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Volumn , Issue , 2003, Pages 349-372

Mast cell proteases

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EID: 34248218881     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (1)

References (141)
  • 1
    • 14444279516 scopus 로고
    • Neutral proteases of mast cells
    • Hanson LA, Shakib F, eds., Basel: Karger
    • Schwartz LB. Neutral proteases of mast cells. In: Hanson LA, Shakib F, eds. Monographs in Allergy. Vol. 27. Basel: Karger, 1990:165.
    • (1990) Monographs in Allergy , vol.27 , pp. 165
    • Schwartz, L.B.1
  • 3
    • 0031157105 scopus 로고    scopus 로고
    • Of mites and men: Trypsin-like proteases in the lungs
    • Caughey GH. Of mites and men: Trypsin-like proteases in the lungs. Am J Respir CellMol Biol 1997; 16:621-628.
    • (1997) Am J Respir CellMol Biol , vol.16 , pp. 621-628
    • Caughey, G.H.1
  • 4
    • 0000018942 scopus 로고
    • Proteolytic enzymes of mast cells
    • Lagunoff D, Benditt EP. Proteolytic enzymes of mast cells. Ann NY Acad Sci 1963;103:185-198.
    • (1963) Ann NY Acad Sci , vol.103 , pp. 185-198
    • Lagunoff, D.1    Benditt, E.P.2
  • 5
    • 0000452039 scopus 로고
    • Histochemical demonstration of a species-specific trypsinlike enzyme in mast cells
    • Glenner GG, Cohen LA. Histochemical demonstration of a species-specific trypsinlike enzyme in mast cells. Nature 1960; 185:846-847.
    • (1960) Nature , vol.185 , pp. 846-847
    • Glenner, G.G.1    Cohen, L.A.2
  • 6
    • 0016685799 scopus 로고
    • Human skin proteases: Separation and characterization oftwo alkaline proteases, one splitting trypsin and the other chymotrypsin substrates
    • Fraki JE, Hopsu-Havu VK. Human skin proteases: Separation and characterization oftwo alkaline proteases, one splitting trypsin and the other chymotrypsin substrates.Arch Dermatol Res 1975; 253:261-276.
    • (1975) Arch Dermatol Res , vol.253 , pp. 261-276
    • Fraki, J.E.1    Hopsu-Havu, V.K.2
  • 7
    • 0017652842 scopus 로고
    • Human skin proteases: Effect of separated proteases on vascular permeabilityand leukocyte emigration in skin
    • Fraki JE. Human skin proteases: Effect of separated proteases on vascular permeabilityand leukocyte emigration in skin. Acta Dermatovener 1977; 57:393-398.
    • (1977) Acta Dermatovener , vol.57 , pp. 393-398
    • Fraki, J.E.1
  • 8
    • 0019888627 scopus 로고
    • Tryptase from human pulmonary mast cells.Purification and characterization
    • Schwartz LB, Lewis RA, Austen KF. Tryptase from human pulmonary mast cells.Purification and characterization. J Biol Chem 1981; 256:11939-11943.
    • (1981) J Biol Chem , vol.256 , pp. 11939-11943
    • Schwartz, L.B.1    Lewis, R.A.2    Austen, K.F.3
  • 9
    • 0021044821 scopus 로고
    • Mammalian tissue trypsin-like enzymes. Comparative reactivities of human skin tryptase, human lung tryptase, and bovine trypsin withpeptide 4-nitroanilide and thioester substrates
    • Tanaka T, McRae BJ, Cho K, et al. Mammalian tissue trypsin-like enzymes. Comparative reactivities of human skin tryptase, human lung tryptase, and bovine trypsin withpeptide 4-nitroanilide and thioester substrates. J Biol Chem 1983; 258:13552-13557.
    • (1983) J Biol Chem , vol.258 , pp. 13552-13557
    • Tanaka, T.1    McRae, B.J.2    Cho, K.3
  • 10
    • 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; 259:11046-11051.
    • (1984) J Biol Chem , vol.259 , pp. 11046-11051
    • Smith, T.J.1    Hougland, M.W.2    Johnson, D.A.3
  • 11
    • 0024328773 scopus 로고
    • Molecular cloning of dog mast celltryptase and a related protease: Structural evidence of a unique mode of serine proteaseactivation
    • Vanderslice P, Craik CS, Nadel JA, Caughey GH. Molecular cloning of dog mast celltryptase and a related protease: Structural evidence of a unique mode of serine proteaseactivation. Biochemistry 1989; 28:4148-4155.
    • (1989) Biochemistry , vol.28 , pp. 4148-4155
    • Vanderslice, P.1    Craik, C.S.2    Nadel, J.A.3    Caughey, G.H.4
  • 12
    • 0024434198 scopus 로고
    • Cloning and characterization of complementaryDNA for human tryptase
    • Miller JS, Westin EH, Schwartz LB. Cloning and characterization of complementaryDNA for human tryptase. J Clin Invest 1989; 84:1188-1195.
    • (1989) J Clin Invest , vol.84 , pp. 1188-1195
    • Miller, J.S.1    Westin, E.H.2    Schwartz, L.B.3
  • 15
    • 0029035748 scopus 로고
    • Quantitationof tryptase, chymase, FceRIa, and FceRIy mRNAs in human mast cells and basophilsby competitive reverse transcription-polymerase chain reaction
    • Xia H-Z, Kepley CL, Sakai K, Chelliah J, Irani A-M. A, Schwartz LB. Quantitationof tryptase, chymase, FceRIa, and FceRIy mRNAs in human mast cells and basophilsby competitive reverse transcription-polymerase chain reaction. J Immunol 1995; 154:5472-5480.
    • (1995) J Immunol , vol.154 , pp. 5472-5480
    • Xia, H.-Z.1    Kepley, C.L.2    Sakai, K.3    Chelliah, J.4    Irani, A.-M.A.5    Schwartz, L.B.6
  • 16
    • 0032212188 scopus 로고    scopus 로고
    • Identification of basophilic cells that express mast cellgranule proteases in the peripheral blood of asthma, allergy, and drug-reactive patients
    • Li L, Li Y, Reddel SW, et al. Identification of basophilic cells that express mast cellgranule proteases in the peripheral blood of asthma, allergy, and drug-reactive patients.J Immunol 1998; 161:5079-86.
    • (1998) J Immunol , vol.161 , pp. 5079-5086
    • Li, L.1    Li, Y.2    Reddel, S.W.3
  • 17
    • 0033525211 scopus 로고    scopus 로고
    • Characterization ofgenes encoding known and novel human mast cell tryptases on chromosome 16p 13.3
    • Pallaoro M, Fejzo MS, Shayesteh L, Blount JL, Caughey GH. Characterization ofgenes encoding known and novel human mast cell tryptases on chromosome 16p 13.3.J Biol Chem 1999; 274:3355-3362.
    • (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
  • 18
    • 0030068941 scopus 로고    scopus 로고
    • A novel heparin-dependent processing pathway forhuman tryptase: Autocatalysis followed by activation with dipeptidyl peptidase I
    • Sakai K, Ren S, Schwartz LB. A novel heparin-dependent processing pathway forhuman tryptase: Autocatalysis followed by activation with dipeptidyl peptidase I. J ClinInvest 1996; 97:988-995.
    • (1996) J ClinInvest , vol.97 , pp. 988-995
    • Sakai, K.1    Ren, S.2    Schwartz, L.B.3
  • 19
    • 0033538454 scopus 로고    scopus 로고
    • Human tryptases a and p/II are functionally distinctdue, in part, to a single amino acid difference in one of the surface loops that formsthe substrate-binding cleft
    • Huang C, Li L, Krilis SA, et al. Human tryptases a and p/II are functionally distinctdue, in part, to a single amino acid difference in one of the surface loops that formsthe substrate-binding cleft. J Biol Chem 1999; 274:19670-19676.
    • (1999) J Biol Chem , vol.274 , pp. 19670-19676
    • Huang, C.1    Li, L.2    Krilis, S.A.3
  • 20
    • 0028881815 scopus 로고
    • The alpha form of human tryptase is thepredominant type present in blood at baseline in normal subjects and is elevated inthose with systemic mastocytosis
    • Schwartz LB, Sakai K, Bradford TR, et al. The alpha form of human tryptase is thepredominant type present in blood at baseline in normal subjects and is elevated inthose with systemic mastocytosis. J Clin Invest 1995; 96:2702-2710.
    • (1995) J Clin Invest , vol.96 , pp. 2702-2710
    • Schwartz, L.B.1    Sakai, K.2    Bradford, T.R.3
  • 22
    • 0035798947 scopus 로고    scopus 로고
    • Constitutively raised serumconcentrations of mast-cell tryptase and severe anaphylactic reactions to Hymenopterastings
    • Ludolph-Hauser D, Rueff F, Fries C, Schopf P, Przybilla B. Constitutively raised serumconcentrations of mast-cell tryptase and severe anaphylactic reactions to Hymenopterastings. Lancet 2001; 357:361-362.
    • (2001) Lancet , vol.357 , pp. 361-362
    • Ludolph-Hauser, D.1    Rueff, F.2    Fries, C.3    Schopf, P.4    Przybilla, B.5
  • 23
    • 0033917596 scopus 로고    scopus 로고
    • Characterization of two highly polymorphic humantryptase loci and comparison with a newly discovered monkey tryptase ortholog
    • Guida M, Riedy M, Lee D, Hall J. Characterization of two highly polymorphic humantryptase loci and comparison with a newly discovered monkey tryptase ortholog. Pharmacogenetics 2000; 10:389-396.
    • (2000) Pharmacogenetics , vol.10 , pp. 389-396
    • Guida, M.1    Riedy, M.2    Lee, D.3    Hall, J.4
  • 24
    • 0034659960 scopus 로고    scopus 로고
    • Characterization of human y-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 y-tryptases, novel members of the chromosome 16p mast cell tryptase and prostasin gene families.J Immunol 2000; 164:6566-6575.
    • (2000) J Immunol , vol.164 , pp. 6566-6575
    • Caughey, G.H.1    Raymond, W.W.2    Blount, J.L.3
  • 25
    • 0019471330 scopus 로고
    • Acid hydrolases and tryptase fromsecretory granules of dispersed human lung mast cells
    • Schwartz LB, Lewis RA, Seldin D, Austen KF. Acid hydrolases and tryptase fromsecretory granules of dispersed human lung mast cells. J Immunol 1981; 126:1290-1294.
    • (1981) J Immunol , vol.126 , pp. 1290-1294
    • Schwartz, L.B.1    Lewis, R.A.2    Seldin, D.3    Austen, K.F.4
  • 26
    • 0035860703 scopus 로고    scopus 로고
    • Definition of the extended substrate specificitydeterminants for p-tryptases I and II
    • Harris JL, Niles A, Burdick K, et al. Definition of the extended substrate specificitydeterminants for p-tryptases I and II. J Biol Chem 2001; 276:34941-34947.
    • (2001) J Biol Chem , vol.276 , pp. 34941-34947
    • Harris, J.L.1    Niles, A.2    Burdick, K.3
  • 27
    • 2642600031 scopus 로고    scopus 로고
    • Human p-tryptase is a ring-liketetramer with active sites facing a central pore
    • Pereira PJB, Bergner A, Macedo-Ribeiro S, et al. Human p-tryptase is a ring-liketetramer with active sites facing a central pore. Nature 1998; 392:306-311.
    • (1998) Nature , vol.392 , pp. 306-311
    • Pereira, P.1    Bergner, A.2    Macedo-Ribeiro, S.3
  • 28
    • 0023875638 scopus 로고
    • Substance P and vasoactive intestinalpeptide degradation by mast cell tryptase and chymase
    • Caughey GH, Leidig F, Viro NF, Nadel JA. Substance P and vasoactive intestinalpeptide degradation by mast cell tryptase and chymase. J Pharmacol Exp Ther 1988;244:133-137.
    • (1988) J Pharmacol Exp Ther , vol.244 , pp. 133-137
    • Caughey, G.H.1    Leidig, F.2    Viro, N.F.3    Nadel, J.A.4
  • 29
    • 0025455517 scopus 로고
    • Degradation of airway neuropeptides by human lung tryptase
    • Tam EK, Caughey GH. Degradation of airway neuropeptides by human lung tryptase.Am J Respir Cell Mol Biol 1990; 3:27-32.
    • (1990) Am J Respir Cell Mol Biol , vol.3 , pp. 27-32
    • Tam, E.K.1    Caughey, G.H.2
  • 30
    • 0029964503 scopus 로고    scopus 로고
    • Induction of vascular permeabilityenhancement by human tryptase: Dependence on activation of prekallikrein and directrelease of bradykinin from kininogens
    • Imamura T, Dubin A, Moore W, Tanaka R, Travis J. Induction of vascular permeabilityenhancement by human tryptase: Dependence on activation of prekallikrein and directrelease of bradykinin from kininogens. Lab Invest 1996; 74:861-870.
    • (1996) Lab Invest , vol.74 , pp. 861-870
    • Imamura, T.1    Dubin, A.2    Moore, W.3    Tanaka, R.4    Travis, J.5
  • 31
    • 0032509201 scopus 로고    scopus 로고
    • Novelmechanism for bradykinin production at inflammatory sites. Diverse effects of a mixture of neutrophil elastase and mast cell tryptase versus tissue and plasma kallikreinson native and oxidized kininogens
    • Kozik A, Moore RB, Potempa J, Imamura T, Rapala-Kozik M, Travis J. A novelmechanism for bradykinin production at inflammatory sites. Diverse effects of a mixture of neutrophil elastase and mast cell tryptase versus tissue and plasma kallikreinson native and oxidized kininogens. J Biol Chem 1998; 273:33224-33229.
    • (1998) J Biol Chem , vol.273 , pp. 33224-33229
    • Kozik, A.1    Moore, R.B.2    Potempa, J.3    Imamura, T.4    Rapala-Kozik, M.5    Travis, J.A.6
  • 32
    • 0022388692 scopus 로고
    • The fibrinolytic activity ofpurified tryptase from human lung mast cells
    • Schwartz LB, Bradford TR, Littman BH, Wintroub BU. The fibrinolytic activity ofpurified tryptase from human lung mast cells. J Immunol 1985; 135:2762-2767.
    • (1985) J Immunol , vol.135 , pp. 2762-2767
    • Schwartz, L.B.1    Bradford, T.R.2    Littman, B.H.3    Wintroub, B.U.4
  • 33
    • 0024429920 scopus 로고
    • Synovial procollagenase activation byhuman mast cell tryptase. Dependence upon matrix metalloproteinase 3 activation
    • Gruber BL, Marchese MJ, Suzuki K, et al. Synovial procollagenase activation byhuman mast cell tryptase. Dependence upon matrix metalloproteinase 3 activation. JClin Invest 1989; 84:1657-1662.
    • (1989) JClin Invest , vol.84 , pp. 1657-1662
    • Gruber, B.L.1    Marchese, M.J.2    Suzuki, K.3
  • 34
    • 0028363122 scopus 로고
    • Human mast cell tryptase activates single-chain urinary-typeplasminogen activator (Pro-urokinase)
    • Stack MS, Johnson DA. Human mast cell tryptase activates single-chain urinary-typeplasminogen activator (pro-urokinase). J Biol Chem 1994; 269:9416-9419.
    • (1994) J Biol Chem , vol.269 , pp. 9416-9419
    • Stack, M.S.1    Johnson, D.A.2
  • 35
    • 1842414265 scopus 로고    scopus 로고
    • Mast cell tryptase regulates rat colonicmyocytes through proteinase-activated receptor 2
    • Corvera CU, Dery O, McConalogue K, et al. Mast cell tryptase regulates rat colonicmyocytes through proteinase-activated receptor 2. J Clin Invest 1997; 100:1383-1393.
    • (1997) J Clin Invest , vol.100 , pp. 1383-1393
    • Corvera, C.U.1    Dery, O.2    McConalogue, K.3
  • 36
    • 15444346942 scopus 로고    scopus 로고
    • Interactions of mast cell tryptase withthrombin receptors and PAR-2
    • Molino M, Barnathan ES, Numerof R, et al. Interactions of mast cell tryptase withthrombin receptors and PAR-2. J Biol Chem 1997; 272:4043-4049.
    • (1997) J Biol Chem , vol.272 , pp. 4043-4049
    • Molino, M.1    Barnathan, E.S.2    Numerof, R.3
  • 37
    • 0033971235 scopus 로고    scopus 로고
    • Agonists of proteinase-activated receptor2 induce inflammation by a neurogenic mechanism
    • Steinhoff M, Vergnolle N, Young SH, et al. Agonists of proteinase-activated receptor2 induce inflammation by a neurogenic mechanism. Nat Med 2000; 6:151-158.
    • (2000) Nat Med , vol.6 , pp. 151-158
    • Steinhoff, M.1    Vergnolle, N.2    Young, S.H.3
  • 38
    • 0035482476 scopus 로고    scopus 로고
    • Expression and function of proteinase-activatedreceptor 2 in human bronchial smooth muscle
    • Schmidlin F, Amadesi S, Vidil R, et al. Expression and function of proteinase-activatedreceptor 2 in human bronchial smooth muscle. Am J Respir Crit Care Med 2001; 164:1276-1281.
    • (2001) Am J Respir Crit Care Med , vol.164 , pp. 1276-1281
    • Schmidlin, F.1    Amadesi, S.2    Vidil, R.3
  • 39
    • 0034748449 scopus 로고    scopus 로고
    • Glycosylation and the activation of proteinase-activated receptor 2 (PAR(2)) by human mast cell tryptase
    • Compton SJ, Renaux B, Wijesuriya SJ, Hollenberg MD. Glycosylation and the activation of proteinase-activated receptor 2 (PAR(2)) by human mast cell tryptase. Br JPharmacol 2001; 134:705-718.
    • (2001) Br JPharmacol , vol.134 , pp. 705-718
    • Compton, S.J.1    Renaux, B.2    Wijesuriya, S.J.3    Hollenberg, M.D.4
  • 41
    • 0028820753 scopus 로고
    • Tryptase inhibitors block allergen-inducedairway and inflammatory responses in allergic sheep
    • Clark JM, Abraham WM, Fishman CE, et al. Tryptase inhibitors block allergen-inducedairway and inflammatory responses in allergic sheep. Am J Respir Crit Care Med1995; 152:2076-2083.
    • (1995) Am J Respir Crit Care Med , vol.152 , pp. 2076-2083
    • Clark, J.M.1    Abraham, W.M.2    Fishman, C.E.3
  • 42
    • 0031023694 scopus 로고    scopus 로고
    • Mast celltryptase potentiates histamine-induced contraction in human sensitized bronchus
    • Johnson PRA, Ammit AJ, Carlin SM, Armour CL, Caughey GH, Black JL. Mast celltryptase potentiates histamine-induced contraction in human sensitized bronchus. EurResp J 1997; 10:38-43.
    • (1997) EurResp J , vol.10 , pp. 38-43
    • Johnson, P.1    Ammit, A.J.2    Carlin, S.M.3    Armour, C.L.4    Caughey, G.H.5    Black, J.L.6
  • 43
    • 0033001630 scopus 로고    scopus 로고
    • Mast cell tryptase as a mediator of hyperresponsiveness in human isolated bronchi
    • Berger P, Compton SJ, Molimard M, et al. Mast cell tryptase as a mediator of hyperresponsiveness in human isolated bronchi. Clin Exp Allergy 1999; 29:804-812.
    • (1999) Clin Exp Allergy , vol.29 , pp. 804-812
    • Berger, P.1    Compton, S.J.2    Molimard, M.3
  • 45
    • 0025864033 scopus 로고
    • Mast cell tryptase is a mitogen for culturedfibroblasts
    • Ruoss SJ, Hartmann T, Caughey GH. Mast cell tryptase is a mitogen for culturedfibroblasts. J Clin Invest 1991; 88:493-499.
    • (1991) J Clin Invest , vol.88 , pp. 493-499
    • Ruoss, S.J.1    Hartmann, T.2    Caughey, G.H.3
  • 46
    • 0029354163 scopus 로고
    • Tryptase, thedominant secretory granular protein in humans mast cells, is a potent mitogen forcultured dog tracheal smooth muscle cells
    • Brown JK, Tyler CL, Jones CA, Ruoss SJ, Hartmann T, Caughey GH. Tryptase, thedominant secretory granular protein in humans mast cells, is a potent mitogen forcultured dog tracheal smooth muscle cells. Am J Respir Cell Mol Biol 1995; 13:227-236.
    • (1995) Am J Respir Cell Mol Biol , vol.13 , pp. 227-236
    • Brown, J.K.1    Tyler, C.L.2    Jones, C.A.3    Ruoss, S.J.4    Hartmann, T.5    Caughey, G.H.6
  • 47
    • 0030032558 scopus 로고    scopus 로고
    • Mast cell tryptase is a mitogen for epithelial cells—stimulationof IL-8 production and intercellular adhesion molecule-1 expression
    • Cairns JA, Walls AF. Mast cell tryptase is a mitogen for epithelial cells—stimulationof IL-8 production and intercellular adhesion molecule-1 expression. J Immunol 1996;156:275-283.
    • (1996) J Immunol , vol.156 , pp. 275-283
    • Cairns, J.A.1    Walls, A.F.2
  • 48
    • 0031091747 scopus 로고    scopus 로고
    • Human mast cells activate fibroblasts: Tryptaseis a fibrogenic factor stimulating collagen messenger ribonucleic acid synthesis andfibroblast chemotaxis
    • Gruber BL, Kew RR, Jelaska A, et al. Human mast cells activate fibroblasts: Tryptaseis a fibrogenic factor stimulating collagen messenger ribonucleic acid synthesis andfibroblast chemotaxis. J Immunol 1997; 158:2310-2317.
    • (1997) J Immunol , vol.158 , pp. 2310-2317
    • Gruber, B.L.1    Kew, R.R.2    Jelaska, A.3
  • 49
    • 0030952324 scopus 로고    scopus 로고
    • Mast cell tryptase stimulates synthesis of type I collagen inhuman lung fibroblasts
    • Cairns JA, Walls AF. Mast cell tryptase stimulates synthesis of type I collagen inhuman lung fibroblasts. J Clin Invest 1997; 99:1313-1321.
    • (1997) J Clin Invest , vol.99 , pp. 1313-1321
    • Cairns, J.A.1    Walls, A.F.2
  • 50
    • 0032562226 scopus 로고    scopus 로고
    • Human mast cell tryptase fibrino-genolysis: Kinetics, anticoagulation mechanism, and cell adhesion disruption
    • Thomas VA, Wheeless CJ, Stack MS, Johnson DA. Human mast cell tryptase fibrino-genolysis: Kinetics, anticoagulation mechanism, and cell adhesion disruption. Biochemistry 1998; 37:2291-2298.
    • (1998) Biochemistry , vol.37 , pp. 2291-2298
    • Thomas, V.A.1    Wheeless, C.J.2    Stack, M.S.3    Johnson, D.A.4
  • 51
    • 0032529228 scopus 로고    scopus 로고
    • The role of mast cell tryptase inregulating endothelial cell proliferation, cytokine release, and adhesion moleculeexpression: Tryptase induces expression of mRNA for IL-1 pand IL-8 and stimulatesthe selective release of IL-8 from human umbilical vein endothelial cells
    • Compton SJ, Cairns JA, Holgate ST, Walls AF. The role of mast cell tryptase inregulating endothelial cell proliferation, cytokine release, and adhesion moleculeexpression: Tryptase induces expression of mRNA for IL-1 pand IL-8 and stimulatesthe selective release of IL-8 from human umbilical vein endothelial cells. J Immunol1998; 161:1939-1946.
    • (1998) J Immunol , vol.161 , pp. 1939-1946
    • Compton, S.J.1    Cairns, J.A.2    Holgate, S.T.3    Walls, A.F.4
  • 52
    • 0030940777 scopus 로고    scopus 로고
    • Human mast cell tryptase: A stimulus of microvascular leakage andmast cell activation
    • He SH, Walls AF. Human mast cell tryptase: A stimulus of microvascular leakage andmast cell activation. Eur J Pharmacol 1997; 328:89-97.
    • (1997) Eur J Pharmacol , vol.328 , pp. 89-97
    • He, S.H.1    Walls, A.F.2
  • 53
    • 0035854794 scopus 로고    scopus 로고
    • Evaluation of the substrate specificity ofhuman mast cell tryptase p 1 and demonstration of its importance in bacterial infectionsof the lung
    • Huang C, De Sanctis GT, O’Brien PJ, et al. Evaluation of the substrate specificity ofhuman mast cell tryptase p 1 and demonstration of its importance in bacterial infectionsof the lung. J Biol Chem 2001; 276:26276-26284.
    • (2001) J Biol Chem , vol.276 , pp. 26276-26284
    • Huang, C.1    De Sanctis, G.T.2    O’Brien, P.J.3
  • 54
    • 0031010717 scopus 로고    scopus 로고
    • Human mast cells stimulate vascular tubeformation. Tryptase is a novel, potent angiogenic factor
    • Blair RJ, Meng H, Marchese MJ, et al. Human mast cells stimulate vascular tubeformation. Tryptase is a novel, potent angiogenic factor. J Clin Invest 1997; 99:2691-2700.
    • (1997) J Clin Invest , vol.99 , pp. 2691-2700
    • Blair, R.J.1    Meng, H.2    Marchese, M.J.3
  • 55
    • 0033151608 scopus 로고    scopus 로고
    • Inflammatory mast cells upregulateangiogenesis during squamous epithelial carcinogenesis
    • Coussens LM, Raymond WW, Bergers G, et al. Inflammatory mast cells upregulateangiogenesis during squamous epithelial carcinogenesis. Genes Dev 1999; 13:1382-1397.
    • (1999) Genes Dev , vol.13 , pp. 1382-1397
    • Coussens, L.M.1    Raymond, W.W.2    Bergers, G.3
  • 56
    • 0027759314 scopus 로고
    • Bis(5-amidino-2-benzimidazolyl)methane and related amidines are potent, reversible inhibitors of mastcell tryptases
    • Caughey GH, Raymond WW, Bacci E, Lombardy RJ, Tidwell RR. Bis(5-amidino-2-benzimidazolyl)methane and related amidines are potent, reversible inhibitors of mastcell tryptases. J Pharmacol Exp Therap 1993; 264:676-682.
    • (1993) J Pharmacol Exp Therap , vol.264 , pp. 676-682
    • Caughey, G.H.1    Raymond, W.W.2    Bacci, E.3    Lombardy, R.J.4    Tidwell, R.R.5
  • 57
    • 0026940256 scopus 로고
    • Inhibition of human mast cell tryptase bybenzamidine derivatives
    • Sturzebecher J, Prasa D, Sommerhoff CP. Inhibition of human mast cell tryptase bybenzamidine derivatives. Biol Chem Hoppe Seyler 1992; 373:1025-1030.
    • (1992) Biol Chem Hoppe Seyler , vol.373 , pp. 1025-1030
    • Sturzebecher, J.1    Prasa, D.2    Sommerhoff, C.P.3
  • 58
    • 0028942267 scopus 로고
    • Mammalian tissue trypsin-like enzymes:substrate specificity and inhibitory potency of substituted isocoumarin mechanism-based inhibitors, benzamidine derivatives, and arginine fluoroalkyl ketone transition-state inhibitors
    • Kam CM, Hernandez MA, Patil GS, et al. Mammalian tissue trypsin-like enzymes:substrate specificity and inhibitory potency of substituted isocoumarin mechanism-based inhibitors, benzamidine derivatives, and arginine fluoroalkyl ketone transition-state inhibitors. Arch Biochem Biophys 1995; 316:808-814.
    • (1995) Arch Biochem Biophys , vol.316 , pp. 808-814
    • Kam, C.M.1    Hernandez, M.A.2    Patil, G.S.3
  • 59
    • 0032484901 scopus 로고    scopus 로고
    • Design of potent selective zinc-mediatedserine protease inhibitors
    • Katz BA, Clark JM, Finer-Moore JS, et al. Design of potent selective zinc-mediatedserine protease inhibitors. Nature 1998; 391:608-612.
    • (1998) Nature , vol.391 , pp. 608-612
    • Katz, B.A.1    Clark, J.M.2    Finer-Moore, J.S.3
  • 60
    • 0034712661 scopus 로고    scopus 로고
    • A novel approachto serine protease inhibition: Kinetic characterization of inhibitors whose potencies andselectivities are dramatically enhanced by zinc(II)
    • Janc JW, Clark JM, Warne RL, Elrod KC, Katz BA, Moore WR. A novel approachto serine protease inhibition: Kinetic characterization of inhibitors whose potencies andselectivities are dramatically enhanced by zinc(II). Biochemistry 2000; 39:4792-4800.
    • (2000) Biochemistry , vol.39 , pp. 4792-4800
    • Janc, J.W.1    Clark, J.M.2    Warne, R.L.3    Elrod, K.C.4    Katz, B.A.5    Moore, W.R.6
  • 61
    • 0000498068 scopus 로고    scopus 로고
    • Effect of inhaled APC 366 on allergen-induced bronchoconstriction and airway hyperresponsiveness to histamine in atopicsubjects
    • Krishna MT, Chauhan AJ, Little L, et al. Effect of inhaled APC 366 on allergen-induced bronchoconstriction and airway hyperresponsiveness to histamine in atopicsubjects. Am J Respir Crit Care Med. 1998; 157:A456.
    • (1998) Am J Respir Crit Care Med , vol.157 , pp. A456
    • Krishna, M.T.1    Chauhan, A.J.2    Little, L.3
  • 62
    • 0034675757 scopus 로고    scopus 로고
    • Dibasic inhibitors of human mast cell tryptase.Part 2: Structure-activity relationships and requirements for potent activity
    • Rice KD, Wang VR, Gangloff AR, et al. Dibasic inhibitors of human mast cell tryptase.Part 2: Structure-activity relationships and requirements for potent activity. BioorgMed Chem Lett 2000; 10:2361-2366.
    • (2000) BioorgMed Chem Lett , vol.10 , pp. 2361-2366
    • Rice, K.D.1    Wang, V.R.2    Gangloff, A.R.3
  • 63
    • 13044313485 scopus 로고    scopus 로고
    • Potent selective nonpeptidic inhibitors ofhuman lung tryptase
    • Burgess LE, Newhouse BJ, Ibrahim P, et al. Potent selective nonpeptidic inhibitors ofhuman lung tryptase. Proc Natl Acad Sci USA 1999; 96:8348-8352.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8348-8352
    • Burgess, L.E.1    Newhouse, B.J.2    Ibrahim, P.3
  • 64
    • 0035033274 scopus 로고    scopus 로고
    • Bivalent inhibition of human p-tryptase
    • Schaschke N, Matschiner G, Zettl F, et al. Bivalent inhibition of human p-tryptase.Chem Biol 2001; 8:313-327.
    • (2001) Chem Biol , vol.8 , pp. 313-327
    • Schaschke, N.1    Matschiner, G.2    Zettl, F.3
  • 66
    • 0032742390 scopus 로고    scopus 로고
    • Inhibition of allergen-induced pulmonaryresponses by the selective tryptase inhibitor 1,5-bis-[4-[(3-carbamimidoyl-benzenesul-fonylamino)-methyl] -phenoxy]-pentane (AMG-126737)
    • Wright CD, Havill AM, Middleton SC, et al. Inhibition of allergen-induced pulmonaryresponses by the selective tryptase inhibitor 1,5-bis-[4-[(3-carbamimidoyl-benzenesul-fonylamino)-methyl] -phenoxy]-pentane (AMG-126737). Biochem Pharmacol 1999;58:1989-1996.
    • (1999) Biochem Pharmacol , vol.58 , pp. 1989-1996
    • Wright, C.D.1    Havill, A.M.2    Middleton, S.C.3
  • 67
    • 0032548001 scopus 로고    scopus 로고
    • 1,2-Benzisothiazol-3-one 1,1-dioxideinhibitors of human mast cell tryptase
    • Combrink KD, HB GI, Meanwell NA, et al. 1,2-Benzisothiazol-3-one 1,1-dioxideinhibitors of human mast cell tryptase. J Med Chem 1998; 41:4854-4860.
    • (1998) J Med Chem , vol.41 , pp. 4854-4860
    • Combrink, K.D.1    Hb, G.I.2    Meanwell, N.A.3
  • 68
    • 0028520933 scopus 로고
    • A Kazal-type inhibitor of human mast cell tryptase: Isolation from the medicinal leechHirudo medicinalis, characterization, and sequence analysis
    • Sommerhoff CP, Sollner C, Mentele R, Piechottka GP, Auerswald EA, Fritz H. A Kazal-type inhibitor of human mast cell tryptase: Isolation from the medicinal leechHirudo medicinalis, characterization, and sequence analysis. Biol Chem Hoppe-Seyler1994; 375:685-694.
    • (1994) Biol Chem Hoppe-Seyler , vol.375 , pp. 685-694
    • Sommerhoff, C.P.1    Sollner, C.2    Mentele, R.3    Piechottka, G.P.4    Auerswald, E.A.5    Fritz, H.6
  • 69
    • 0030754090 scopus 로고    scopus 로고
    • The three-dimensional structure ofrecombinant leech-derived tryptase inhibitor in complex with trypsin. Implications forthe structure of human mast cell tryptase and its inhibition
    • Stubbs MT, Morenweiser R, Sturzebecher J, et al. The three-dimensional structure ofrecombinant leech-derived tryptase inhibitor in complex with trypsin. Implications forthe structure of human mast cell tryptase and its inhibition. J Biol Chem 1997; 272:19931-19937.
    • (1997) J Biol Chem , vol.272 , pp. 19931-19937
    • Stubbs, M.T.1    Morenweiser, R.2    Sturzebecher, J.3
  • 70
    • 0030744683 scopus 로고    scopus 로고
    • Lactoferrin, a potent tryptaseinhibitor, abolishes late-phase airway responses in allergic sheep
    • Elrod KC, Moore WR, Abraham WM, Tanaka RD. Lactoferrin, a potent tryptaseinhibitor, abolishes late-phase airway responses in allergic sheep. Am J Respir CritCare Med 1997; 156:375-381.
    • (1997) Am J Respir CritCare Med , vol.156 , pp. 375-381
    • Elrod, K.C.1    Moore, W.R.2    Abraham, W.M.3    Tanaka, R.D.4
  • 71
    • 0033150593 scopus 로고    scopus 로고
    • Neutrophil myeloperoxidase is a potentand selective inhibitor of mast cell tryptase
    • Cregar L, Elrod KC, Putnam D, Moore WR. Neutrophil myeloperoxidase is a potentand selective inhibitor of mast cell tryptase. Arch Biochem Biophys 1999; 366:125-130.
    • (1999) Arch Biochem Biophys , vol.366 , pp. 125-130
    • Cregar, L.1    Elrod, K.C.2    Putnam, D.3    Moore, W.R.4
  • 72
    • 0032741435 scopus 로고    scopus 로고
    • Identification of a new member of the tryptasefamily of mouse and human mast cell proteases which possesses a novel COOH-terminal hydrophobic extension
    • Wong GW, Tang Y, Feyfant E, et al. Identification of a new member of the tryptasefamily of mouse and human mast cell proteases which possesses a novel COOH-terminal hydrophobic extension. J Biol Chem 1999; 274:30784-30793.
    • (1999) J Biol Chem , vol.274 , pp. 30784-30793
    • Wong, G.W.1    Tang, Y.2    Feyfant, E.3
  • 73
    • 0023214640 scopus 로고
    • Molecular cloningof human cathepsin G: Structural similarity to mast cell and cytotoxic T lymphocyteproteinases
    • Salvesen G, Farley D, Shuman J, Przybyla A, Reilly C, Travis J. Molecular cloningof human cathepsin G: Structural similarity to mast cell and cytotoxic T lymphocyteproteinases. Biochemistry 1987; 26:2289-2293.
    • (1987) Biochemistry , vol.26 , pp. 2289-2293
    • Salvesen, G.1    Farley, D.2    Shuman, J.3    Przybyla, A.4    Reilly, C.5    Travis, J.6
  • 74
    • 0025835534 scopus 로고
    • Structure, chromosomal assignment, anddeduced amino acid sequence of a human gene for mast cell chymase
    • Caughey GH, Zerweck EH, Vanderslice P. Structure, chromosomal assignment, anddeduced amino acid sequence of a human gene for mast cell chymase. J Biol Chem1991; 266:12956-12963.
    • (1991) J Biol Chem , vol.266 , pp. 12956-12963
    • Caughey, G.H.1    Zerweck, E.H.2    Vanderslice, P.3
  • 75
    • 0029853820 scopus 로고    scopus 로고
    • The 1.8 A crystal structure of human cathepsin G incomplex with Suc-Val-Pro-PheP-(OPh)2: A Janus-faced proteinase with two oppositespecificities
    • Hof P, Mayr I, Huber R, et al. The 1.8 A crystal structure of human cathepsin G incomplex with Suc-Val-Pro-PheP-(OPh)2: A Janus-faced proteinase with two oppositespecificities. EMBO J 1996; 15:5481-5491.
    • (1996) EMBO J , vol.15 , pp. 5481-5491
    • Hof, P.1    Mayr, I.2    Huber, R.3
  • 76
    • 0033547878 scopus 로고    scopus 로고
    • The 2.2 A crystal structure of human chymasein complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: Structural explanationfor its dipeptidyl carboxypeptidase specificity
    • Pereira PJB, Wang ZM, Rubin H, et al. The 2.2 A crystal structure of human chymasein complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: Structural explanationfor its dipeptidyl carboxypeptidase specificity. J Mol Biol 1999; 286:163-173.
    • (1999) J Mol Biol , vol.286 , pp. 163-173
    • Pereira, P.1    Wang, Z.M.2    Rubin, H.3
  • 77
    • 0027415378 scopus 로고
    • The human mast cell chymasegene (CMA1): Mapping to the cathepsin G/granzyme gene cluster and lineage-restrictedexpression
    • Caughey GH, Schaumberg TH, Zerweck EH, et al. The human mast cell chymasegene (CMA1): Mapping to the cathepsin G/granzyme gene cluster and lineage-restrictedexpression. Genomics 1993; 15:614-620.
    • (1993) Genomics , vol.15 , pp. 614-620
    • Caughey, G.H.1    Schaumberg, T.H.2    Zerweck, E.H.3
  • 80
    • 0031910094 scopus 로고    scopus 로고
    • Mast cell chymase-like protease(S)modulates Escherichia coli lipopolysaccharide-induced vasomotor dysfunction in skeletal muscle in vivo
    • Suzuki H, Caughey GH, Gao X-P, Rubinstein I. Mast cell chymase-like protease(s)modulates Escherichia coli lipopolysaccharide-induced vasomotor dysfunction in skeletal muscle in vivo. J Pharmacol Exp Therap 1998; 284:1156-1164.
    • (1998) J Pharmacol Exp Therap , vol.284 , pp. 1156-1164
    • Suzuki, H.1    Caughey, G.H.2    Gao, X.-P.3    Rubinstein, I.4
  • 81
    • 0033514908 scopus 로고    scopus 로고
    • Tranilast suppresses vascular chymase expressionand neointima formation in balloon-injured dog carotid artery
    • Shiota N, Okunishi H, Takai S, et al. Tranilast suppresses vascular chymase expressionand neointima formation in balloon-injured dog carotid artery. Circulation 1999; 99:1084-1090.
    • (1999) Circulation , vol.99 , pp. 1084-1090
    • Shiota, N.1    Okunishi, H.2    Takai, S.3
  • 82
    • 0027240447 scopus 로고
    • Catabolism of intact type VI collagen microfibrils: Susceptibility to degradation by serine proteinases
    • Kielty CM, Lees M, Shuttleworth CA, Woolley D. Catabolism of intact type VI collagen microfibrils: Susceptibility to degradation by serine proteinases. Biochem BiophysRes Commun 1993; 191:1230-1236.
    • (1993) Biochem BiophysRes Commun , vol.191 , pp. 1230-1236
    • Kielty, C.M.1    Lees, M.2    Shuttleworth, C.A.3    Woolley, D.4
  • 83
    • 0028956737 scopus 로고
    • Human mast cell chymaseand leukocyte elastase release latent transforming growth factor-p 1 from the extracellular matrix of cultured human epithelial and endothelial cells
    • Taipale J, Lohi J, Saarinen J, Kovanen PT, Keski-Oja J. Human mast cell chymaseand leukocyte elastase release latent transforming growth factor-p 1 from the extracellular matrix of cultured human epithelial and endothelial cells. J Biol Chem 1995; 270:4689-4696.
    • (1995) J Biol Chem , vol.270 , pp. 4689-4696
    • Taipale, J.1    Lohi, J.2    Saarinen, J.3    Kovanen, P.T.4    Keski-Oja, J.5
  • 84
    • 0031571260 scopus 로고    scopus 로고
    • Selective conversion of big endothelins to tracheal smooth muscle-constricting 31-amino acid-lengthendothelins by chymase from human mast cells
    • Nakano A, Kishi F, Minami K, Wakabayashi H, Nakaya Y, Kido H. Selective conversion of big endothelins to tracheal smooth muscle-constricting 31-amino acid-lengthendothelins by chymase from human mast cells. J Immunol 1997; 159:1987-1992.
    • (1997) J Immunol , vol.159 , pp. 1987-1992
    • Nakano, A.1    Kishi, F.2    Minami, K.3    Wakabayashi, H.4    Nakaya, Y.5    Kido, H.6
  • 86
    • 0026606459 scopus 로고
    • Mast cell proteoglycans modulate the secretagogue, proteoglycanase, and amidolytic activities of dog mast cell chymase
    • Sommerhoff CP, Ruoss SJ, Caughey GH. Mast cell proteoglycans modulate the secretagogue, proteoglycanase, and amidolytic activities of dog mast cell chymase. J Immunol1992; 148:2859-2866.
    • (1992) J Immunol , vol.148 , pp. 2859-2866
    • Sommerhoff, C.P.1    Ruoss, S.J.2    Caughey, G.H.3
  • 87
    • 0034801226 scopus 로고    scopus 로고
    • Design, synthesis and pharmacological evaluationof 3-benzylazetidine-2-one-based human chymase inhibitors
    • Aoyama Y, Uenaka M, Kii M, et al. Design, synthesis and pharmacological evaluationof 3-benzylazetidine-2-one-based human chymase inhibitors. Bioorg Med Chem 2001;9:3065-3075.
    • (2001) Bioorg Med Chem , vol.9 , pp. 3065-3075
    • Aoyama, Y.1    Uenaka, M.2    Kii, M.3
  • 88
    • 0035848580 scopus 로고    scopus 로고
    • Synthesis, structure-activity relationships, and pharmacokinetic profiles of nonpeptidic difluoromethylene ketones as novel inhibitors of human chymase
    • Akahoshi F, Ashimori A, Sakashita H, et al. Synthesis, structure-activity relationships, and pharmacokinetic profiles of nonpeptidic difluoromethylene ketones as novel inhibitors of human chymase. J Med Chem 2001; 44:1297-1304.
    • (2001) J Med Chem , vol.44 , pp. 1297-1304
    • Akahoshi, F.1    Ashimori, A.2    Sakashita, H.3
  • 89
    • 0033517091 scopus 로고    scopus 로고
    • Human chymase inhibitorsbased on the 1,2,5-thiadiazolidin-3-one-1, 1-dioxide scaffold
    • Groutas WC, Schechter NM, He S, Yu H, Huang P, Tu J. Human chymase inhibitorsbased on the 1,2,5-thiadiazolidin-3-one-1, 1-dioxide scaffold. Bioorg Med Chem Lett1999; 9:2199-2204.
    • (1999) Bioorg Med Chem Lett , vol.9 , pp. 2199-2204
    • Groutas, W.C.1    Schechter, N.M.2    He, S.3    Yu, H.4    Huang, P.5    Tu, J.6
  • 90
    • 0033555724 scopus 로고    scopus 로고
    • The mast cell as site of tissue-type plasminogen activator expression and fibrinolysis
    • Sillaber C, Baghestanian M, Bevec D, et al. The mast cell as site of tissue-type plasminogen activator expression and fibrinolysis. J Immunol 1999; 162:1032-1041.
    • (1999) J Immunol , vol.162 , pp. 1032-1041
    • Sillaber, C.1    Baghestanian, M.2    Bevec, D.3
  • 91
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissueremodeling
    • Woessner JF, Jr. Matrix metalloproteinases and their inhibitors in connective tissueremodeling. FASEB J 1991; 5:2145-2154.
    • (1991) FASEB J , vol.5 , pp. 2145-2154
    • Woessner, J.F.1
  • 92
    • 0032038574 scopus 로고    scopus 로고
    • Mast cell collagenase correlates with regression of pulmonary vascular remodeling in the rat
    • Tozzi CA, Thakker-Varia S, Yu SY, et al. Mast cell collagenase correlates with regression of pulmonary vascular remodeling in the rat. Am J Respir Cell Mol Biol 1998;18:497-510.
    • (1998) Am J Respir Cell Mol Biol , vol.18 , pp. 497-510
    • Tozzi, C.A.1    Thakker-Varia, S.2    Yu, S.Y.3
  • 93
    • 0033214269 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 production, a newly identified function of mast cell progenitors, is downregulated by c-kit receptoractivation
    • Tanaka A, Arai K, Kitamura Y, Matsuda H. Matrix metalloproteinase-9 production, a newly identified function of mast cell progenitors, is downregulated by c-kit receptoractivation. Blood 1999; 94:2390-2395.
    • (1999) Blood , vol.94 , pp. 2390-2395
    • Tanaka, A.1    Arai, K.2    Kitamura, Y.3    Matsuda, H.4
  • 95
    • 0029011698 scopus 로고
    • Immunolocalization of stromelysin-relatedprotein in murine mast cell granules
    • Brownell E, Fiorentino L, Jolly G, et al. Immunolocalization of stromelysin-relatedprotein in murine mast cell granules. Int Arch Allergy Immunol 1995; 107:333-335.
    • (1995) Int Arch Allergy Immunol , vol.107 , pp. 333-335
    • Brownell, E.1    Fiorentino, L.2    Jolly, G.3
  • 96
    • 0029995317 scopus 로고    scopus 로고
    • Dog mastocytoma cells secretea 92-kD gelatinase activated extracellularly by mast cell chymase
    • Fang KC, Raymond WW, Lazarus SC, Caughey GH. Dog mastocytoma cells secretea 92-kD gelatinase activated extracellularly by mast cell chymase. J Clin Invest 1996;97:1589-1596.
    • (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
  • 97
    • 0030845183 scopus 로고    scopus 로고
    • Dog mast cell a-chymase activatesprogelatinase B by cleaving the Phe88-Gln89 and Phe91-Glu92 bonds of the catalyticdomain
    • 92 bonds of the catalyticdomain. J Biol Chem 1997; 272:25628-25635.
    • (1997) J Biol Chem , vol.272 , pp. 25628-25635
    • Fang, K.C.1    Raymond, W.W.2    Blount, J.L.3    Caughey, G.H.4
  • 99
    • 0035865351 scopus 로고    scopus 로고
    • Mast cell tissue inhibitor of metalloproteinase-1 is cleaved and inactivated extracellularly by a-chymase
    • Frank BT, Rossall JC, Caughey GH, Fang KC. Mast cell tissue inhibitor of metalloproteinase-1 is cleaved and inactivated extracellularly by a-chymase. J Immunol 2001;166:2783-2792.
    • (2001) J Immunol , vol.166 , pp. 2783-2792
    • Frank, B.T.1    Rossall, J.C.2    Caughey, G.H.3    Fang, K.C.4
  • 100
    • 0033777688 scopus 로고    scopus 로고
    • In vitro and in vivo expression of interstitial collagenase/MMP-1 by human mast cells
    • Di Girolamo N, Wakefield D. In vitro and in vivo expression of interstitial collagenase/MMP-1 by human mast cells. Dev Immunol 2000; 7:131-142.
    • (2000) Dev Immunol , vol.7 , pp. 131-142
    • Di Girolamo, N.1    Wakefield, D.2
  • 102
    • 0028794828 scopus 로고
    • Activation of precursorsfor matrix metalloproteinases 1 (Interstitial collagenase) and 3 (stromelysin) by ratmast-cell proteinases I and II
    • Suzuki K, Lees M, Newlands GF, Nagase H, Woolley DE. Activation of precursorsfor matrix metalloproteinases 1 (interstitial collagenase) and 3 (stromelysin) by ratmast-cell proteinases I and II. Biochem J 1995; 305:301-306.
    • (1995) Biochem J , vol.305 , pp. 301-306
    • Suzuki, K.1    Lees, M.2    Newlands, G.F.3    Nagase, H.4    Woolley, D.E.5
  • 103
    • 0028302145 scopus 로고
    • Mast cell proteinases activate precursor forms ofcollagenase and stromelysin, but not of gelatinases A and B
    • Lees M, Taylor DJ, Woolley DE. Mast cell proteinases activate precursor forms ofcollagenase and stromelysin, but not of gelatinases A and B. Eur J Biochem 1994;223:171-177.
    • (1994) Eur J Biochem , vol.223 , pp. 171-177
    • Lees, M.1    Taylor, D.J.2    Woolley, D.E.3
  • 104
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation ofmetalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • Van Wart HE, Birkedal-Hansen H. The cysteine switch: A principle of regulation ofmetalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci USA 1990; 87:5578-5582.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 105
    • 0026660964 scopus 로고
    • Matrix metalloproteinase 3 (Stromelysin) activatesthe precursor for the human matrix metalloproteinase 9
    • Ogata Y, Enghild JJ, Nagase H. Matrix metalloproteinase 3 (stromelysin) activatesthe precursor for the human matrix metalloproteinase 9. J Biol Chem 1992; 267:3581-3584.
    • (1992) J Biol Chem , vol.267 , pp. 3581-3584
    • Ogata, Y.1    Enghild, J.J.2    Nagase, H.3
  • 106
    • 0029034457 scopus 로고
    • Activation of progelatinase B (MMP-9)by gelatinase A (MMP-2)
    • Fridman R, Toth M, Pena D, Mobashery S. Activation of progelatinase B (MMP-9)by gelatinase A (MMP-2). Cancer Res 1995; 55:2548-2555.
    • (1995) Cancer Res , vol.55 , pp. 2548-2555
    • Fridman, R.1    Toth, M.2    Pena, D.3    Mobashery, S.4
  • 107
    • 0021918104 scopus 로고
    • Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase
    • Hibbs MS, Hasty KA, Seyer JM, Kang AH, Mainardi CL. Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase. J Biol Chem1985; 260:2493-2500.
    • (1985) J Biol Chem , vol.260 , pp. 2493-2500
    • Hibbs, M.S.1    Hasty, K.A.2    Seyer, J.M.3    Kang, A.H.4    Mainardi, C.L.5
  • 108
    • 0035477996 scopus 로고    scopus 로고
    • Human mastcells release metalloproteinase-9 on contact with activated t cells: Juxtacrine regulationby TNF-alpha
    • Baram D, Vaday GG, Salamon P, Drucker I, Hershkoviz R, Mekori YA. Human mastcells release metalloproteinase-9 on contact with activated t cells: Juxtacrine regulationby TNF-alpha. J Immunol 2001; 167:4008-4016.
    • (2001) J Immunol , vol.167 , pp. 4008-4016
    • Baram, D.1    Vaday, G.G.2    Salamon, P.3    Drucker, I.4    Hershkoviz, R.5    Mekori, Y.A.6
  • 109
    • 0035406562 scopus 로고    scopus 로고
    • MatsudaH. Mast cell MMP-9 production enhanced by bacteriallipopolysaccharide
    • Tanaka A, Yamane Y, MatsudaH. Mast cell MMP-9 production enhanced by bacteriallipopolysaccharide. J Vet Med Sci 2001; 63:811-813.
    • (2001) J Vet Med Sci , vol.63 , pp. 811-813
    • Tanaka, A.1    Yamane, Y.2
  • 110
    • 0027420678 scopus 로고
    • Structural and functional heterogeneity among peroxidase-negative granules in human neutrophils: Identification of adistinct gelatinase-containing granule subset by combined immunocytochemistry andsubcellular fractionation
    • Kjeldsen L, Bainton DF, Sengelov H, Borregaard N. Structural and functional heterogeneity among peroxidase-negative granules in human neutrophils: Identification of adistinct gelatinase-containing granule subset by combined immunocytochemistry andsubcellular fractionation. Blood 1993; 82:3183-3191.
    • (1993) Blood , vol.82 , pp. 3183-3191
    • Kjeldsen, L.1    Bainton, D.F.2    Sengelov, H.3    Borregaard, N.4
  • 111
    • 0031753315 scopus 로고    scopus 로고
    • Bronchial subepithelial fibrosisand expression of matrix metalloproteinase-9 in asthmatic airway inflammation
    • Hoshino M, Nakamura Y, Sim J, Shimojo J, Isogai S. Bronchial subepithelial fibrosisand expression of matrix metalloproteinase-9 in asthmatic airway inflammation. J Allergy Clin Immunol 1998; 102:783-788.
    • (1998) J Allergy Clin Immunol , vol.102 , pp. 783-788
    • Hoshino, M.1    Nakamura, Y.2    Sim, J.3    Shimojo, J.4    Isogai, S.5
  • 112
    • 0032784215 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-1 levels in bronchoalveolar lavage fluid from asthmatic subjects
    • Mautino G, Henriquet C, Jaffuel D, Bousquet J, Capony F. Tissue inhibitor of metalloproteinase-1 levels in bronchoalveolar lavage fluid from asthmatic subjects. Am JRespir Crit Care Med 1999; 160:324-330.
    • (1999) Am JRespir Crit Care Med , vol.160 , pp. 324-330
    • Mautino, G.1    Henriquet, C.2    Jaffuel, D.3    Bousquet, J.4    Capony, F.5
  • 113
    • 0032417102 scopus 로고    scopus 로고
    • Sputum metalloproteinase-9/tissue inhibitor of metalloproteinase-1 ratio correlates with airflow obstruction in asthma andchronic bronchitis
    • Vignola AM, Riccobono L, Mirabella A, et al. Sputum metalloproteinase-9/tissue inhibitor of metalloproteinase-1 ratio correlates with airflow obstruction in asthma andchronic bronchitis. Am J Respir Crit Care Med 1998; 158:1945-1950.
    • (1998) Am J Respir Crit Care Med , vol.158 , pp. 1945-1950
    • Vignola, A.M.1    Riccobono, L.2    Mirabella, A.3
  • 114
    • 0032906774 scopus 로고    scopus 로고
    • Contribution of 92 kDa gelatinase/type IVcollagenase in bronchial inflammation during status asthmaticus
    • Lemjabbar H, Gosset P, Lamblin C, et al. Contribution of 92 kDa gelatinase/type IVcollagenase in bronchial inflammation during status asthmaticus. Am J Respir CritCare Med 1999; 159:1298-1307.
    • (1999) Am J Respir CritCare Med , vol.159 , pp. 1298-1307
    • Lemjabbar, H.1    Gosset, P.2    Lamblin, C.3
  • 115
    • 0034502357 scopus 로고    scopus 로고
    • Proteinase-activated receptor-2-mediated matrix metalloproteinase-9 release from airway epithelial cells
    • Vliagoftis H, Schwingshackl A, Milne CD, et al. Proteinase-activated receptor-2-mediated matrix metalloproteinase-9 release from airway epithelial cells. J Allergy ClinImmunol 2000; 106:537-545.
    • (2000) J Allergy ClinImmunol , vol.106 , pp. 537-545
    • Vliagoftis, H.1    Schwingshackl, A.2    Milne, C.D.3
  • 116
    • 0032791025 scopus 로고    scopus 로고
    • Regulation of gelatinases in human airway smoothmuscle cells: Mechanism of progelatinase A activation
    • Foda HD, George S, Rollo E, et al. Regulation of gelatinases in human airway smoothmuscle cells: Mechanism of progelatinase A activation. Am J Physiol 1999; 277:L174-182.
    • (1999) Am J Physiol , vol.277 , pp. L174-L182
    • Foda, H.D.1    George, S.2    Rollo, E.3
  • 117
    • 0031092090 scopus 로고    scopus 로고
    • Eosinophils as a source of matrix metalloproteinase-9 in asthmatic airway inflammation
    • Ohno I, Ohtani H, Nitta Y, et al. Eosinophils as a source of matrix metalloproteinase-9 in asthmatic airway inflammation. Am J Respir Cell Mol Biol 1997; 16:212-219.
    • (1997) Am J Respir Cell Mol Biol , vol.16 , pp. 212-219
    • Ohno, I.1    Ohtani, H.2    Nitta, Y.3
  • 118
    • 0025818438 scopus 로고
    • Dexamethasone selectivelymodulates basal and lipoplysaccharide-induced metalloproteinase and tissue inhibitorof metalloproteinase production by human alveolar macrophages
    • Shapiro SD, Campbell EJ, Kobayashi DK, Welgus HG. Dexamethasone selectivelymodulates basal and lipoplysaccharide-induced metalloproteinase and tissue inhibitorof metalloproteinase production by human alveolar macrophages. J Immunol 1991;146:2724-2729.
    • (1991) J Immunol , vol.146 , pp. 2724-2729
    • Shapiro, S.D.1    Campbell, E.J.2    Kobayashi, D.K.3    Welgus, H.G.4
  • 119
    • 0031280307 scopus 로고    scopus 로고
    • Increased release of matrixmetalloproteinase-9 in bronchoalveolar lavage fluid and by alveolar macrophages ofasthmatics
    • Mautino G, Oliver N, Chanez P, Bousquet J, Capony F. Increased release of matrixmetalloproteinase-9 in bronchoalveolar lavage fluid and by alveolar macrophages ofasthmatics. Am J Respir Cell Mol Biol 1997; 17:583-591.
    • (1997) Am J Respir Cell Mol Biol , vol.17 , pp. 583-591
    • Mautino, G.1    Oliver, N.2    Chanez, P.3    Bousquet, J.4    Capony, F.5
  • 120
    • 0000692136 scopus 로고    scopus 로고
    • Serum matrixmetalloproteinase-9; tissue inhibitor of metalloproteinase-1 ratio correlates with steroidresponsiveness in moderate to severe asthma
    • Bosse M, Chakir J, Rouabhia M, Boulet LP, Audette M, Laviolette M. Serum matrixmetalloproteinase-9; tissue inhibitor of metalloproteinase-1 ratio correlates with steroidresponsiveness in moderate to severe asthma. Am J Respir Crit Care Med 1999; 159:596-602.
    • (1999) Am J Respir Crit Care Med , vol.159 , pp. 596-602
    • Bosse, M.1    Chakir, J.2    Rouabhia, M.3    Boulet, L.P.4    Audette, M.5    Laviolette, M.6
  • 121
    • 0032845858 scopus 로고    scopus 로고
    • Inhaled corticosteroids decrease subepithelial collagen deposition by modulation of the balance between matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 expression in asthma
    • Hoshino M, Takahashi M, Takai Y, Sim J. Inhaled corticosteroids decrease subepithelial collagen deposition by modulation of the balance between matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 expression in asthma. J Allergy ClinImmunol 1999; 104:356-363.
    • (1999) J Allergy ClinImmunol , vol.104 , pp. 356-363
    • Hoshino, M.1    Takahashi, M.2    Takai, Y.3    Sim, J.4
  • 122
    • 0035933151 scopus 로고    scopus 로고
    • Mechanical stress is communicated between different cell types to elicit matrix remodeling
    • Swartz MA, Tschumperlin DJ, Kamm RD, Drazen JM. Mechanical stress is communicated between different cell types to elicit matrix remodeling. Proc Natl Acad Sci USA2001; 98:6180-6185.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6180-6185
    • Swartz, M.A.1    Tschumperlin, D.J.2    Kamm, R.D.3    Drazen, J.M.4
  • 123
    • 0033120966 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinases preventsallergen-induced airway inflammation in a murine model of asthma
    • Kumagai K, Ohno I, Okada S, et al. Inhibition of matrix metalloproteinases preventsallergen-induced airway inflammation in a murine model of asthma. J Immunol 1999;162:4212-4219.
    • (1999) J Immunol , vol.162 , pp. 4212-4219
    • Kumagai, K.1    Ohno, I.2    Okada, S.3
  • 124
    • 0030841721 scopus 로고    scopus 로고
    • Increased vascularity of the bronchial mucosa in mild asthma
    • Li X, Wilson JW. Increased vascularity of the bronchial mucosa in mild asthma. AmJ Respir Crit Care Med 1997; 156:229-233.
    • (1997) AmJ Respir Crit Care Med , vol.156 , pp. 229-233
    • Li, X.1    Wilson, J.W.2
  • 126
    • 0346963598 scopus 로고    scopus 로고
    • MMP-9/gelatinase B is a key regulator of growthplate angiogenesis and apoptosis of hypertrophic chondrocytes
    • Vu TH, Shipley JM, Bergers G, et al. MMP-9/gelatinase B is a key regulator of growthplate angiogenesis and apoptosis of hypertrophic chondrocytes. Cell 1998; 93:411-422.
    • (1998) Cell , vol.93 , pp. 411-422
    • Vu, T.H.1    Shipley, J.M.2    Bergers, G.3
  • 127
    • 0035819527 scopus 로고    scopus 로고
    • Development of matrix metalloproteinase inhibitors in cancertherapy
    • Hidalgo M, Eckhardt SG. Development of matrix metalloproteinase inhibitors in cancertherapy. J Natl Cancer Inst 2001; 93:178-193.
    • (2001) J Natl Cancer Inst , vol.93 , pp. 178-193
    • Hidalgo, M.1    Eckhardt, S.G.2
  • 128
  • 130
    • 0031773610 scopus 로고    scopus 로고
    • Activation of matrix-degradingmetalloproteinases by mast cell proteases in atherosclerotic plaques
    • Johnson JL, Jackson CL, Angelini GD, George SJ. Activation of matrix-degradingmetalloproteinases by mast cell proteases in atherosclerotic plaques. ArteriosclerThromb Vasc Biol 1998; 18:1707-1715.
    • (1998) ArteriosclerThromb Vasc Biol , vol.18 , pp. 1707-1715
    • Johnson, J.L.1    Jackson, C.L.2    Angelini, G.D.3    George, S.J.4
  • 131
    • 0033049944 scopus 로고    scopus 로고
    • Immunohistochemical localisation of the matrix metalloproteinases MMP-3 and MMP-9 within the airways in asthma
    • Dahlen B, Shute J, Howarth P. Immunohistochemical localisation of the matrix metalloproteinases MMP-3 and MMP-9 within the airways in asthma. Thorax 1999; 54:590-596.
    • (1999) Thorax , vol.54 , pp. 590-596
    • Dahlen, B.1    Shute, J.2    Howarth, P.3
  • 132
    • 0035217088 scopus 로고    scopus 로고
    • A murine model of toluene diisocyanate-inducedasthma can be treated with matrix metalloproteinase inhibitor
    • Lee YC, Song CH, Lee HB, et al. A murine model of toluene diisocyanate-inducedasthma can be treated with matrix metalloproteinase inhibitor. J Allergy Clin Immunol2001; 108:1021-1026.
    • (2001) J Allergy Clin Immunol , vol.108 , pp. 1021-1026
    • Lee, Y.C.1    Song, C.H.2    Lee, H.B.3
  • 133
    • 0035069059 scopus 로고    scopus 로고
    • Inhibitionof bleomycin-induced pulmonary fibrosis in mice by the matrix metalloproteinaseinhibitor batimastat
    • Corbel M, Caulet-Maugendre S, Germain N, Molet S, Lagente V, Boichot E. Inhibitionof bleomycin-induced pulmonary fibrosis in mice by the matrix metalloproteinaseinhibitor batimastat. J Pathol 2001; 193:538-545.
    • (2001) J Pathol , vol.193 , pp. 538-545
    • Corbel, M.1    Caulet-Maugendre, S.2    Germain, N.3    Molet, S.4    Lagente, V.5    Boichot, E.6
  • 134
    • 0035198816 scopus 로고    scopus 로고
    • Ventilator-Induced Lung Injury Upregulates andActivates Gelatinases and EMMPRIN. Attenuation by the synthetic matrix metalloproteinase inhibitor, prinomastat (AG3340)
    • Foda HD, Rollo EE, Drews M, et al. Ventilator-Induced Lung Injury Upregulates andActivates Gelatinases and EMMPRIN. Attenuation by the synthetic matrix metalloproteinase inhibitor, prinomastat (AG3340). Am J Respir Cell Mol Biol 2001; 25:717-724.
    • (2001) Am J Respir Cell Mol Biol , vol.25 , pp. 717-724
    • Foda, H.D.1    Rollo, E.E.2    Drews, M.3
  • 135
    • 0033609534 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitor preventsacute lung injury after cardiopulmonary bypass
    • Carney DE, Lutz CJ, Picone AL, et al. Matrix metalloproteinase inhibitor preventsacute lung injury after cardiopulmonary bypass. Circulation 1999; 100:400-406.
    • (1999) Circulation , vol.100 , pp. 400-406
    • Carney, D.E.1    Lutz, C.J.2    Picone, A.L.3
  • 137
    • 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. AmJ Respir Cell Mol Biol 2000; 22:183-190.
    • (2000) AmJ Respir Cell Mol Biol , vol.22 , pp. 183-190
    • Wolters, P.J.1    Laig-Webster, M.2    Caughey, G.H.3
  • 138
    • 0027518670 scopus 로고
    • Generation of active myeloid and lymphoidgranule serine proteases requires processing by the granule thiol protease dipeptidylpeptidase I
    • McGuire MJ, Lipsky PE, Thiele DL. Generation of active myeloid and lymphoidgranule serine proteases requires processing by the granule thiol protease dipeptidylpeptidase I. J Biol Chem 1993; 268:2458-2467.
    • (1993) J Biol Chem , vol.268 , pp. 2458-2467
    • McGuire, M.J.1    Lipsky, P.E.2    Thiele, D.L.3
  • 139
    • 0035947568 scopus 로고    scopus 로고
    • Dipeptidyl peptidase Iis essential for activation of mast cell chymases, but not tryptases, in mice
    • Wolters PJ, Pham CT, Muilenburg DJ, Ley TJ, Caughey GH. Dipeptidyl peptidase Iis essential for activation of mast cell chymases, but not tryptases, in mice. J BiolChem 2001; 276:18551-18556.
    • (2001) J BiolChem , 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
  • 140
    • 0026518944 scopus 로고
    • Protease composition of exocytosedhuman skin mast cell protease-proteoglycan complexes: Tryptase resides in a complexdistinct from chymase and carboxypeptidase
    • Goldstein SM, Leong J, Schwartz LB, Cooke D. Protease composition of exocytosedhuman skin mast cell protease-proteoglycan complexes: Tryptase resides in a complexdistinct from chymase and carboxypeptidase. J Immunol 1992; 148:2475-2482.
    • (1992) J Immunol , vol.148 , pp. 2475-2482
    • Goldstein, S.M.1    Leong, J.2    Schwartz, L.B.3    Cooke, D.4
  • 141
    • 0343863344 scopus 로고
    • Mast cell carboxypeptidase: Structure and regulation of gene expression
    • Caughey GH. ed., New York:Marcel Dekker
    • Goldstein SM. Mast cell carboxypeptidase: Structure and regulation of gene expression.In: Caughey GH. ed. Mast Cell Proteases in Immunology and Biology. New York:Marcel Dekker, 1995:109-126.
    • (1995) Mast Cell Proteases in Immunology and Biology , pp. 109-126
    • Goldstein, S.M.1


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