cellular, and clinical consequences of cathepsin C/dipeptidyl peptidase I deficiency in humans
    • Pham CT, Ivanovich JL, Raptis SZ, Zehnbauer B, Ley TJ. Papillon-Lefevre syndrome: correlating the molecular, cellular, and clinical consequences of cathepsin C/dipeptidyl peptidase I deficiency in humans. J Immunol 2004; 173: 7277-81.
    • (2004) J Immunol , vol.173 , pp. 7277-7281
    • Pham, C.T.1    Ivanovich, J.L.2    Raptis, S.Z.3    Zehnbauer, B.4    Ley, T.J.5
  • 38
    • 0030068941 scopus 로고    scopus 로고
    • A novel heparin-dependent processing pathway for human tryptase: Autocatalysis followed by activation with dipeptidyl peptidase I
    • Sakai K, Ren S, Schwartz LB. A novel heparin-dependent processing pathway for human tryptase: autocatalysis followed by activation with dipeptidyl peptidase I. J Clin Invest 1996; 97: 988-95.
    • (1996) J Clin Invest , vol.97 , pp. 988-995
    • Sakai, K.1    Ren, S.2    Schwartz, L.B.3
  • 39
    • 0010234421 scopus 로고
    • Substrate specificity of the chymotrypsin-like protease in secretory granules isolated from rat mast cells
    • Le Trong H, Neurath H, Woodbury RG. Substrate specificity of the chymotrypsin-like protease in secretory granules isolated from rat mast cells. Proc Natl Acad Sci USA 1987; 84: 364-7.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 364-367
    • Le Trong, H.1    Neurath, H.2    Woodbury, R.G.3
  • 40
    • 0026518944 scopus 로고
    • Protease composition of exocytosed human skin mast cell protease-proteoglycan complexes: Tryptase resides in a complex distinct from chymase and carboxypeptidase
    • Goldstein SM, Leong J, Schwartz LB, Cooke D. Protease composition of exocytosed human skin mast cell protease-proteoglycan complexes: tryptase resides in a complex distinct from chymase and carboxypeptidase. J Immunol 1992; 148: 2475-82.
    • (1992) J Immunol , vol.148 , pp. 2475-2482
    • Goldstein, S.M.1    Leong, J.2    Schwartz, L.B.3    Cooke, D.4
  • 41
    • 0021148042 scopus 로고
    • Human lung tryptase. Purification and characterization
    • Smith TJ, Hougland MW, Johnson DA. Human lung tryptase. Purification and characterization. J Biol Chem 1984; 259: 11046-51.
    • (1984) J Biol Chem , vol.259 , pp. 11046-11051
    • Smith, T.J.1    Hougland, M.W.2    Johnson, D.A.3
  • 42
    • 0022872843 scopus 로고
    • Regulation of tryptase from human lung mast cells by heparin. Stabilization of the active tetramer
    • Schwartz LB, Bradford TR. Regulation of tryptase from human lung mast cells by heparin. Stabilization of the active tetramer. J Biol Chem 1986; 261: 7372-9.
    • (1986) J Biol Chem , vol.261 , pp. 7372-7379
    • Schwartz, L.B.1    Bradford, T.R.2
  • 43
    • 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 CA, Campbell MA, Sannes PL, Boukedes SS, Campbell EJ. 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 1995; 131: 775-89.
    • (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
  • 44
    • 0031939933 scopus 로고    scopus 로고
    • Angiotensin II generation at the cell surface of activated neutrophils: Novel cathepsin G-mediated catalytic activity that is resistant to inhibition
    • Owen CA, Campbell EJ. Angiotensin II generation at the cell surface of activated neutrophils: novel cathepsin G-mediated catalytic activity that is resistant to inhibition. J Immunol 1998; 160: 1436-43.
    • (1998) J Immunol , vol.160 , pp. 1436-1443
    • Owen, C.A.1    Campbell, E.J.2
  • 45
    • 23844554460 scopus 로고    scopus 로고
    • Inhibition of neutrophil elastase by α1-protease inhibitor at the surface of human polymorphonuclear neutrophils
    • Korkmaz B, Attucci S, Jourdan ML, Juliano L, Gauthier F. Inhibition of neutrophil elastase by α1-protease inhibitor at the surface of human polymorphonuclear neutrophils. J Immmunol 2005; 175: 3329-38.
    • (2005) J Immmunol , vol.175 , pp. 3329-3338
    • Korkmaz, B.1    Attucci, S.2    Jourdan, M.L.3    Juliano, L.4    Gauthier, F.5
  • 46
    • 0032741435 scopus 로고    scopus 로고
    • Identification of a new member of the tryptase family of mouse and human mast cell proteases which possesses a novel COON-terminal hydrophobic extension
    • Wong GW, Tang Y, Feyfant E, et al. Identification of a new member of the tryptase family of mouse and human mast cell proteases which possesses a novel COON-terminal hydrophobic extension. J Biol Chem 1999; 274: 30784-93.
    • (1999) J Biol Chem , vol.274 , pp. 30784-30793
    • Wong, G.W.1    Tang, Y.2    Feyfant, E.3
  • 47
    • 0036830570 scopus 로고    scopus 로고
    • Biochemical and functional characterization of human transmembrane tryptase (TMT)/tryptase gamma. TMT is an exocytosed mast cell protease that induces airway hyperresponsiveness in vivo via an interleukin-13 /interleukin-4 receptor alpha/signal transducer and activator of transcription (STAT) 6-dependent pathway
    • Wong GW, Foster PS, Yasuda S, et al. Biochemical and functional characterization of human transmembrane tryptase (TMT)/tryptase gamma. TMT is an exocytosed mast cell protease that induces airway hyperresponsiveness in vivo via an interleukin-13/interleukin-4 receptor alpha/signal transducer and activator of transcription (STAT) 6-dependent pathway. J Biol Chem 2002; 277: 41906-15.
    • (2002) J Biol Chem , vol.277 , pp. 41906-41915
    • Wong, G.W.1    Foster, P.S.2    Yasuda, S.3
  • 48
    • 0035863818 scopus 로고    scopus 로고
    • Mast cell-dependent B and T lymphocyte activation is mediated by the secretion of immunologically active exosomes
    • Skokos D, Le Panse S, Villa I, et al. Mast cell-dependent B and T lymphocyte activation is mediated by the secretion of immunologically active exosomes. J Immunol 2001; 166: 868-76.
    • (2001) J Immunol , vol.166 , pp. 868-876
    • Skokos, D.1    Le Panse, S.2    Villa, I.3
  • 49
    • 0037443410 scopus 로고    scopus 로고
    • Mast cell-derived exosomes induce phenotypic and fractional maturation of dendritic cells and elicit specific immune responses in vivo
    • Skokos D, Botros HG, Demeure C, et al. Mast cell-derived exosomes induce phenotypic and fractional maturation of dendritic cells and elicit specific immune responses in vivo. J Immunol 2003; 170: 3037-45.
    • (2003) J Immunol , vol.170 , pp. 3037-3045
    • Skokos, D.1    Botros, H.G.2    Demeure, C.3
  • 50
    • 0034665315 scopus 로고    scopus 로고
    • Bioactive proteinase 3 on the cell surface of human neutrophils: Quantification, catalytic activity, and susceptibility to inhibition
    • Campbell EJ, Campbell MA, Owen CA. Bioactive proteinase 3 on the cell surface of human neutrophils: quantification, catalytic activity, and susceptibility to inhibition. J Immunol 2000; 165: 3366-74.
    • (2000) J Immunol , vol.165 , pp. 3366-3374
    • Campbell, E.J.1    Campbell, M.A.2    Owen, C.A.3
  • 51
    • 0348143307 scopus 로고    scopus 로고
    • Membrane proteinase 3 expression on resting neutrophils as a pathogenic factor in PR3-ANCA-associated vasculitis
    • van Rossum AP, Limburg PC, Kallenberg CG. Membrane proteinase 3 expression on resting neutrophils as a pathogenic factor in PR3-ANCA-associated vasculitis. Clin Exp Rheumatol 2003; 21: S64-8.
    • (2003) Clin Exp Rheumatol , vol.21
    • van Rossum, A.P.1    Limburg, P.C.2    Kallenberg, C.G.3
  • 52
    • 0033557766 scopus 로고    scopus 로고
    • Structural basis of profactor D activation: From a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D
    • Jing H, Macon KJ, Moore D, DeLucas LJ, Volanakis JE, Narayana SV. Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D. EMBO J 1999; 18: 804-14.
    • (1999) EMBO J , vol.18 , pp. 804-814
    • Jing, H.1    Macon, K.J.2    Moore, D.3    DeLucas, L.J.4    Volanakis, J.E.5    Narayana, S.V.6
  • 53
    • 0032500627 scopus 로고    scopus 로고
    • Structures of native and complexed complement factor D: Implications of the atypical His57 conformation and self-inhibitory loop in the regulation of specific serine protease activity
    • Jing H, Babu YS, Moore D, et al. Structures of native and complexed complement factor D: implications of the atypical His57 conformation and self-inhibitory loop in the regulation of specific serine protease activity. J Mol Biol 1998; 282: 1061-81.
    • (1998) J Mol Biol , vol.282 , pp. 1061-1081
    • Jing, H.1    Babu, Y.S.2    Moore, D.3
  • 54
    • 2642600031 scopus 로고    scopus 로고
    • Human β-tryptase is a ring-like tetramer with active sites facing a central pore
    • Pereira PJB, Bergner A, Macedo-Ribeiro S, et al. Human β-tryptase is a ring-like tetramer with active sites facing a central pore. Nature 1998; 392: 306-11.
    • (1998) Nature , vol.392 , pp. 306-311
    • Pereira, P.J.B.1    Bergner, A.2    Macedo-Ribeiro, S.3
  • 55
    • 0029042981 scopus 로고
    • Purification and characterization of dog mast cell protease-3, an oligomeric relative of tryptases
    • Raymond WW, Tam EK, Blount JL, Caughey GH. Purification and characterization of dog mast cell protease-3, an oligomeric relative of tryptases. J Biol Chem 1995; 270: 13164-70.
    • (1995) J Biol Chem , vol.270 , pp. 13164-13170
    • Raymond, W.W.1    Tam, E.K.2    Blount, J.L.3    Caughey, G.H.4
  • 56
    • 0038392751 scopus 로고    scopus 로고
    • The oligomeric structure of human granzyme A is a determinant of its extended substrate specificity
    • Bell JK, Goetz DH, Mahrus S, Harris JL, Fletterick RJ, Craik CS. The oligomeric structure of human granzyme A is a determinant of its extended substrate specificity. Nat Struct Biol 2003; 10: 527-34.
    • (2003) Nat Struct Biol , vol.10 , pp. 527-534
    • Bell, J.K.1    Goetz, D.H.2    Mahrus, S.3    Harris, J.L.4    Fletterick, R.J.5    Craik, C.S.6
  • 58
    • 0019321009 scopus 로고
    • Kinetics of association of serine proteinases with native and oxidized α1-proteinase inhibitor and α1-antichymotrypsin
    • Beatty K, Bieth J, Travis J. Kinetics of association of serine proteinases with native and oxidized α1-proteinase inhibitor and α1-antichymotrypsin. J Biol Chem 1980; 255: 3931-4.
    • (1980) J Biol Chem , vol.255 , pp. 3931-3934
    • Beatty, K.1    Bieth, J.2    Travis, J.3
  • 59
    • 0024558667 scopus 로고
    • Alpha 1-antitrypsin deficiency: Lessons learned from the bedside to the gene and back again. Historic perspectives
    • Eriksson S. Alpha 1-antitrypsin deficiency: lessons learned from the bedside to the gene and back again. Historic perspectives. Chest 1989; 95: 181-9.
    • (1989) Chest , vol.95 , pp. 181-189
    • Eriksson, S.1
  • 60
    • 0030465416 scopus 로고    scopus 로고
    • A 30-year perspective on alpha 1-antitrypsin deficiency
    • Eriksson S. A 30-year perspective on alpha 1-antitrypsin deficiency. Chest 1996; 110: 237S-42S.
    • (1996) Chest , vol.110
    • Eriksson, S.1
  • 61
    • 0037011795 scopus 로고    scopus 로고
    • Alpha1-antitrypsin deficiency--a model for conformational diseases
    • Carrell RW, Lomas DA. Alpha1-antitrypsin deficiency--a model for conformational diseases. N Engl J Med 2002; 346: 45-53.
    • (2002) N Engl J Med , vol.346 , pp. 45-53
    • Carrell, R.W.1    Lomas, D.A.2
  • 62
    • 4744356921 scopus 로고    scopus 로고
    • Alpha-1-antitrypsin deficiency: Diagnosis and treatment
    • Perlmutter DH. Alpha-1-antitrypsin deficiency: diagnosis and treatment. Clin Liver Dis 2004; 8: 839-59.
    • (2004) Clin Liver Dis , vol.8 , pp. 839-859
    • Perlmutter, D.H.1
  • 63
    • 0027328108 scopus 로고
    • A leucine-to-proline substitution causes a defective α1-antichymotrypsin allele associated with familial obstructive lung disease
    • Poller W, Faber JP, Weidinger S, et al. A leucine-to-proline substitution causes a defective α1-antichymotrypsin allele associated with familial obstructive lung disease. Genomics 1993; 17: 740-3.
    • (1993) Genomics , vol.17 , pp. 740-743
    • Poller, W.1    Faber, J.P.2    Weidinger, S.3
  • 64
    • 0027169598 scopus 로고
    • The molecular basis of α1-antichymotrypsin deficiency in a heterozygote with liver and lung disease
    • Faber JP, Poller W, Olek K, et al. The molecular basis of α1-antichymotrypsin deficiency in a heterozygote with liver and lung disease. J Hepatol 1993; 18: 313-21.
    • (1993) J Hepatol , vol.18 , pp. 313-321
    • Faber, J.P.1    Poller, W.2    Olek, K.3
  • 67
    • 0035284891 scopus 로고    scopus 로고
    • The granzyme B inhibitor, protease inhibitor 9, is mainly expressed by dendritic cells and at immune-privileged sites
    • Bladergroen BA, Strik MC, Bovenschen N, et al. The granzyme B inhibitor, protease inhibitor 9, is mainly expressed by dendritic cells and at immune-privileged sites. J Immunol 2001; 166: 3218-25.
    • (2001) J Immunol , vol.166 , pp. 3218-3225
    • Bladergroen, B.A.1    Strik, M.C.2    Bovenschen, N.3
  • 68
    • 17444408171 scopus 로고    scopus 로고
    • The granzyme B inhibitor proteinase inhibitor 9 (PI9) is expressed by human mast cells
    • Bladergroen BA, Strik MC, Wolbink AM, et al. The granzyme B inhibitor proteinase inhibitor 9 (PI9) is expressed by human mast cells. Eur J Immunol 2005; 35: 1175-83.
    • (2005) Eur J Immunol , vol.35 , pp. 1175-1183
    • Bladergroen, B.A.1    Strik, M.C.2    Wolbink, A.M.3
  • 69
    • 0026042309 scopus 로고
    • Expression of the secretory leukoprotease inhibitor gene in epithelial cells
    • Abe T, Kobayashi N, Yoshimura K, et al. Expression of the secretory leukoprotease inhibitor gene in epithelial cells. J Clin Invest 1991; 87: 2207-15.
    • (1991) J Clin Invest , vol.87 , pp. 2207-2215
    • Abe, T.1    Kobayashi, N.2    Yoshimura, K.3
  • 71
    • 0023736418 scopus 로고
    • Alveolar fluid neutrophil elastase activity in the adult respiratory distress syndrome is complexed to α2-macroglobulin
    • Wewers MD, Herzyk DJ, Gadek JE. Alveolar fluid neutrophil elastase activity in the adult respiratory distress syndrome is complexed to α2-macroglobulin. J Clin Invest 1988; 82: 1260-7.
    • (1988) J Clin Invest , vol.82 , pp. 1260-1267
    • Wewers, M.D.1    Herzyk, D.J.2    Gadek, J.E.3
  • 72
    • 0346847766 scopus 로고    scopus 로고
    • Albumin is a substrate of human chymase: Prediction by combinatorial peptide screening and development of a selective inhibitor based on the albumin cleavage site
    • Raymond WW, Ruggles S, Craik CS, Caughey GH. Albumin is a substrate of human chymase: Prediction by combinatorial peptide screening and development of a selective inhibitor based on the albumin cleavage site. J Biol Chem 2003; 278(36): 34517-24.
    • (2003) J Biol Chem , vol.278 , Issue.36 , pp. 34517-34524
    • Raymond, W.W.1    Ruggles, S.2    Craik, C.S.3    Caughey, G.H.4
  • 73
    • 0020312338 scopus 로고
    • Rapid conversion of angiotensin I to angiotensin II by neutrophil and mast cell proteinases
    • Reilly CF, Tewksbury DA, Schechter NB, Travis J. Rapid conversion of angiotensin I to angiotensin II by neutrophil and mast cell proteinases. J Biol Chem 1982; 257: 8619-22.
    • (1982) J Biol Chem , vol.257 , pp. 8619-8622
    • Reilly, C.F.1    Tewksbury, D.A.2    Schechter, N.B.3    Travis, J.4
  • 74
    • 0025598309 scopus 로고
    • Identification of a highly specific chymase as the major angiotensin II-forming enzyme in the human heart
    • Urata H, Kinoshita A, Misono KS, Bumpus FM, Husain A. Identification of a highly specific chymase as the major angiotensin II-forming enzyme in the human heart. J Biol Chem 1990; 265: 22348-57.
    • (1990) J Biol Chem , vol.265 , pp. 22348-22357
    • Urata, H.1    Kinoshita, A.2    Misono, K.S.3    Bumpus, F.M.4    Husain, A.5
  • 75
    • 0034647653 scopus 로고    scopus 로고
    • Angiotensin II generation by mast cell α- and β-chymases
    • Caughey GH, Raymond WW, Wolters PJ. Angiotensin II generation by mast cell α- and β-chymases. Biochim Biophys Acta 2000; 1480: 245-57.
    • (2000) Biochim Biophys Acta , vol.1480 , pp. 245-257
    • Caughey, G.H.1    Raymond, W.W.2    Wolters, P.J.3
  • 76
    • 0030838414 scopus 로고    scopus 로고
    • Compartmentalization of angiotensin II generation in the dog heart. Evidence for independent mechanisms in intravascular and interstitial spaces
    • Dell'Italia LJ, Meng QC, Balcells E, et al. Compartmentalization of angiotensin II generation in the dog heart. Evidence for independent mechanisms in intravascular and interstitial spaces. J Clin Invest 1997; 100: 253-8.
    • (1997) J Clin Invest , vol.100 , pp. 253-258
    • Dell'Italia, L.J.1    Meng, Q.C.2    Balcells, E.3
  • 78
    • 0031057649 scopus 로고    scopus 로고
    • Sheep mast cell proteinase-1: Characterization as a member of a new class of dual-specific ruminant chymases
    • Pemberton AD, Huntley JF, Miller HR. Sheep mast cell proteinase-1: characterization as a member of a new class of dual-specific ruminant chymases. Biochem J 1997; 321: 665-70.
    • (1997) Biochem J , vol.321 , pp. 665-670
    • Pemberton, A.D.1    Huntley, J.F.2    Miller, H.R.3
  • 81
    • 0030711516 scopus 로고    scopus 로고
    • Crystal structure of phenylmethanesulfonyl fluoride-treated human chymase at 1.9Å
    • McGrath ME, Mirzadegan T, Schmidt BF. Crystal structure of phenylmethanesulfonyl fluoride-treated human chymase at 1.9Å. Biochemistry 1997; 36: 14318-24.
    • (1997) Biochemistry , vol.36 , pp. 14318-14324
    • McGrath, M.E.1    Mirzadegan, T.2    Schmidt, B.F.3
  • 82
    • 0033547878 scopus 로고    scopus 로고
    • The 2.2 Å crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phechloromethylketone: Structural explanation for its dipeptidyl carboxypeptidase specificity
    • Pereira PJB, Wang ZM, Rubin H, et al. The 2.2 Å crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phechloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity. J Mol Biol 1999; 286: 163-73.
    • (1999) J Mol Biol , vol.286 , pp. 163-173
    • Pereira, P.J.B.1    Wang, Z.M.2    Rubin, H.3
  • 83
    • 0027401683 scopus 로고
    • Three-dimensional models of four mouse mast cell chymases. Identification of proteoglycan binding regions and protease-specific antigenic epitopes
    • Sali A, Matsumoto R, McNeil HP, Karplus M, Stevens RL. Three-dimensional models of four mouse mast cell chymases. Identification of proteoglycan binding regions and protease-specific antigenic epitopes. J Biol Chem 1993; 268: 9023-34.
    • (1993) J Biol Chem , vol.268 , pp. 9023-9034
    • Sali, A.1    Matsumoto, R.2    McNeil, H.P.3    Karplus, M.4    Stevens, R.L.5
  • 84
    • 0037193192 scopus 로고    scopus 로고
    • Lys40 but not Arg143 influences selectivity of angiotensin conversion by human α-chymase
    • Muilenburg DJ, Raymond WW, Wolters PJ, Caughey GH. Lys40 but not Arg143 influences selectivity of angiotensin conversion by human α-chymase. Biochim Biophys Acta 2002; 1596: 346-56.
    • (2002) Biochim Biophys Acta , vol.1596 , pp. 346-356
    • Muilenburg, D.J.1    Raymond, W.W.2    Wolters, P.J.3    Caughey, G.H.4
  • 85
    • 0002451901 scopus 로고
    • Structure of human neutrophil elastase in complex with a peptide chloromethyl ketone inhibitor at 1.84-Å resolution
    • Navia MA, McKeever BM, Springer JP, et al. Structure of human neutrophil elastase in complex with a peptide chloromethyl ketone inhibitor at 1.84-Å resolution. Proc Natl Acad Sci USA 1989; 86: 7-11.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 7-11
    • Navia, M.A.1    McKeever, B.M.2    Springer, J.P.3
  • 86
    • 0029853820 scopus 로고    scopus 로고
    • The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: A Janus-faced proteinase with two opposite specificities
    • Hof P, Mayr I, Huber R et al. The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities. EMBO J 1996; 15: 5481-91.
    • (1996) EMBO J , vol.15 , pp. 5481-5491
    • Hof, P.1    Mayr, I.2    Huber, R.3
  • 87
    • 0033818886 scopus 로고    scopus 로고
    • The structure of the pro-apoptotic protease granzyme B reveals the molecular determinants of its specificity
    • Waugh SM, Harris JL, Fletterick R, Craik CS. The structure of the pro-apoptotic protease granzyme B reveals the molecular determinants of its specificity. Nat Struct Biol 2000; 7: 762-5.
    • (2000) Nat Struct Biol , vol.7 , pp. 762-765
    • Waugh, S.M.1    Harris, J.L.2    Fletterick, R.3    Craik, C.S.4
  • 88
    • 0037184613 scopus 로고    scopus 로고
    • The 2.2-A crystal structure of human pro-granzyme K reveals a rigid zymogen with unusual features
    • Hink-Schauer C, Estebanez-Perpina E, Wilharm E, et al. The 2.2-A crystal structure of human pro-granzyme K reveals a rigid zymogen with unusual features. J Biol Chem 2002; 277: 50923-33.
    • (2002) J Biol Chem , vol.277 , pp. 50923-50933
    • Hink-Schauer, C.1    Estebanez-Perpina, E.2    Wilharm, E.3
  • 89
    • 0037066138 scopus 로고    scopus 로고
    • Diverse stability and catalytic properties of human tryptase α and β isoforms are mediated by residue differences at the S1 Pocket
    • Selwood T, Wang ZM, McCaslin DR, Schechter NM. Diverse stability and catalytic properties of human tryptase α and β isoforms are mediated by residue differences at the S1 Pocket. Biochemistry 2002; 41: 3329-40.
    • (2002) Biochemistry , vol.41 , pp. 3329-3340
    • Selwood, T.1    Wang, Z.M.2    McCaslin, D.R.3    Schechter, N.M.4
  • 90
    • 0029888610 scopus 로고    scopus 로고
    • A novel substrate-binding pocket interaction restricts the specificity of the human NK cell-specific serine protease, Met-ase-1
    • Smyth MJ, O'Connor MD, Trapani JA, Kershaw MH, Brinkworth RI. A novel substrate-binding pocket interaction restricts the specificity of the human NK cell-specific serine protease, Met-ase-1. J Immunol 1996; 156: 4174-81.
    • (1996) J Immunol , vol.156 , pp. 4174-4181
    • Smyth, M.J.1    O'Connor, M.D.2    Trapani, J.A.3    Kershaw, M.H.4    Brinkworth, R.I.5
  • 91
    • 0024349230 scopus 로고
    • Adipsin and complement factor D activity: An immune-related defect in obesity
    • Rosen BS, Cook KS, Yaglon J, et al. Adipsin and complement factor D activity: An immune-related defect in obesity. Science 1989; 244: 1483-7.
    • (1989) Science , vol.244 , pp. 1483-1487
    • Rosen, B.S.1    Cook, K.S.2    Yaglon, J.3
  • 92
    • 0026794743 scopus 로고
    • Human adipsin is identical to complement factor D and is expressed at high levels in adipose tissue
    • White ET, Damm D, Hancock N, et al. Human adipsin is identical to complement factor D and is expressed at high levels in adipose tissue. J Biol Chem 1992; 267: 9210-3.
    • (1992) J Biol Chem , vol.267 , pp. 9210-9213
    • White, E.T.1    Damm, D.2    Hancock, N.3
  • 93
    • 0034885408 scopus 로고    scopus 로고
    • Murine hypodense eosinophils induce tumour cell apoptosis by a granzyme B-dependent mechanism
    • Costain DJ, Guha AK, Liwski RS, Lee TD. Murine hypodense eosinophils induce tumour cell apoptosis by a granzyme B-dependent mechanism. Cancer Immunol Immunother 2001; 50: 293-9.
    • (2001) Cancer Immunol Immunother , vol.50 , pp. 293-299
    • Costain, D.J.1    Guha, A.K.2    Liwski, R.S.3    Lee, T.D.4
  • 94
    • 0023126197 scopus 로고
    • Quantitation of histamine, tryptase, and chymase in dispersed human T and TC mast cells
    • Schwartz LB, Irani A-MA, Roller K, Castells MC, Schechter NM. Quantitation of histamine, tryptase, and chymase in dispersed human T and TC mast cells. J Immunol 1987; 138: 2611-5.
    • (1987) J Immunol , vol.138 , pp. 2611-2615
    • Schwartz, L.B.1    Irani, A.-M.A.2    Roller, K.3    Castells, M.C.4    Schechter, N.M.5
  • 96
    • 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 EJ, Silverman EK, Campbell MA. 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 1989; 143: 2961-8.
    • (1989) J Immunol , vol.143 , pp. 2961-2968
    • Campbell, E.J.1    Silverman, E.K.2    Campbell, M.A.3
  • 98
  • 99
    • 0024474186 scopus 로고
    • Detection of MCT and MCTC types of human mast cells by immunohistochemistry using new monoclonal anti-tryptase and antichymase antibodies
    • Irani AM, Bradford TR, Kepley CL, Schechter NM, Schwartz LB. Detection of MCT and MCTC types of human mast cells by immunohistochemistry using new monoclonal anti-tryptase and antichymase antibodies. J Histochem Cytochem 1989; 37: 1509-15.
    • (1989) J Histochem Cytochem , vol.37 , pp. 1509-1515
    • Irani, A.M.1    Bradford, T.R.2    Kepley, C.L.3    Schechter, N.M.4    Schwartz, L.B.5
  • 100
    • 0042377711 scopus 로고    scopus 로고
    • The human cytotoxic T cell granule serine protease granzyme H has chymotrypsin-like (chymase) activity and is taken up into cytoplasmic vesicles reminiscent of granzyme B-containing endosomes
    • Edwards KM, Kam CM, Powers JC, Trapani JA. The human cytotoxic T cell granule serine protease granzyme H has chymotrypsin-like (chymase) activity and is taken up into cytoplasmic vesicles reminiscent of granzyme B-containing endosomes. J Biol Chem 1999; 274: 30468-73.
    • (1999) J Biol Chem , vol.274 , pp. 30468-30473
    • Edwards, K.M.1    Kam, C.M.2    Powers, J.C.3    Trapani, J.A.4
  • 101
    • 0031836105 scopus 로고    scopus 로고
    • Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis
    • Belaaouaj A, McCarthy R, Baumann M, et al. Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis. Nat Med 1998; 4: 615-8.
    • (1998) Nat Med , vol.4 , pp. 615-618
    • Belaaouaj, A.1    McCarthy, R.2    Baumann, M.3
  • 102
    • 0034682860 scopus 로고    scopus 로고
    • Degradation of outer membrane protein A in Escherichia coli killing by neutrophil elastase
    • Belaaouaj A, Kim KS, Shapiro SD. Degradation of outer membrane protein A in Escherichia coli killing by neutrophil elastase. Science 2000; 289: 1185-8.
    • (2000) Science , vol.289 , pp. 1185-1188
    • Belaaouaj, A.1    Kim, K.S.2    Shapiro, S.D.3
  • 104
    • 0033986322 scopus 로고    scopus 로고
    • A critical role for neutrophil elastase in experimental bullous pemphigoid
    • Liu Z, Shapiro SD, Zhou X, et al. A critical role for neutrophil elastase in experimental bullous pemphigoid. J Clin Invest 2000; 105: 113-23.
    • (2000) J Clin Invest , vol.105 , pp. 113-123
    • Liu, Z.1    Shapiro, S.D.2    Zhou, X.3
  • 106
    • 0034117111 scopus 로고    scopus 로고
    • Acute cigarette smoke-induced connective tissue breakdown is mediated by neutrophils and prevented by α1-antitrypsin
    • Dhami R, Gilks B, Xie C, Zay K, Wright JL, Churg A. Acute cigarette smoke-induced connective tissue breakdown is mediated by neutrophils and prevented by α1-antitrypsin. Am J Respir Cell Mol Biol 2000; 22: 244-52.
    • (2000) Am J Respir Cell Mol Biol , vol.22 , pp. 244-252
    • Dhami, R.1    Gilks, B.2    Xie, C.3    Zay, K.4    Wright, J.L.5    Churg, A.6
  • 108
    • 0036800045 scopus 로고    scopus 로고
    • Synthetic serine elastase inhibitor reduces cigarette smoke-induced emphysema in guinea pigs
    • Wright JL, Farmer SG, Churg A. Synthetic serine elastase inhibitor reduces cigarette smoke-induced emphysema in guinea pigs. Am J Respir Crit Care Med 2002; 166: 954-60.
    • (2002) Am J Respir Crit Care Med , vol.166 , pp. 954-960
    • Wright, J.L.1    Farmer, S.G.2    Churg, A.3
  • 109
    • 0030823772 scopus 로고    scopus 로고
    • Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice
    • Hautamaki RD, Kobayashi DK, Senior RM, Shapiro SD. Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice. Science 1997; 277: 2002-4.
    • (1997) Science , vol.277 , pp. 2002-2004
    • Hautamaki, R.D.1    Kobayashi, D.K.2    Senior, R.M.3    Shapiro, S.D.4
  • 112
    • 20444433960 scopus 로고    scopus 로고
    • Serine protease cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering
    • Raptis SZ, Shapiro SD, Simmons PM, Cheng AM, Pham CT. Serine protease cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering. Immunity 2005; 22: 679-91.
    • (2005) Immunity , vol.22 , pp. 679-691
    • Raptis, S.Z.1    Shapiro, S.D.2    Simmons, P.M.3    Cheng, A.M.4    Pham, C.T.5
  • 113
    • 0034684681 scopus 로고    scopus 로고
    • Delayed expulsion of the nematode Trichinella spiralis in mice lacking the mucosal mast cell-specific granule chymase, mouse mast cell protease-1
    • Knight PA, Wright SH, Lawrence CE, Paterson YY, Miller HR. Delayed expulsion of the nematode Trichinella spiralis in mice lacking the mucosal mast cell-specific granule chymase, mouse mast cell protease-1. J Exp Med 2000; 192: 1849-56.
    • (2000) J Exp Med , vol.192 , pp. 1849-1856
    • Knight, P.A.1    Wright, S.H.2    Lawrence, C.E.3    Paterson, Y.Y.4    Miller, H.R.5
  • 114
    • 0029995317 scopus 로고    scopus 로고
    • Dog mastocytoma cells secrete a 92-kD gelatinase activated extracellularly by mast cell chymase
    • Fang KC, Raymond WW, Lazarus SC, Caughey GH. Dog mastocytoma cells secrete a 92-kD gelatinase activated extracellularly by mast cell chymase. J Clin Invest 1996; 97: 1589-96.
    • (1996) J Clin Invest , vol.97 , pp. 1589-1596
    • Fang, K.C.1    Raymond, W.W.2    Lazarus, S.C.3    Caughey, G.H.4
  • 115
    • 0035865351 scopus 로고    scopus 로고
    • Mast cell tissue inhibitor of metalloproteinase-1 is cleaved and inactivated extracellularly by α-chymase
    • Frank BT, Rossall JC, Caughey GH, Fang KC. Mast cell tissue inhibitor of metalloproteinase-1 is cleaved and inactivated extracellularly by α-chymase. J Immunol 2001; 166: 2783-92.
    • (2001) J Immunol , vol.166 , pp. 2783-2792
    • Frank, B.T.1    Rossall, J.C.2    Caughey, G.H.3    Fang, K.C.4
  • 116
    • 0033151608 scopus 로고    scopus 로고
    • Inflammatory mast cells upregulate angiogenesis during squamous epithelial carcinogenesis
    • Coussens LM, Raymond WW, Bergers G et al. Inflammatory mast cells upregulate angiogenesis during squamous epithelial carcinogenesis. Genes Develop 1999; 13: 1382-97.
    • (1999) Genes Develop , vol.13 , pp. 1382-1397
    • Coussens, L.M.1    Raymond, W.W.2    Bergers, G.3
  • 117
    • 15744388309 scopus 로고    scopus 로고
    • A key role for mast cell chymase in the activation of pro-matrix metalloprotease-9 and pro-matrix metalloprotease-2
    • Tchougounova E, Lundequist A, Fajardo I, Winberg JO, Abrink M, Pejler G. A key role for mast cell chymase in the activation of pro-matrix metalloprotease-9 and pro-matrix metalloprotease-2. J Biol Chem 2005; 280: 9291-6.
    • (2005) J Biol Chem , vol.280 , pp. 9291-9296
    • Tchougounova, E.1    Lundequist, A.2    Fajardo, I.3    Winberg, J.O.4    Abrink, M.5    Pejler, G.6
  • 118
    • 0035830852 scopus 로고    scopus 로고
    • Altered processing of fibronectin in mice lacking heparin. A role for heparin-dependent mast cell chymase in fibronectin degradation
    • Tchougounova E, Forsberg E, Angelborg G, Kjellen L, Pejler G. Altered processing of fibronectin in mice lacking heparin. A role for heparin-dependent mast cell chymase in fibronectin degradation. J Biol Chem 2001; 276: 3772-7.
    • (2001) J Biol Chem , vol.276 , pp. 3772-3777
    • Tchougounova, E.1    Forsberg, E.2    Angelborg, G.3    Kjellen, L.4    Pejler, G.5
  • 119
    • 0002079441 scopus 로고
    • Mast cell chymases and tryptases: Phylogeny, family relations and biogenesis
    • In: Caughey GH, editor. New York: Marcel Dekker
    • Caughey GH. Mast cell chymases and tryptases: Phylogeny, family relations and biogenesis. In: Caughey GH, editor. Mast Cell Proteases in Immunology and Biology. New York: Marcel Dekker, 1995. pp. 305-29.
    • (1995) Mast Cell Proteases in Immunology and Biology , pp. 305-329
    • Caughey, G.H.1
  • 120
    • 21044433149 scopus 로고    scopus 로고
    • Mast cell protease 5 mediates ischemia-reperfusion injury of mouse skeletal muscle
    • Abonia JP, Friend DS, Austen WG, Jr., et al. Mast cell protease 5 mediates ischemia-reperfusion injury of mouse skeletal muscle. J Immunol 2005; 174: 7285-91.
    • (2005) J Immunol , vol.174 , pp. 7285-7291
    • Abonia, J.P.1    Friend, D.S.2    Austen Jr., W.G.3
  • 122
    • 0027982477 scopus 로고
    • Lack of expression of the tryptase mouse mast cell protease 7 in mast cells of the C57BL/6J mouse
    • Ghildyal N, Friend DS, Freelund R, et al. Lack of expression of the tryptase mouse mast cell protease 7 in mast cells of the C57BL/6J mouse. J Immunol 1994; 153: 2624-30.
    • (1994) J Immunol , vol.153 , pp. 2624-2630
    • Ghildyal, N.1    Friend, D.S.2    Freelund, R.3
  • 126
    • 0035013541 scopus 로고    scopus 로고
    • Inhibition of mast cell tryptase by inhaled APC 366 attenuates allergen-induced late-phase airway obstruction in asthma
    • Krishna MT, Chauhan A, Little L, et al. Inhibition of mast cell tryptase by inhaled APC 366 attenuates allergen-induced late-phase airway obstruction in asthma. J Allergy Clin Immunol 2001; 107: 1039-45.
    • (2001) J Allergy Clin Immunol , vol.107 , pp. 1039-1045
    • Krishna, M.T.1    Chauhan, A.2    Little, L.3
  • 127
    • 0037083293 scopus 로고    scopus 로고
    • Tryptase inhibition blocks airway inflammation in a mouse asthma model
    • Oh S-W, Pae CI, Lee D-K, et al. Tryptase inhibition blocks airway inflammation in a mouse asthma model. J Immunol 2002; 168: 1992-2000.
    • (2002) J Immunol , vol.168 , pp. 1992-2000
    • Oh, S.-W.1    Pae, C.I.2    Lee, D.-K.3
  • 128
    • 0029088944 scopus 로고
    • Quantitative locus analysis of airway hyperresponsiveness in A/J and C57BL/6J mice
    • De Sanctis GT, Merchant M, Beier DR, et al. Quantitative locus analysis of airway hyperresponsiveness in A/J and C57BL/6J mice. Nat Genet 1995; 11: 150-4.
    • (1995) Nat Genet , vol.11 , pp. 150-154
    • De Sanctis, G.T.1    Merchant, M.2    Beier, D.R.3
  • 129
    • 0035854794 scopus 로고    scopus 로고
    • Evaluation of the substrate specificity of human mast cell tryptase βI and demonstration of its importance in bacterial infections of the lung
    • Huang C, De Sanctis GT, O'Brien PJ, et al. Evaluation of the substrate specificity of human mast cell tryptase βI and demonstration of its importance in bacterial infections of the lung. J Biol Chem 2001; 276: 26276-84.
    • (2001) J Biol Chem , vol.276 , pp. 26276-26284
    • Huang, C.1    De Sanctis, G.T.2    O'Brien, P.J.3
  • 130
    • 0029981928 scopus 로고    scopus 로고
    • Mast cell modulation of neutrophil influx and bacterial clearance at sites of infection through TNF-α
    • Malaviya R, Ikeda T, Ross E, Abraham SN. Mast cell modulation of neutrophil influx and bacterial clearance at sites of infection through TNF-α. Nature 1996; 381: 77-80.
    • (1996) Nature , vol.381 , pp. 77-80
    • Malaviya, R.1    Ikeda, T.2    Ross, E.3    Abraham, S.N.4
  • 131
    • 31944437499 scopus 로고    scopus 로고
    • Mast cells protect mice from mycoplasma pneumonia
    • Xu X, Zhang D, Lyubynska N, et al. Mast cells protect mice from mycoplasma pneumonia. Am J Respir Crit Care Med 2006; 173: 219-25.
    • (2006) Am J Respir Crit Care Med , vol.173 , pp. 219-225
    • Xu, X.1    Zhang, D.2    Lyubynska, N.3
  • 132
    • 0029083438 scopus 로고
    • Granzyme A-deficient mice retain potent cell-mediated toxicity
    • Ebnet K, Hausmann M, Lehmann-Grube F, et al. Granzyme A-deficient mice retain potent cell-mediated toxicity. EMBO J. 1995; 14: 4230-9.
    • (1995) EMBO J. , vol.14 , pp. 4230-4239
    • Ebnet, K.1    Hausmann, M.2    Lehmann-Grube, F.3
  • 133
    • 0030723209 scopus 로고    scopus 로고
    • In vitro- and ex vivo-derived cytolytic leukocytes from granzyme AxB double knockout mice are defective in granule-mediated apoptosis but not lysis of target cells
    • Simon MM, Hausmann M, Tran T, et al. In vitro- and ex vivo-derived cytolytic leukocytes from granzyme AxB double knockout mice are defective in granule-mediated apoptosis but not lysis of target cells. J Exp Med 1997; 186: 1781-6.
    • (1997) J Exp Med , vol.186 , pp. 1781-1786
    • Simon, M.M.1    Hausmann, M.2    Tran, T.3
  • 134
    • 0028258577 scopus 로고
    • Cytotoxic lymphocytes require granzyme B for the rapid induction of DNA fragmentation and apoptosis in allogeneic target cells
    • Heusel JW, Wesselschmidt RL, Shresta S, Russell JH, Ley TJ. Cytotoxic lymphocytes require granzyme B for the rapid induction of DNA fragmentation and apoptosis in allogeneic target cells. Cell 1994; 76: 977-87.
    • (1994) Cell , vol.76 , pp. 977-987
    • Heusel, J.W.1    Wesselschmidt, R.L.2    Shresta, S.3    Russell, J.H.4    Ley, T.J.5
  • 135
    • 0030014911 scopus 로고    scopus 로고
    • Granzyme A is critical for recovery from infection with the natural cytopathic viral pathogen, ectromelia
    • Mullbacher A, Ebnet K, Blanden RV, et al. Granzyme A is critical for recovery from infection with the natural cytopathic viral pathogen, ectromelia. Proc Natl Acad Sci USA 1996; 93: 5783-7.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5783-5787
    • Mullbacher, A.1    Ebnet, K.2    Blanden, R.V.3
  • 136
    • 0033598718 scopus 로고    scopus 로고
    • Granzymes are the essential downstream effector molecules for the control of primary virus infections by cytolytic leukocytes
    • Mullbacher A, Waring P, Tha Hla R, et al. Granzymes are the essential downstream effector molecules for the control of primary virus infections by cytolytic leukocytes. Proc Natl Acad Sci USA 1999; 96: 13950-5.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13950-13955
    • Mullbacher, A.1    Waring, P.2    Tha Hla, R.3
  • 137
    • 0034880940 scopus 로고    scopus 로고
    • Concerted action of the FasL/Fas and perforin/granzyme A and B pathways is mandatory for the development of early viral hepatitis but not for recovery from viral infection
    • Balkow S, Kersten A, Tran TT, et al. Concerted action of the FasL/Fas and perforin/granzyme A and B pathways is mandatory for the development of early viral hepatitis but not for recovery from viral infection. J Virol 2001; 75: 8781-91.
    • (2001) J Virol , vol.75 , pp. 8781-8791
    • Balkow, S.1    Kersten, A.2    Tran, T.T.3
  • 138
    • 0034033438 scopus 로고    scopus 로고
    • Murine cytomegalovirus replication in salivary glands is controlled by both perforin and granzymes during acute infection
    • Riera L, Gariglio M, Valente G, et al. Murine cytomegalovirus replication in salivary glands is controlled by both perforin and granzymes during acute infection. Eur J Immunol 2000; 30: 1350-5.
    • (2000) Eur J Immunol , vol.30 , pp. 1350-1355
    • Riera, L.1    Gariglio, M.2    Valente, G.3
  • 139
    • 23844461112 scopus 로고    scopus 로고
    • Functional analysis of granzyme M and its role in immunity to infection
    • Pao LI, Sumaria N, Kelly JM, et al. Functional analysis of granzyme M and its role in immunity to infection. J Immunol 2005; 175: 3235-43.
    • (2005) J Immunol , vol.175 , pp. 3235-3243
    • Pao, L.I.1    Sumaria, N.2    Kelly, J.M.3
  • 141
    • 13544266566 scopus 로고    scopus 로고
    • Granzyme B and the downstream granzymes C and/or F are important for cytotoxic lymphocyte functions
    • Revell PA, Grossman WJ, Thomas DA, et al. Granzyme B and the downstream granzymes C and/or F are important for cytotoxic lymphocyte functions. J Immunol 2005; 174: 2124-31.
    • (2005) J Immunol , vol.174 , pp. 2124-2131
    • Revell, P.A.1    Grossman, W.J.2    Thomas, D.A.3
  • 142
    • 0034488761 scopus 로고    scopus 로고
    • Crystal structure of the caspase activator human granzyme B, a proteinase highly specific for an Asp-P1 residue
    • Estebanez-Perpina E, Fuentes-Prior P, Belorgey D, et al. Crystal structure of the caspase activator human granzyme B, a proteinase highly specific for an Asp-P1 residue. Biol Chem 2000; 381: 1203-14.
    • (2000) Biol Chem , vol.381 , pp. 1203-1214
    • Estebanez-Perpina, E.1    Fuentes-Prior, P.2    Belorgey, D.3
  • 143
    • 0043047404 scopus 로고    scopus 로고
    • Transgenic mice that possess a disrupted mast cell protease 5 (mMCP-5) gene cannot store carboxypeptidase A in their granules
    • Stevens RL, Qui D, McNeill HP, et al. Transgenic mice that possess a disrupted mast cell protease 5 (mMCP-5) gene cannot store carboxypeptidase A in their granules. FASEB J 1996; 10: 1307.
    • (1996) FASEB J , vol.10 , pp. 1307
    • Stevens, R.L.1    Qui, D.2    McNeill, H.P.3
  • 144
    • 0344253682 scopus 로고    scopus 로고
    • Mast cell cathepsins C and S control levels of carboxypeptidase A and the chymase, mouse mast cell protease 5
    • Henningsson F, Wolters P, Chapman HA, Caughey GH, Pejler G. Mast cell cathepsins C and S control levels of carboxypeptidase A and the chymase, mouse mast cell protease 5. Biol Chem 2003; 384: 1527-31.
    • (2003) Biol Chem , vol.384 , pp. 1527-1531
    • Henningsson, F.1    Wolters, P.2    Chapman, H.A.3    Caughey, G.H.4    Pejler, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.