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Volumn 184, Issue 3, 1996, Pages 1061-1073

Fate of two mast cell tryptases in V3 mastocytosis and normal BALB/c mice undergoing passive systemic anaphylaxis: Prolonged retention of exocytosed mMCP-6 in connective tissues, and rapid accumulation of enzymatically active mMCP-7 in the blood

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN E; PROTEOGLYCAN; TRYPTASE;

EID: 0029787629     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.184.3.1061     Document Type: Article
Times cited : (75)

References (66)
  • 1
    • 0025212267 scopus 로고
    • Different mouse mast cell populations express various combinations of at least six distinct mast cell serine proteases
    • Reynolds, D.S., R.L. Stevens, W.S. Lane, M.H. Carr, K.F. Austen, and W.E. Serafin. 1990. Different mouse mast cell populations express various combinations of at least six distinct mast cell serine proteases. Proc. Natl. Acad. Sci. USA. 87: 3230-3234.
    • (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
  • 2
    • 0025849174 scopus 로고
    • Cloning of the cDNA and gene of mouse mast cell protease-6. Transcription by progenitor mast cells and mast cells of the connective tissue subclass
    • Reynolds, D.S., D.S. Gurley, K.F. Austen, and W.E. Serafin. 1991. Cloning of the cDNA and gene of mouse mast cell protease-6. Transcription by progenitor mast cells and mast cells of the connective tissue subclass. J. Biol. Chem. 266: 3847-3853.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3847-3853
    • Reynolds, D.S.1    Gurley, D.S.2    Austen, K.F.3    Serafin, W.E.4
  • 4
    • 0027070909 scopus 로고
    • Mast cell tryptases: Examination of unusual characteristics by multiple sequence alignment and molecular modeling
    • Johnson, D.A., and G.J. Barton. 1992. Mast cell tryptases: examination of unusual characteristics by multiple sequence alignment and molecular modeling. Protein Sci. 1:370-377.
    • (1992) Protein Sci. , vol.1 , pp. 370-377
    • Johnson, D.A.1    Barton, G.J.2
  • 5
    • 0019888627 scopus 로고
    • Tryptase from human pulmonary mast cells: Purification and characterization
    • Schwartz, L.B., R.A. Lewis, and K.F. Austen. 1981. Tryptase from human pulmonary mast cells: purification and characterization. J. Biol. Chem. 256:11939-11943.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11939-11943
    • Schwartz, L.B.1    Lewis, R.A.2    Austen, K.F.3
  • 6
    • 0021148042 scopus 로고
    • Human lung tryptase. Purification and characterization
    • Smith, T.J., M.W. Hougland, and D.A. Johnson. 1984. Human lung tryptase. Purification and characterization. J. Biol. Chem. 259:11046-11051.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11046-11051
    • Smith, T.J.1    Hougland, M.W.2    Johnson, D.A.3
  • 7
    • 0024434198 scopus 로고
    • Cloning and characterization of complementary DNA for human tryptase
    • Miller, J.S., E.H. Westin, and L.B. Schwartz. 1989. Cloning and characterization of complementary DNA for human tryptase. J. Clin. Invest. 84:1188-1195.
    • (1989) J. Clin. Invest. , vol.84 , pp. 1188-1195
    • Miller, J.S.1    Westin, E.H.2    Schwartz, L.B.3
  • 8
    • 0025053169 scopus 로고
    • Cloning and characterization of a second complementary DNA for human tryptase
    • Miller, J.S., G. Moxley, and L.B. Schwartz. 1990. Cloning and characterization of a second complementary DNA for human tryptase. J. Clin. Invest. 86:864-870.
    • (1990) J. Clin. Invest. , vol.86 , pp. 864-870
    • Miller, J.S.1    Moxley, G.2    Schwartz, L.B.3
  • 12
    • 0024414345 scopus 로고
    • Autosomal recessive inheritance of airway hyperreactivity to 5-hydroxytryptamine
    • Levitt, R.C., and W. Mitzner. 1989. Autosomal recessive inheritance of airway hyperreactivity to 5-hydroxytryptamine. J. Appl. Physiol. 67:1125-1132.
    • (1989) J. Appl. Physiol. , vol.67 , pp. 1125-1132
    • Levitt, R.C.1    Mitzner, W.2
  • 14
    • 0030028575 scopus 로고    scopus 로고
    • Natural disruption of the mouse mast cell protease 7 gene in the C57BL/6 mouse
    • Hunt, J.E., R.L. Stevens, K.F. Austen, J. Zhang, Z. Xia, and N. Ghildyal. 1996. Natural disruption of the mouse mast cell protease 7 gene in the C57BL/6 mouse. J. Biol. Chem. 271: 2851-2855.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2851-2855
    • Hunt, J.E.1    Stevens, R.L.2    Austen, K.F.3    Zhang, J.4    Xia, Z.5    Ghildyal, N.6
  • 17
    • 0024597956 scopus 로고
    • Mast cell tryptase and chymase reverse airway smooth muscle relaxation induced by vasoactive intestinal peptide in the ferret
    • Franconi, G.M., P.D. Graf, S.C. Lazarus, J.A. Nadel, and G.H. Caughey. 1989. Mast cell tryptase and chymase reverse airway smooth muscle relaxation induced by vasoactive intestinal peptide in the ferret. J. Pharmacol. Exp. Ther. 248:947-951.
    • (1989) J. Pharmacol. Exp. Ther. , vol.248 , pp. 947-951
    • Franconi, G.M.1    Graf, P.D.2    Lazarus, S.C.3    Nadel, J.A.4    Caughey, G.H.5
  • 18
    • 0025864033 scopus 로고
    • Mast cell tryptase is a mitogen for cultured fibroblasts
    • Ruoss, S.J., T. Hartmann, and G.H. Caughey. 1991. Mast cell tryptase is a mitogen for cultured fibroblasts. J. Clin. Invest. 88:493-499.
    • (1991) J. Clin. Invest. , vol.88 , pp. 493-499
    • Ruoss, S.J.1    Hartmann, T.2    Caughey, G.H.3
  • 19
    • 0030032558 scopus 로고    scopus 로고
    • Mast cell tryptase is a mitogen for epithelial cells
    • Cairns, J.A., and A.F. Walls. 1996. Mast cell tryptase is a mitogen for epithelial cells. J. Immunol. 156:275-283.
    • (1996) J. Immunol. , vol.156 , pp. 275-283
    • Cairns, J.A.1    Walls, A.F.2
  • 20
    • 0020627947 scopus 로고
    • Inactivation of human high molecular weight kininogen by human mast cell tryptase
    • Maier, M., J. Spragg, and L.B. Schwartz. 1983. Inactivation of human high molecular weight kininogen by human mast cell tryptase. J. Immunol. 130:2352-2356.
    • (1983) J. Immunol. , vol.130 , pp. 2352-2356
    • Maier, M.1    Spragg, J.2    Schwartz, L.B.3
  • 21
    • 0023875638 scopus 로고
    • Substance P and vasoactive intestinal peptide degradation by mast cell tryptase and chymase
    • Caughey, G.H., F. Leidig, N.F. Viro, and J.A. Nadel. 1988. Substance P and vasoactive intestinal peptide degradation by mast cell tryptase and chymase. J. Pharmacol. Exp. Ther. 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
  • 22
    • 0024429920 scopus 로고
    • Synovial procollagenase activation by human mast cell tryptase. Dependence upon matrix metalloproteinase 3 activation
    • Gruber, B.L., M.J. Marchese, K. Suzuki, L.B. Schwartz, Y. Okada, H. Nagase, and N.S. Ramamurthy. 1989. Synovial procollagenase activation by human mast cell tryptase. Dependence upon matrix metalloproteinase 3 activation. J. Clin. Invest. 84:1657-1662.
    • (1989) J. Clin. Invest. , vol.84 , pp. 1657-1662
    • Gruber, B.L.1    Marchese, M.J.2    Suzuki, K.3    Schwartz, L.B.4    Okada, Y.5    Nagase, H.6    Ramamurthy, N.S.7
  • 23
    • 0028363122 scopus 로고
    • Human mast cell tryptase activates single-chain urinary-type plasminogen activator (pro-urokinase)
    • Stack, M.S., and D.A. Johnson. 1994. Human mast cell tryptase activates single-chain urinary-type plasminogen activator (pro-urokinase). J. Biol. Chem. 269:9416-9419.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9416-9419
    • Stack, M.S.1    Johnson, D.A.2
  • 24
    • 0021160734 scopus 로고
    • Granule-associated serine neutral proteases of the mouse bone marrow-derived mast cell that degrade fibronectin: Their increase after sodium buryrate treatment of the cells
    • DuBuske, L., K.F. Austen, J. Czop, and R.L. Stevens. 1984. Granule-associated serine neutral proteases of the mouse bone marrow-derived mast cell that degrade fibronectin: their increase after sodium buryrate treatment of the cells. J. Immunol. 133:1535-1541.
    • (1984) J. Immunol. , vol.133 , pp. 1535-1541
    • DuBuske, L.1    Austen, K.F.2    Czop, J.3    Stevens, R.L.4
  • 25
    • 0026677848 scopus 로고
    • Pericellular substrates of human mast cell tryptase: 72,000 dalton gelatinase and fibronectin
    • Lohi, J., I. Harvima, and J. Keski-Oja. 1992. Pericellular substrates of human mast cell tryptase: 72,000 dalton gelatinase and fibronectin. J. Cell. Biochem. 50:337-349.
    • (1992) J. Cell. Biochem. , vol.50 , pp. 337-349
    • Lohi, J.1    Harvima, I.2    Keski-Oja, J.3
  • 26
    • 0022388692 scopus 로고
    • The fribrinogenolytic activity of purified tryptase from human lung mast cells
    • Schwartz, L.B., T.R. Bradford, B.H. Littman, and B.U. Wintroub. 1985. The fribrinogenolytic activity of purified tryptase from human lung mast cells. J. Immunol. 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
  • 28
    • 0023266455 scopus 로고
    • Measurement of the internal pH of mast cell granules using micro volumetric fluorescence and isotopic techniques
    • De Young, M.B., E.F. Nemeth, and A. Scarpa. 1987. Measurement of the internal pH of mast cell granules using micro volumetric fluorescence and isotopic techniques. Arch. Biochem. Biophys. 254:222-233.
    • (1987) Arch. Biochem. Biophys. , vol.254 , pp. 222-233
    • De Young, M.B.1    Nemeth, E.F.2    Scarpa, A.3
  • 29
    • 0023025461 scopus 로고
    • 3H]diisopropyl fluorophosphate-binding proteins are exocytosed from activated mouse bone marrow-derived mast cells
    • 3H]diisopropyl fluorophosphate-binding proteins are exocytosed from activated mouse bone marrow-derived mast cells. J. Biol. Chem. 261:15017-15021.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15017-15021
    • Serafin, W.E.1    Katz, H.R.2    Austen, K.F.3    Stevens, R.L.4
  • 30
    • 0019416681 scopus 로고
    • Cell association of complexes of chymase, heparin proteoglycan, and protein after degranulation by rat mast cells
    • Schwartz, L.B., C. Riedel, J.P. Caulfield, S.I. Wasserman, and K.F. Austen. 1981. Cell association of complexes of chymase, heparin proteoglycan, and protein after degranulation by rat mast cells. J. Immunol. 126:2071-2078.
    • (1981) J. Immunol. , vol.126 , pp. 2071-2078
    • Schwartz, L.B.1    Riedel, C.2    Caulfield, J.P.3    Wasserman, S.I.4    Austen, K.F.5
  • 31
    • 0022872843 scopus 로고
    • Regulation of tryptase from human lung mast cells by heparin. Stabilization of the active tetramer
    • Schwartz, L.B., and T.R. Bradford. 1986. Regulation of tryptase from human lung mast cells by heparin. Stabilization of the active tetramer. J. Biol. Chem. 261:7372-7379.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7372-7379
    • Schwartz, L.B.1    Bradford, T.R.2
  • 32
    • 0026518944 scopus 로고
    • Protease composition of exocytosed human skin mast cell protease-proteoglycan complexes
    • Goldstein, S.M., J. Leong, L.B. Schwartz, and D. Cooke. 1992. Protease composition of exocytosed human skin mast cell protease-proteoglycan complexes. J. Immunol. 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
  • 33
    • 0001275278 scopus 로고
    • Tissue mast cells. Studies with a histamine-liberator of low toxicity (compound 48/80)
    • Riley, J.F., and G.B. West. 1955. Tissue mast cells. Studies with a histamine-liberator of low toxicity (compound 48/80). J. Pathol. Bacterial. 69:269-282.
    • (1955) J. Pathol. Bacterial. , vol.69 , pp. 269-282
    • Riley, J.F.1    West, G.B.2
  • 34
    • 0016288940 scopus 로고
    • Ultrastructure of mucosal mast cells in normal and compound 48/80-treated rats
    • Enerbäck, L., and P.M. Lundin. 1974. Ultrastructure of mucosal mast cells in normal and compound 48/80-treated rats. Cell Tissue Res. 150:95-105.
    • (1974) Cell Tissue Res. , vol.150 , pp. 95-105
    • Enerbäck, L.1    Lundin, P.M.2
  • 35
    • 0022243368 scopus 로고
    • Fibroblasts maintain the phenotype and viability of the rat heparin-containing mast cell in vitro
    • Levi-Schaffer, F., K.F. Austen, J.P. Caulfield, A. Hein, W.F. Bloes, and R.L. Stevens. 1985. Fibroblasts maintain the phenotype and viability of the rat heparin-containing mast cell in vitro. J. Immunol. 135:3454-3462.
    • (1985) J. Immunol. , vol.135 , pp. 3454-3462
    • Levi-Schaffer, F.1    Austen, K.F.2    Caulfield, J.P.3    Hein, A.4    Bloes, W.F.5    Stevens, R.L.6
  • 36
    • 0023567897 scopus 로고
    • Regulation of human mast cell tryptase. Effects of enzyme concentration, ionic strength and the structure and negative charge density of polysaccharides
    • Alter, S.C., D.D. Metcalfe, T.R. Bradford, and L.B. Schwartz. 1987. Regulation of human mast cell tryptase. Effects of enzyme concentration, ionic strength and the structure and negative charge density of polysaccharides. Biochem. J. 248:821-827.
    • (1987) Biochem. J. , vol.248 , pp. 821-827
    • Alter, S.C.1    Metcalfe, D.D.2    Bradford, T.R.3    Schwartz, L.B.4
  • 37
    • 0010234421 scopus 로고
    • Substrate specificity of the chymotrypsin-like protease in secretory granules isolated from rat mast cells
    • Le Trong, H., H. Neurath, and R.G. Woodbury. 1987. Substrate specificity of the chymotrypsin-like protease in secretory granules isolated from rat mast cells. Proc. Natl. Acad. Sci. USA. 84:364-367.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 364-367
    • Le Trong, H.1    Neurath, H.2    Woodbury, R.G.3
  • 39
    • 0027401683 scopus 로고
    • Three-dimensional models of four mouse mast cell chymases. Identification of proteoglycan-binding regions and protease-specific antigenic epitopes
    • Šali, A., R. Matsumoto, H.P. McNeil, M. Karplus, and R.L. Stevens. 1993. Three-dimensional models of four mouse mast cell chymases. Identification of proteoglycan-binding regions and protease-specific antigenic epitopes. J. Biol. Chem. 268:9023-9034.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9023-9034
    • Šali, A.1    Matsumoto, R.2    McNeil, H.P.3    Karplus, M.4    Stevens, R.L.5
  • 40
    • 0029094503 scopus 로고
    • Packaging of proteases and proteoglycans in the granules of mast cells and other hematopoietic cells. A cluster of histidines on mouse mast cell protease 7 regulates its binding to heparin serglycin proteoglycans
    • Matsumoto, R., A. Šali, N. Ghildyal, M. Karplus, and R.L. Stevens. 1995. Packaging of proteases and proteoglycans in the granules of mast cells and other hematopoietic cells. A cluster of histidines on mouse mast cell protease 7 regulates its binding to heparin serglycin proteoglycans. J. Biol. Chem. 270:19524-19531.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19524-19531
    • Matsumoto, R.1    Šali, A.2    Ghildyal, N.3    Karplus, M.4    Stevens, R.L.5
  • 45
    • 0019518080 scopus 로고
    • Enzyme histochemistry and immunohistochemistry on biopsy specimens of pathologic human bone marrow
    • Beckstead, J.H., P.S. Halverson, C.A. Ries, and D.F. Bainton. 1981. Enzyme histochemistry and immunohistochemistry on biopsy specimens of pathologic human bone marrow. Blood. 57:1088-1098.
    • (1981) Blood , vol.57 , pp. 1088-1098
    • Beckstead, J.H.1    Halverson, P.S.2    Ries, C.A.3    Bainton, D.F.4
  • 46
    • 0026773502 scopus 로고
    • Distribution of chymase-containing mast cells in human bronchi
    • Matin, R., E.K. Tam, J.A. Nadel, and G.H. Caughey. 1992. Distribution of chymase-containing mast cells in human bronchi. J. Histochem. Cytochem. 40:781-786.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 781-786
    • Matin, R.1    Tam, E.K.2    Nadel, J.A.3    Caughey, G.H.4
  • 47
    • 0000832262 scopus 로고
    • Synthetic chromogenic substrates for determination of trypsin, thrombin, and thrombin-like enzymes
    • Svendsen, L., B. Blomback, M. Blomback, and P.I. Olsson. 1972. Synthetic chromogenic substrates for determination of trypsin, thrombin, and thrombin-like enzymes. Throm. Res. 1:267-278.
    • (1972) Throm. Res. , vol.1 , pp. 267-278
    • Svendsen, L.1    Blomback, B.2    Blomback, M.3    Olsson, P.I.4
  • 48
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Šali, A., and T.L. Blundell. 1993. Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol. 234: 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Šali, A.1    Blundell, T.L.2
  • 49
    • 0028051828 scopus 로고
    • Derivation of rules for comparative protein modeling from a database of protein structure alignments
    • Šali, A., and J.P. Overington. 1994. Derivation of rules for comparative protein modeling from a database of protein structure alignments. Prot. Sci. 3:1582-1596.
    • (1994) Prot. Sci. , vol.3 , pp. 1582-1596
    • Šali, A.1    Overington, J.P.2
  • 51
    • 0000243829 scopus 로고
    • A program to check the stereochemical quality of protein structures
    • Laskowski, R.L., M.W. McArthur, D.S. Moss, and J.M. Thornton. 1993. A program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26:283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.L.1    McArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 52
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., K.A. Sharp, and B. Honig. 1991. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 54
    • 0025789989 scopus 로고
    • Molecular cloning of the mouse mast cell protease-5 gene. A novel secretory granule protease expressed early in the differentiation of serosal mast cells
    • McNeil, H.P., K.F. Austen, L.L. Somerville, M.F. Gurish, and R.L. Stevens. 1991. Molecular cloning of the mouse mast cell protease-5 gene. A novel secretory granule protease expressed early in the differentiation of serosal mast cells. J. Biol. Chem. 266:20316-20322.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20316-20322
    • McNeil, H.P.1    Austen, K.F.2    Somerville, L.L.3    Gurish, M.F.4    Stevens, R.L.5
  • 55
    • 0012578734 scopus 로고
    • Phagocytosis of granules from disrupted mast cells
    • Smith, D.E., and Y.S. Lewis. 1958. Phagocytosis of granules from disrupted mast cells. Anat. Rec. 132:93-111.
    • (1958) Anat. Rec. , vol.132 , pp. 93-111
    • Smith, D.E.1    Lewis, Y.S.2
  • 56
    • 9544247081 scopus 로고
    • Phagocytosis of mast cell granules by the eosinophilic leukocyte in the rat
    • Welsh, R.A., and J.C. Geer. 1959. Phagocytosis of mast cell granules by the eosinophilic leukocyte in the rat. Am. J. Pathol. 35:103-111.
    • (1959) Am. J. Pathol. , vol.35 , pp. 103-111
    • Welsh, R.A.1    Geer, J.C.2
  • 57
    • 0020059671 scopus 로고
    • Phagocytosis of mast cell granules by mononuclear phagocytes, neutrophils, and eosinophils during anaphylaxis
    • Baggiolini, M., U. Horisberger, and U. Martin. 1982. Phagocytosis of mast cell granules by mononuclear phagocytes, neutrophils, and eosinophils during anaphylaxis. Int. Arch. Allergy Appl. Immunol. 67:219-226.
    • (1982) Int. Arch. Allergy Appl. Immunol. , vol.67 , pp. 219-226
    • Baggiolini, M.1    Horisberger, U.2    Martin, U.3
  • 58
    • 0020660995 scopus 로고
    • Phagocytosis of mast cell granules by cultured fibroblasts
    • Rao, P.V.S., M.M. Friedman, F.M. Atkins, and D.D. Metcalfe. 1983. Phagocytosis of mast cell granules by cultured fibroblasts. J. Immunol. 130:341-349.
    • (1983) J. Immunol. , vol.130 , pp. 341-349
    • Rao, P.V.S.1    Friedman, M.M.2    Atkins, F.M.3    Metcalfe, D.D.4
  • 59
    • 0024237214 scopus 로고
    • Kunitz-type protease inhibitor found in rat mast cells. Purification, properties, and amino acid sequence
    • Kido, H., Y. Yokogoshi, and N. Katunuma. 1988. Kunitz-type protease inhibitor found in rat mast cells. Purification, properties, and amino acid sequence. J. Biol. Chem. 263: 18104-18107.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18104-18107
    • Kido, H.1    Yokogoshi, Y.2    Katunuma, N.3
  • 60
    • 0028124193 scopus 로고
    • Mast cell protease inhibitor, trypstatin, is a fragment of inter-α-trypsin inhibitor light chain
    • Itoh, H., H. Ide, N. Ishikawa, and Y. Nawa. 1994. Mast cell protease inhibitor, trypstatin, is a fragment of inter-α-trypsin inhibitor light chain. J. Biol. Chem. 269:3818-3822.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3818-3822
    • Itoh, H.1    Ide, H.2    Ishikawa, N.3    Nawa, Y.4
  • 61
    • 0027955033 scopus 로고
    • Identification of targeting proteinase for rat α1-macroglobulin in vivo. Mast cell tryptase is a major component of the α1-macroglobulin-proteinase complex endocytosed into rat liver lysosomes
    • Tsuji, A., T. Akamatsu, H. Nagamune, and Y. Matsuda. 1994. Identification of targeting proteinase for rat α1-macroglobulin in vivo. Mast cell tryptase is a major component of the α1-macroglobulin-proteinase complex endocytosed into rat liver lysosomes. Biochem. J. 298:79-85.
    • (1994) Biochem. J. , vol.298 , pp. 79-85
    • Tsuji, A.1    Akamatsu, T.2    Nagamune, H.3    Matsuda, Y.4
  • 62
    • 0023262466 scopus 로고
    • Tryptase levels as an indicator of mast cell activation in systemic anaphylaxis and mastocytosis
    • Schwartz, L.B., D.D. Metcalfe, J.S. Miller, H. Earl, and T. Sullivan. 1987. Tryptase levels as an indicator of mast cell activation in systemic anaphylaxis and mastocytosis. N. Engl. J. Med. 316:1622-1626.
    • (1987) N. Engl. J. Med. , vol.316 , pp. 1622-1626
    • Schwartz, L.B.1    Metcalfe, D.D.2    Miller, J.S.3    Earl, H.4    Sullivan, T.5
  • 63
    • 0024547878 scopus 로고
    • Time course of appearance and disappearance of human mast cell tryptase in the circulation after anaphylaxis
    • Schwartz, L.B., J.W. Yunginger, J. Miller, R. Bokhari, and D. Dull. 1989. Time course of appearance and disappearance of human mast cell tryptase in the circulation after anaphylaxis. J. Clin. Invest. 83:1551-1555.
    • (1989) J. Clin. Invest. , vol.83 , pp. 1551-1555
    • Schwartz, L.B.1    Yunginger, J.W.2    Miller, J.3    Bokhari, R.4    Dull, D.5
  • 65
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu, T.-K.H., D.T. Hung, V.I. Wheaton, and S.R. Coughlin. 1991. Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell. 64:1057-1068.
    • (1991) Cell , vol.64 , pp. 1057-1068
    • Vu, T.-K.H.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 66
    • 0028934047 scopus 로고
    • The mouse proteinase-activated receptor-2 cDNA and gene. Molecular cloning and functional expression
    • Nystedt, S., A.-K. Larsson, H. Åberg, and J. Sundelin. 1995. The mouse proteinase-activated receptor-2 cDNA and gene. Molecular cloning and functional expression. J. Biol. Chem. 270:5950-5955.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5950-5955
    • Nystedt, S.1    Larsson, A.-K.2    Åberg, H.3    Sundelin, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.