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Volumn 183, Issue 4, 2009, Pages 2223-2231

The cathelicidin LL-37 activates human mast cells and is degraded by mast cell tryptase: Counter-regulation by CXCL4

Author keywords

[No Author keywords available]

Indexed keywords

CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; CHEMOKINE; CXCL4 PROTEIN; HEPARIN; LIPOPOLYSACCHARIDE; TETRAMER; TRYPTASE; UNCLASSIFIED DRUG; ANTIMICROBIAL PEPTIDE LL-37; AUTACOID; CATHELICIDIN; THROMBOCYTE FACTOR 4;

EID: 70149093034     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.0803587     Document Type: Article
Times cited : (44)

References (57)
  • 1
    • 34248140140 scopus 로고    scopus 로고
    • Mast cell tryptases and chymases in inflammation and host defense
    • Caughey, G. H. 2007. Mast cell tryptases and chymases in inflammation and host defense. Immunol. Rev. 217: 141-154.
    • (2007) Immunol. Rev. , vol.217 , pp. 141-154
    • Caughey, G.H.1
  • 2
    • 23444460431 scopus 로고    scopus 로고
    • Cytokine production by skin-derived mast cells: Endogenous proteases are responsible for degradation of cytokines
    • Zhao, W., C. A. Oskeritzian, A. L. Pozez, and L. B. Schwartz. 2005. Cytokine production by skin-derived mast cells: endogenous proteases are responsible for degradation of cytokines. J. Immunol. 175: 2635-2642. (Pubitemid 41113878)
    • (2005) Journal of Immunology , vol.175 , Issue.4 , pp. 2635-2642
    • Zhao, W.1    Oskeritzian, C.A.2    Pozez, A.L.3    Schwartz, L.B.4
  • 4
    • 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, S. M., J. Leong, L. B. Schwartz, and D. Cooke. 1992. Protease composition of exocytosed human skin mast cell protease-proteoglycan complexes: tryptase resides in a complex distinct from chymase and carboxypeptidase. 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
  • 5
    • 0020312338 scopus 로고
    • Rapid conversion of angiotensin I to angiotensin II by neutrophil and mast cell proteinases
    • Reilly, C. F., D. A. Tewksbury, N. M. Schechter, and J. Travis. 1982. Rapid conversion of angiotensin I to angiotensin II by neutrophil and mast cell proteinases. J. Biol. Chem. 257: 8619-8622.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8619-8622
    • Reilly, C.F.1    Tewksbury, D.A.2    Schechter, N.M.3    Travis, J.4
  • 7
    • 33644772132 scopus 로고    scopus 로고
    • Mast cells and neutrophils proteolytically activate chemokine precursor CTAP-III and are subject to counterregulation by PF-4 through inhibition of chymase and cathepsin G
    • Schiemann, F., T. A. Grimm, J. Hoch, R. Gross, B. Lindner, F. Petersen, S. Bulfone-Paus, and E. Brandt. 2006. Mast cells and neutrophils proteolytically activate chemokine precursor CTAP-III and are subject to counterregulation by PF-4 through inhibition of chymase and cathepsin G. Blood 107: 2234-2242.
    • (2006) Blood , vol.107 , pp. 2234-2242
    • Schiemann, F.1    Grimm, T.A.2    Hoch, J.3    Gross, R.4    Lindner, B.5    Petersen, F.6    Bulfone-Paus, S.7    Brandt, E.8
  • 11
    • 0025162150 scopus 로고
    • Interactions of human mast cell tryptase with biological protease inhibitors
    • Alter, S. C., J. A. Kramps, A. Janoff, and L. B. Schwartz. 1990. Interactions of human mast cell tryptase with biological protease inhibitors. Arch. Biochem. Biophys. 276: 26-31.
    • (1990) Arch. Biochem. Biophys. , vol.276 , pp. 26-31
    • Alter, S.C.1    Kramps, J.A.2    Janoff, A.3    Schwartz, L.B.4
  • 12
    • 0030744683 scopus 로고    scopus 로고
    • Lactoferrin, a potent tryptase inhibitor, abolishes late-phase airway responses in allergic sheep
    • Elrod, K. C., W. R. Moore, W. M. Abraham, and R. D. Tanaka. 1997. Lactoferrin, a potent tryptase inhibitor, abolishes late-phase airway responses in allergic sheep. Am. J. Respir. Crit. Care Med. 156: 375-381.
    • (1997) Am. J. Respir. Crit. Care Med. , vol.156 , pp. 375-381
    • Elrod, K.C.1    Moore, W.R.2    Abraham, W.M.3    Tanaka, R.D.4
  • 14
    • 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., G. T. De Sanctis, P. J. O'Brien, J. P. Mizgerd, D. S. Friend, J. M. Drazen, L. F. Brass, and R. L. Stevens. 2001. 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. 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    Mizgerd, J.P.4    Friend, D.S.5    Drazen, J.M.6    Brass, L.F.7    Stevens, R.L.8
  • 15
    • 0031573586 scopus 로고    scopus 로고
    • Potent Induction of a Neutrophil and Eosinophil-Rich Infiltrate in Vivo by Human Mast Cell Tryptase: Selective Enhancement of Eosinophil Recruitment by Histamine
    • He, S., Q. Peng, and A. F. Walls. 1997. Potent induction of a neutrophil and eosinophil-rich infiltrate in vivo by human mast cell tryptase: selective enhancement of eosinophil recruitment by histamine. J. Immunol. 159: 6216-6225. (Pubitemid 127471563)
    • (1997) Journal of Immunology , vol.159 , Issue.12 , pp. 6216-6225
    • He, S.1    Peng, Q.2    Walls, A.F.3
  • 17
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
    • Sorensen, O. E., P. Follin, A. H. Johnsen, J. Calafat, G. S. Tjabringa, P. S. Hiemstra, and N. Borregaard. 2001. Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 97: 3951-3959.
    • (2001) Blood , vol.97 , pp. 3951-3959
    • Sorensen, O.E.1    Follin, P.2    Johnsen, A.H.3    Calafat, J.4    Tjabringa, G.S.5    Hiemstra, P.S.6    Borregaard, N.7
  • 18
    • 0035007963 scopus 로고    scopus 로고
    • Interaction of CAP18-derived peptides with membranes made from endotoxins or phospholipids
    • Gutsmann, T., S. O. Hagge, J. W. Larrick, U. Seydel, and A. Wiese. 2001. Interaction of CAP18-derived peptides with membranes made from endotoxins or phospholipids. Biophys. J. 80: 2935-2945. (Pubitemid 32521665)
    • (2001) Biophysical Journal , vol.80 , Issue.6 , pp. 2935-2945
    • Gutsmann, T.1    Hagge, S.O.2    Larrick, J.W.3    Seydel, U.4    Wiese, A.5
  • 20
    • 0034596945 scopus 로고    scopus 로고
    • LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells
    • Yang, D., Q. Chen, A. P. Schmidt, G. M. Anderson, J. M. Wang, J. Wooters, J. J. Oppenheim, and O. Chertov. 2000. LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J. Exp. Med. 192: 1069-1074.
    • (2000) J. Exp. Med. , vol.192 , pp. 1069-1074
    • Yang, D.1    Chen, Q.2    Schmidt, A.P.3    Anderson, G.M.4    Wang, J.M.5    Wooters, J.6    Oppenheim, J.J.7    Chertov, O.8
  • 21
  • 23
    • 50849097211 scopus 로고    scopus 로고
    • Surface acoustic wave biosensor as a tool to study the interaction of antimicrobial peptides with phospholipid and lipopolysaccharide model membranes
    • Andra, J., A. Bohling, T. M. Gronewold, U. Schlecht, M. Perpeet, and T. Gutsmann. 2008. Surface acoustic wave biosensor as a tool to study the interaction of antimicrobial peptides with phospholipid and lipopolysaccharide model membranes. Langmuir. 24: 9148-9153.
    • (2008) Langmuir. , vol.24 , pp. 9148-9153
    • Andra, J.1    Bohling, A.2    Gronewold, T.M.3    Schlecht, U.4    Perpeet, M.5    Gutsmann, T.6
  • 24
    • 0029671459 scopus 로고    scopus 로고
    • TNF-α renders human neutrophils responsive to platelet factor 4: Comparison of PF-4 and IL-8 reveals different activity profiles of the two chemokines
    • Petersen, F., A. Ludwig, H. D. Flad, and E. Brandt. 1996. TNF-α renders human neutrophils responsive to platelet factor 4: comparison of PF-4 and IL-8 reveals different activity profiles of the two chemokines. J. Immunol. 156: 1954-1962. (Pubitemid 26069331)
    • (1996) Journal of Immunology , vol.156 , Issue.5 , pp. 1954-1962
    • Petersen, F.1    Ludwig, A.2    Flad, H.-D.3    Brandt, E.4
  • 25
    • 0031657134 scopus 로고    scopus 로고
    • Recombinant human mast cell tryptase β: Stable expression in Pichia pastoris and purification of fully active enzyme
    • Niles, A. L., M. Maffitt, M. Haak-Frendscho, C. J. Wheeless, and D. A. Johnson. 1998. Recombinant human mast cell tryptase β: stable expression in Pichia pastoris and purification of fully active enzyme. Biotechnol. Appl. Biochem. 28(Pt. 2): 125-131.
    • (1998) Biotechnol. Appl. Biochem. , vol.28 , Issue.PART 2 , pp. 125-131
    • Niles, A.L.1    Maffitt, M.2    Haak-Frendscho, M.3    Wheeless, C.J.4    Johnson, D.A.5
  • 26
    • 12344254105 scopus 로고    scopus 로고
    • Affinity chromatography of tryptases: Design, synthesis and characterization of a novel matrix-bound bivalent inhibitor
    • Schaschke, N., D. Gabrijelcic-Geiger, A. Dominik, and C. P. Sommerhoff. 2005. Affinity chromatography of tryptases: design, synthesis and characterization of a novel matrix-bound bivalent inhibitor. Chembiochem. 6: 95-103.
    • (2005) Chembiochem. , vol.6 , pp. 95-103
    • Schaschke, N.1    Gabrijelcic-Geiger, D.2    Dominik, A.3    Sommerhoff, C.P.4
  • 27
    • 0015546107 scopus 로고
    • Determination of the operational molarity of solutions of bovine α-chymotrypsin, trypsin, thrombin and factor Xa by spectrofluorimetric titration
    • Jameson, G. W., D. V. Roberts, R. W. Adams, W. S. Kyle, and D. T. Elmore. 1973. Determination of the operational molarity of solutions of bovine α-chymotrypsin, trypsin, thrombin and factor Xa by spectrofluorimetric titration. Biochem. J. 131: 107-117.
    • (1973) Biochem. J. , vol.131 , pp. 107-117
    • Jameson, G.W.1    Roberts, D.V.2    Adams, R.W.3    Kyle, W.S.4    Elmore, D.T.5
  • 29
    • 0035874533 scopus 로고    scopus 로고
    • The basophil activation marker defined by antibody 97A6 is identical to the ectonucleotide pyrophosphatase/phosphodiesterase 3
    • Buhring, H. J., M. Seiffert, C. Giesert, A. Marxer, L. Kanz, P. Valent, and K. Sano. 2001. The basophil activation marker defined by antibody 97A6 is identical to the ectonucleotide pyrophosphatase/phosphodiesterase 3. Blood 97: 3303-3305.
    • (2001) Blood , vol.97 , pp. 3303-3305
    • Buhring, H.J.1    Seiffert, M.2    Giesert, C.3    Marxer, A.4    Kanz, L.5    Valent, P.6    Sano, K.7
  • 30
    • 0028344958 scopus 로고
    • A new rapid and simple non-radioactive assay to monitor and determine the proliferation of lymphocytes: An alternative to [3H]thymidine incorporation assay
    • Ahmed, S. A., R. M. Gogal, Jr., and J. E. Walsh. 1994. A new rapid and simple non-radioactive assay to monitor and determine the proliferation of lymphocytes: an alternative to [3H]thymidine incorporation assay. J. Immunol. Methods 170: 211-224.
    • (1994) J. Immunol. Methods , vol.170 , pp. 211-224
    • Ahmed, S.A.1    Gogal Jr., R.M.2    Walsh, J.E.3
  • 31
    • 0018715705 scopus 로고
    • Immunologic release of β-hexosaminidase and β-glucuronidase from purified rat serosal mast cells
    • Schwartz, L. B., K. F. Austen, and S. I. Wasserman. 1979. Immunologic release of β-hexosaminidase and β-glucuronidase from purified rat serosal mast cells. J. Immunol. 123: 1445-1450. (Pubitemid 10220721)
    • (1979) Journal of Immunology , vol.123 , Issue.4 , pp. 1445-1450
    • Schwartz, L.B.1    Austen, K.F.2    Wasserman, S.I.3
  • 32
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., and G. Von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166: 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 33
    • 0036721707 scopus 로고    scopus 로고
    • Platelet-derived chemokines CXC chemokine ligand (CXCL)7, connective tissue-activating peptide III, and CXCL4 differentially affect and cross-regulate neutrophil adhesion and transendothelial migration
    • Schenk, B. I., F. Petersen, H. D. Flad, and E. Brandt. 2002. Platelet-derived chemokines CXC chemokine ligand (CXCL)7, connective tissue-activating peptide III, and CXCL4 differentially affect and cross-regulate neutrophil adhesion and transendothelial migration. J. Immunol. 169: 2602-2610.
    • (2002) J. Immunol. , vol.169 , pp. 2602-2610
    • Schenk, B.I.1    Petersen, F.2    Flad, H.D.3    Brandt, E.4
  • 34
    • 0036659179 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV (CD26) on T cells cleaves the CXC chemokine CXCL11 (I-TAC) and abolishes the stimulating but not the desensitizing potential of the chemokine
    • Ludwig, A., F. Schiemann, R. Mentlein, B. Lindner, and E. Brandt. 2002. Dipeptidyl peptidase IV (CD26) on T cells cleaves the CXC chemokine CXCL11 (I-TAC) and abolishes the stimulating but not the desensitizing potential of the chemokine. J. Leukocyte Biol. 72: 183-191.
    • (2002) J. Leukocyte Biol. , vol.72 , pp. 183-191
    • Ludwig, A.1    Schiemann, F.2    Mentlein, R.3    Lindner, B.4    Brandt, E.5
  • 36
    • 0027430713 scopus 로고
    • Phenotypical and functional characterization of Fcγ receptor I (CD64)-negative monocytes, a minor human monocyte subpopulation with high accessory and antiviral activity
    • Grage-Griebenow, E., D. Lorenzen, R. Fetting, H. D. Flad, and M. Ernst. 1993. Phenotypical and functional characterization of Fcγ receptor I (CD64)-negative monocytes, a minor human monocyte subpopulation with high accessory and antiviral activity. Eur. J. Immunol. 23: 3126-3135.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 3126-3135
    • Grage-Griebenow, E.1    Lorenzen, D.2    Fetting, R.3    Flad, H.D.4    Ernst, M.5
  • 37
    • 0025950239 scopus 로고
    • Purification and characterization of a trypsin inhibitor from mouse seminal vesicle secretion
    • Lai, M. L., S. W. Chen, and Y. H. Chen. 1991. Purification and characterization of a trypsin inhibitor from mouse seminal vesicle secretion. Arch. Biochem. Biophys. 290: 265-271.
    • (1991) Arch. Biochem. Biophys. , vol.290 , pp. 265-271
    • Lai, M.L.1    Chen, S.W.2    Chen, Y.H.3
  • 38
    • 0028429960 scopus 로고
    • Differential binding of chemokines to glycosaminoglycan subpopulations
    • Witt, D. P., and A. D. Lander. 1994. Differential binding of chemokines to glycosaminoglycan subpopulations. Curr. Biol. 4: 394-400. (Pubitemid 124001751)
    • (1994) Current Biology , vol.4 , Issue.5 , pp. 394-400
    • Witt, D.P.1    Lander, A.D.2
  • 39
    • 0029610823 scopus 로고
    • Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study. Arginine residues are crucial for binding
    • Mayo, K. H., E. Ilyina, V. Roongta, M. Dundas, J. Joseph, C. K. Lai, T. Maione, and T. J. Daly. 1995. Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study. Arginine residues are crucial for binding. Biochem. J. 312(Pt. 2): 357-365.
    • (1995) Biochem. J. , vol.312 , Issue.PART 2 , pp. 357-365
    • Mayo, K.H.1    Ilyina, E.2    Roongta, V.3    Dundas, M.4    Joseph, J.5    Lai, C.K.6    Maione, T.7    Daly, T.J.8
  • 40
    • 33846160570 scopus 로고    scopus 로고
    • Mast cell tryptase β as a target in allergic inflammation: An evolving story
    • Sommerhoff, C. P., and N. Schaschke. 2007. Mast cell tryptase β as a target in allergic inflammation: an evolving story. Curr. Pharm. Des. 13: 313-332.
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 313-332
    • Sommerhoff, C.P.1    Schaschke, N.2
  • 41
    • 27144462218 scopus 로고    scopus 로고
    • Sputum cathelicidin, urokinase plasminogen activation system components, and cytokines discriminate cystic fibrosis, COPD, and asthma inflammation
    • Xiao, W., Y. P. Hsu, A. Ishizaka, T. Kirikae, and R. B. Moss. 2005. Sputum cathelicidin, urokinase plasminogen activation system components, and cytokines discriminate cystic fibrosis, COPD, and asthma inflammation. Chest 128: 2316-2326.
    • (2005) Chest , vol.128 , pp. 2316-2326
    • Xiao, W.1    Hsu, Y.P.2    Ishizaka, A.3    Kirikae, T.4    Moss, R.B.5
  • 45
    • 0026179119 scopus 로고
    • Evidence for in vivo degradation of C3a anaphylatoxin by mast cell chymase. I. Nonspecific activation of rat peritoneal mast cells by C3ades Arg
    • Kajita, T., and T. E. Hugli. 1991. Evidence for in vivo degradation of C3a anaphylatoxin by mast cell chymase. I. Nonspecific activation of rat peritoneal mast cells by C3ades Arg. Am. J. Pathol. 138: 1359-1369.
    • (1991) Am. J. Pathol. , vol.138 , pp. 1359-1369
    • Kajita, T.1    Hugli, T.E.2
  • 46
    • 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
  • 47
    • 0025010595 scopus 로고
    • Anaphylatoxin binding and degradation by rat peritoneal mast cells: Mechanisms of degranulation and control
    • Fukuoka, Y., and T. E. Hugli. 1990. Anaphylatoxin binding and degradation by rat peritoneal mast cells: mechanisms of degranulation and control. J. Immunol. 145: 1851-1858. (Pubitemid 20336754)
    • (1990) Journal of Immunology , vol.145 , Issue.6 , pp. 1851-1858
    • Fukuoka, Y.1    Hugli, T.E.2
  • 48
    • 47249165576 scopus 로고    scopus 로고
    • Mast cell cathelicidin antimicrobial peptide prevents invasive group a Streptococcus infection of the skin
    • Di Nardo, A., K. Yamasaki, R. A. Dorschner, Y. Lai, and R. L. Gallo. 2008. Mast cell cathelicidin antimicrobial peptide prevents invasive group A Streptococcus infection of the skin. J. Immunol. 180: 7565-7573.
    • (2008) J. Immunol. , vol.180 , pp. 7565-7573
    • Di Nardo, A.1    Yamasaki, K.2    Dorschner, R.A.3    Lai, Y.4    Gallo, R.L.5
  • 49
    • 0036450262 scopus 로고    scopus 로고
    • Cathelicidin anti-microbial peptide expression in sweat, an innate defense system for the skin
    • Murakami, M., T. Ohtake, R. A. Dorschner, B. Schittek, C. Garbe, and R. L. Gallo. 2002. Cathelicidin anti-microbial peptide expression in sweat, an innate defense system for the skin. J. Invest. Dermatol. 119: 1090-1095.
    • (2002) J. Invest. Dermatol. , vol.119 , pp. 1090-1095
    • Murakami, M.1    Ohtake, T.2    Dorschner, R.A.3    Schittek, B.4    Garbe, C.5    Gallo, R.L.6
  • 50
    • 1342282224 scopus 로고    scopus 로고
    • Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense
    • Murakami, M., B. Lopez-Garcia, M. Braff, R. A. Dorschner, and R. L. Gallo. 2004. Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense. J. Immunol. 172: 3070-3077.
    • (2004) J. Immunol. , vol.172 , pp. 3070-3077
    • Murakami, M.1    Lopez-Garcia, B.2    Braff, M.3    Dorschner, R.A.4    Gallo, R.L.5
  • 51
    • 33644978944 scopus 로고    scopus 로고
    • Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides: Peptide properties and plausible modes of action
    • Rosenfeld, Y., N. Papo, and Y. Shai. 2006. Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides: peptide properties and plausible modes of action. J. Biol. Chem. 281: 1636-1643.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1636-1643
    • Rosenfeld, Y.1    Papo, N.2    Shai, Y.3
  • 54
    • 0033652243 scopus 로고    scopus 로고
    • Platelet-derived CXC chemokines: Old players in new games
    • Brandt, E., A. Ludwig, F. Petersen, and H. D. Flad. 2000. Platelet-derived CXC chemokines: old players in new games. Immunol. Rev. 177: 204-216.
    • (2000) Immunol. Rev. , vol.177 , pp. 204-216
    • Brandt, E.1    Ludwig, A.2    Petersen, F.3    Flad, H.D.4
  • 55
    • 0035912953 scopus 로고    scopus 로고
    • Heparin antagonists are potent inhibitors of mast cell tryptase
    • Hallgren, J., S. Estrada, U. Karlson, K. Alving, and G. Pejler. 2001. Heparin antagonists are potent inhibitors of mast cell tryptase. Biochemistry 40: 7342-7349. (Pubitemid 32554060)
    • (2001) Biochemistry , vol.40 , Issue.24 , pp. 7342-7349
    • Hallgren, J.1    Estrada, S.2    Karlson, U.3    Alving, K.4    Pejler, G.5
  • 56
    • 0033150593 scopus 로고    scopus 로고
    • Neutrophil myeloperoxidase is a potent and selective inhibitor of mast cell tryptase
    • Cregar, L., K. C. Elrod, D. Putnam, and W. R. Moore. 1999. Neutrophil myeloperoxidase is a potent and selective inhibitor of mast cell tryptase. Arch. Biochem. Biophys. 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
  • 57
    • 33750861825 scopus 로고    scopus 로고
    • Anaphylaxis-induced mesenteric vascular permeability, granulocyte adhesion, and platelet aggregates in rat
    • Withers, G. D., P. Kubes, G. Ibbotson, and R. B. Scott. 1998. Anaphylaxis-induced mesenteric vascular permeability, granulocyte adhesion, and platelet aggregates in rat. Am. J. Physiol. 275: H274-H284.
    • (1998) Am. J. Physiol. , vol.275
    • Withers, G.D.1    Kubes, P.2    Ibbotson, G.3    Scott, R.B.4


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