Granule proteases of hematopoietic cells, a family of versatile inflammatory mediators – an update on their cleavage specificity, in vivo substrates, and evolution

References

Abonia, J.P., Friend, D.S., Austen, W.G., Jr., Moore, F.D., Jr., Carroll, M.C., Chan, R., Afnan, J., Humbles, A., Gerard, C., Knight, P., et al. (2005). Mast cell protease 5 mediates ischemia-reperfusion injury of mouse skeletal muscle. J. Immunol. 174, 7285–7291.10.4049/jimmunol.174.11.7285Suche in Google Scholar PubMed PubMed Central

Ahooghalandari, P., Hanke, N., Thorpe, M., Witte, A., Messinger, J., and Hellman, L. (2013). Mutations in Arg143 and Lys192 of the human mast cell chymase markedly affect the activity of five potent human chymase inhibitors. PLoS One 8, e65988.10.1371/journal.pone.0065988Suche in Google Scholar PubMed PubMed Central

Akahoshi, M., Song, C.H., Piliponsky, A.M., Metz, M., Guzzetta, A., Abrink, M., Schlenner, S.M., Feyerabend, T.B., Rodewald, H.R., Pejler, G., et al. (2011). Mast cell chymase reduces the toxicity of Gila monster venom, scorpion venom, and vasoactive intestinal polypeptide in mice. J. Clin. Invest. 121, 4180–4191.10.1172/JCI46139Suche in Google Scholar PubMed PubMed Central

Andersson, M.K., Karlson, U., and Hellman, L. (2008a). The extended cleavage specificity of the rodent β-chymases rMCP-1 and mMCP-4 reveal major functional similarities to the human mast cell chymase. Mol. Immunol. 45, 766–775.10.1016/j.molimm.2007.06.360Suche in Google Scholar PubMed

Andersson, M.K., Pemberton, A.D., Miller, H.R., and Hellman, L. (2008b). Extended cleavage specificity of mMCP-1, the major mucosal mast cell protease in mouse-high specificity indicates high substrate selectivity. Mol. Immunol. 45, 2548–2558.10.1016/j.molimm.2008.01.012Suche in Google Scholar PubMed

Andersson, M.K., Enoksson, M., Gallwitz, M., and Hellman, L. (2009). The extended substrate specificity of the human mast cell chymase reveals a serine protease with well-defined substrate recognition profile. Int. Immunol. 21, 95–104.10.1093/intimm/dxn128Suche in Google Scholar PubMed

Andersson, M.K., Thorpe, M., and Hellman, L. (2010). Arg143 and Lys192 of the human mast cell chymase mediate the preference for acidic amino acids in position P2′ of substrates. FEBS J. 277, 2255–2267.10.1111/j.1742-4658.2010.07642.xSuche in Google Scholar PubMed

Andrade, F., Fellows, E., Jenne, D.E., Rosen, A., and Young, C.S. (2007). Granzyme H destroys the function of critical adenoviral proteins required for viral DNA replication and granzyme B inhibition. EMBO J. 26, 2148–2157.10.1038/sj.emboj.7601650Suche in Google Scholar PubMed PubMed Central

Aveskogh, M., Lutzelschwab, C., Huang, M.R., and Hellman, L. (1997). Characterization of cDNA clones encoding mouse proteinase 3 (myeloblastine) and cathepsin G. Immunogenetics 46, 181–191.10.1007/s002510050260Suche in Google Scholar PubMed

Belkowski, S.M., Masucci, J., Mahan, A., Kervinen, J., Olson, M., de Garavilla, L., and D’Andrea, M.R. (2008). Cleaved SLPI, a novel biomarker of chymase activity. Biol. Chem. 389, 1219–1224.10.1515/BC.2008.138Suche in Google Scholar PubMed

Belkowski, S.M., Boot, J.D., Mascelli, M.A., Diamant, Z., de Garavilla, L., Hertzog, B., Polkovitch, D., Towers, M., Batheja, A., and D’Andrea, M.R. (2009). Cleaved secretory leucocyte protease inhibitor as a biomarker of chymase activity in allergic airway disease. Clin. Exp. Allergy 39, 1179–1186.10.1111/j.1365-2222.2009.03247.xSuche in Google Scholar PubMed

Bovenschen, N. and Kummer, J.A. (2010). Orphan granzymes find a home. Immunol. Rev. 235, 117–127.10.1111/j.0105-2896.2010.00889.xSuche in Google Scholar PubMed

Bovenschen, N., Quadir, R., van den Berg, A.L., Brenkman, A.B., Vandenberghe, I., Devreese, B., Joore, J., and Kummer, J.A. (2009). Granzyme K displays highly restricted substrate specificity that only partially overlaps with granzyme A. J. Biol. Chem. 284, 3504–3512.10.1074/jbc.M806716200Suche in Google Scholar PubMed

Brinkmann, V., Reichard, U., Goosmann, C., Fauler, B., Uhlemann, Y., Weiss, D.S., Weinrauch, Y., and Zychlinsky, A. (2004). Neutrophil extracellular traps kill bacteria. Science 303, 1532–1535.10.1126/science.1092385Suche in Google Scholar PubMed

Campanelli, D., Detmers, P.A., Nathan, C.F., and Gabay, J.E. (1990). Azurocidin and a homologous serine protease from neutrophils. Differential antimicrobial and proteolytic properties. J. Clin. Invest. 85, 904–915.10.1172/JCI114518Suche in Google Scholar PubMed PubMed Central

Caughey, G.H. (2004). Genetic insights into mast cell chymase and tryptase function. Clin. Exp. Allergy Rev. 4, 96–101.10.1111/j.1472-9725.2004.00041.xSuche in Google Scholar

Caughey, G.H. (2007). Mast cell tryptases and chymases in inflammation and host defense. Immunol. Rev. 217, 141–154.10.1111/j.1600-065X.2007.00509.xSuche in Google Scholar PubMed PubMed Central

Caughey, G.H. (2011). Mast cell proteases as protective and inflammatory mediators. Adv. Exp. Med. Biol. 716, 212–234.10.1007/978-1-4419-9533-9_12Suche in Google Scholar PubMed PubMed Central

Caughey, G.H., Leidig, F., Viro, N.F., and Nadel, J.A. (1988). Substance P and vasoactive intestinal peptide degradation by mast cell tryptase and chymase. J. Pharmacol. Exp. Ther. 244, 133–137.Suche in Google Scholar

Caughey, G.H., Beauchamp, J., Schlatter, D., Raymond, W.W., Trivedi, N.N., Banner, D., Mauser, H., and Fingerle, J. (2008). Guinea pig chymase is leucine-specific: a novel example of functional plasticity in the chymase/granzyme family of serine peptidases. J. Biol. Chem. 283, 13943–13951.10.1074/jbc.M710502200Suche in Google Scholar PubMed PubMed Central

Cavalcante, M.C., Allodi, S., Valente, A.P., Straus, A.H., Takahashi, H.K., Mourao, P.A., and Pavao, M.S. (2000). Occurrence of heparin in the invertebrate styela plicata (Tunicata) is restricted to cell layers facing the outside environment. An ancient role in defense? J. Biol. Chem. 275, 36189–36186.10.1074/jbc.M005830200Suche in Google Scholar PubMed

Cavalcante, M.C., de Andrade, L.R., Du Bocage Santos-Pinto, C., Straus, A.H., Takahashi, H.K., Allodi, S., and Pavao, M.S. (2002). Colocalization of heparin and histamine in the intracellular granules of test cells from the invertebrate Styela plicata (Chordata-Tunicata). J. Struct. Biol. 137, 313–321.10.1016/S1047-8477(02)00007-2Suche in Google Scholar

Cenac, N., Coelho, A.M., Nguyen, C., Compton, S., Andrade-Gordon, P., MacNaughton, W.K., Wallace, J.L., Hollenberg, M.D., Bunnett, N.W., Garcia-Villar, R., et al. (2002). Induction of intestinal inflammation in mouse by activation of proteinase-activated receptor-2. Am. J. Pathol. 161, 1903–1915.10.1016/S0002-9440(10)64466-5Suche in Google Scholar

Chandrasekharan, U.M., Sanker, S., Glynias, M.J., Karnik, S.S., and Husain, A. (1996). Angiotensin II-forming activity in a reconstructed ancestral chymase. Science 271, 502–505.10.1126/science.271.5248.502Suche in Google Scholar PubMed

Chowdhury, D. and Lieberman, J. (2008). Death by a thousand cuts: granzyme pathways of programmed cell death. Annu. Rev. Immunol. 26, 389–420.10.1146/annurev.immunol.26.021607.090404Suche in Google Scholar PubMed PubMed Central

Corvera, C.U., Dery, O., McConalogue, K., Bohm, S.K., Khitin, L.M., Caughey, G.H., Payan, D.G., and Bunnett, N.W. (1997). Mast cell tryptase regulates rat colonic myocytes through proteinase-activated receptor 2. J. Clin. Invest. 100, 1383–1393.10.1172/JCI119658Suche in Google Scholar PubMed PubMed Central

de Poot, S.A., Westgeest, M., Hostetter, D.R., Van Damme, P., Plasman, K., Demeyer, K., Broekhuizen, R., Gevaert, K., Craik, C.S., and Bovenschen, N. (2011). Human and mouse granzyme M display divergent and species-specific substrate specificities. Biochem. J. 437, 431–442.10.1042/BJ20110210Suche in Google Scholar PubMed

Doumas, S., Kolokotronis, A., and Stefanopoulos, P. (2005). Anti-inflammatory and antimicrobial roles of secretory leukocyte protease inhibitor. Infect. Immun. 73, 1271–1274.10.1128/IAI.73.3.1271-1274.2005Suche in Google Scholar PubMed PubMed Central

Dudeck, A., Dudeck, J., Scholten, J., Petzold, A., Surianarayanan, S., Kohler, A., Peschke, K., Vohringer, D., Waskow, C., Krieg, T., et al. (2011). Mast cells are key promoters of contact allergy that mediate the adjuvant effects of haptens. Immunity 34, 973–984.10.1016/j.immuni.2011.03.028Suche in Google Scholar PubMed

Ebnet, K., Hausmann, M., Lehmann-Grube, F., Mullbacher, A., Kopf, M., Lamers, M., and Simon, M.M. (1995). Granzyme A-deficient mice retain potent cell-mediated cytotoxicity. EMBO J. 14, 4230–4239.10.1002/j.1460-2075.1995.tb00097.xSuche in Google Scholar PubMed PubMed Central

Echtenacher, B., Mannel, D.N., and Hultner, L. (1996). Critical protective role of mast cells in a model of acute septic peritonitis. Nature 381, 75–77.10.1038/381075a0Suche in Google Scholar PubMed

Edwards, K.M., Kam, C.M., Powers, J.C., and Trapani, J.A. (1999). The human cytotoxic T cell granule serine protease granzyme H has chymotrypsin-like (chymase) activity and is taken up into cytoplasmic vesicles reminiscent of granzyme B-containing endosomes. J. Biol. Chem. 274, 30468–30473.10.1074/jbc.274.43.30468Suche in Google Scholar PubMed

Ewen, C.L., Kane, K.P., and Bleackley, R.C. (2012). A quarter century of granzymes. Cell Death Differ. 19, 28–35.10.1038/cdd.2011.153Suche in Google Scholar PubMed PubMed Central

Fajardo, I. and Pejler, G. (2003). Formation of active monomers from tetrameric human β-tryptase. Biochem. J. 369, 603–610.10.1042/bj20021418Suche in Google Scholar

Fellows, E., Gil-Parrado, S., Jenne, D.E., and Kurschus, F.C. (2007). Natural killer cell-derived human granzyme H induces an alternative, caspase-independent cell-death program. Blood 110, 544–552.10.1182/blood-2006-10-051649Suche in Google Scholar PubMed

Feyerabend, T.B., Hausser, H., Tietz, A., Blum, C., Hellman, L., Straus, A.H., Takahashi, H.K., Morgan, E.S., Dvorak, A.M., Fehling, H.J., et al. (2005). Loss of histochemical identity in mast cells lacking carboxypeptidase A. Mol. Cell. Biol. 25, 6199–6210.10.1128/MCB.25.14.6199-6210.2005Suche in Google Scholar PubMed PubMed Central

Feyerabend, T.B., Weiser, A., Tietz, A., Stassen, M., Harris, N., Kopf, M., Radermacher, P., Moller, P., Benoist, C., Mathis, D., et al. (2011). Cre-mediated cell ablation contests mast cell contribution in models of antibody- and T cell-mediated autoimmunity. Immunity 35, 832–844.10.1016/j.immuni.2011.09.015Suche in Google Scholar PubMed

Forsberg, E., Pejler, G., Ringvall, M., Lunderius, C., Tomasini-Johansson, B., Kusche-Gullberg, M., Eriksson, I., Ledin, J., Hellman, L., and Kjellen, L. (1999). Abnormal mast cells in mice deficient in a heparin-synthesizing enzyme. Nature 400, 773–776.10.1038/23488Suche in Google Scholar PubMed

Gallwitz, M. and Hellman, L. (2006). Rapid lineage-specific diversification of the mast cell chymase locus during mammalian evolution. Immunogenetics 58, 641–654.10.1007/s00251-006-0123-4Suche in Google Scholar PubMed

Gallwitz, M., Reimer, J.M., and Hellman, L. (2006). Expansion of the mast cell chymase locus over the past 200 million years of mammalian evolution. Immunogenetics 58, 655–669.10.1007/s00251-006-0126-1Suche in Google Scholar PubMed

Gallwitz, M., Enoksson, M., and Hellman, L. (2007). Expression profile of novel members of the rat mast cell protease (rMCP)-2 and (rMCP)-8 families, and functional analyses of mouse mast cell protease (mMCP)-8. Immunogenetics 59, 391–405.10.1007/s00251-007-0202-1Suche in Google Scholar PubMed

Gallwitz, M., Enoksson, M., Thorpe, M., Ge, X., and Hellman, L. (2010). The extended substrate recognition profile of the dog mast cell chymase reveals similarities and differences to the human chymase. Int. Immunol. 22, 421–431.10.1093/intimm/dxq021Suche in Google Scholar

Gallwitz, M., Enoksson, M., Thorpe, M., and Hellman, L. (2012). The extended cleavage specificity of human thrombin. PLoS One 7, e31756.10.1371/journal.pone.0031756Suche in Google Scholar

Garcia-Sanz, J.A., MacDonald, H.R., Jenne, D.E., Tschopp, J., and Nabholz, M. (1990). Cell specificity of granzyme gene expression. J. Immunol. 145, 3111–3118.10.4049/jimmunol.145.9.3111Suche in Google Scholar

Graf, L., Craik, C.S., Patthy, A., Roczniak, S., Fletterick, R.J., and Rutter, W.J. (1987). Selective alteration of substrate specificity by replacement of aspartic acid-189 with lysine in the binding pocket of trypsin. Biochemistry 26, 2616–2623.10.1021/bi00383a031Suche in Google Scholar

Grimbaldeston, M.A., Chen, C.C., Piliponsky, A.M., Tsai, M., Tam, S.Y., and Galli, S.J. (2005). Mast cell-deficient W-sash c-kit mutant Kit W-sh/W-sh mice as a model for investigating mast cell biology in vivo. Am. J. Pathol. 167, 835–848.10.1016/S0002-9440(10)62055-XSuche in Google Scholar

Grossman, W.J., Revell, P.A., Lu, Z.H., Johnson, H., Bredemeyer, A.J., and Ley, T.J. (2003). The orphan granzymes of humans and mice. Curr. Opin. Immunol. 15, 544–552.10.1016/S0952-7915(03)00099-2Suche in Google Scholar

Gruber, B.L., Marchese, M.J., Suzuki, K., Schwartz, L.B., Okada, Y., Nagase, H., and Ramamurthy, N.S. (1989). Synovial procollagenase activation by human mast cell tryptase dependence upon matrix metalloproteinase 3 activation. J. Clin. Invest. 84, 1657–1662.10.1172/JCI114344Suche in Google Scholar PubMed PubMed Central

Guo, C., Ju, H., Leung, D., Massaeli, H., Shi, M., and Rabinovitch, M. (2001). A novel vascular smooth muscle chymase is upregulated in hypertensive rats. J. Clin. Invest. 107, 703–715.10.1172/JCI9997Suche in Google Scholar PubMed PubMed Central

Guyot, N., Zani, M.L., Berger, P., Dallet-Choisy, S., and Moreau, T. (2005). Proteolytic susceptibility of the serine protease inhibitor trappin-2 (pre-elafin): evidence for tryptase-mediated generation of elafin. Biol. Chem. 386, 391–399.10.1515/BC.2005.047Suche in Google Scholar PubMed

Haddad, P., Jenne, D., Tschopp, J., Clement, M.V., Mathieu-Mahul, D., and Sasportes, M. (1991). Structure and evolutionary origin of the human granzyme H gene. Int. Immunol. 3, 57–66.10.1093/intimm/3.1.57Suche in Google Scholar PubMed

Hallgren, J. and Pejler, G. (2006). Biology of mast cell tryptase. An inflammatory mediator. FEBS J. 273, 1871–1895.10.1111/j.1742-4658.2006.05211.xSuche in Google Scholar PubMed

Hallgren, J., Spillmann, D., and Pejler, G. (2001). Structural requirements and mechanism for heparin-induced activation of a recombinant mouse mast cell tryptase, mouse mast cell protease-6: formation of active tryptase monomers in the presence of low molecular weight heparin. J. Biol. Chem. 276, 42774–42781.10.1074/jbc.M105531200Suche in Google Scholar

Hamilton, M.J., Sinnamon, M.J., Lyng, G.D., Glickman, J.N., Wang, X., Xing, W., Krilis, S.A., Blumberg, R.S., Adachi, R., Lee, D.M., et al. (2011). Essential role for mast cell tryptase in acute experimental colitis. Proc. Natl. Acad. Sci. USA 108, 290–295.10.1073/pnas.1005758108Suche in Google Scholar

Harris, J.L., Peterson, E.P., Hudig, D., Thornberry, N.A., and Craik, C.S. (1998). Definition and redesign of the extended substrate specificity of granzyme B. J. Biol. Chem. 273, 27364–27373.10.1074/jbc.273.42.27364Suche in Google Scholar

He, S. and Walls, A.F. (1998). Human mast cell chymase induces the accumulation of neutrophils, eosinophils and other inflammatory cells in vivo. Br. J. Pharmacol. 125, 1491–1500.10.1038/sj.bjp.0702223Suche in Google Scholar

Heibein, J.A., Barry, M., Motyka, B., and Bleackley, R.C. (1999). Granzyme B-induced loss of mitochondrial inner membrane potential (Δψ_m) and cytochrome c release are caspase independent. J. Immunol. 163, 4683–4693.10.4049/jimmunol.163.9.4683Suche in Google Scholar

Heusel, J.W., Wesselschmidt, R.L., Shresta, S., Russell, J.H., and Ley, T.J. (1994). Cytotoxic lymphocytes require granzyme B for the rapid induction of DNA fragmentation and apoptosis in allogeneic target cells. Cell 76, 977–987.10.1016/0092-8674(94)90376-XSuche in Google Scholar

Heutinck, K.M., ten Berge, I.J., Hack, C.E., Hamann, J., and Rowshani, A.T. (2010). Serine proteases of the human immune system in health and disease. Mol. Immunol. 47, 1943–1955.10.1016/j.molimm.2010.04.020Suche in Google Scholar PubMed

Hirst, C.E., Buzza, M.S., Sutton, V.R., Trapani, J.A., Loveland, K.L., and Bird, P.I. (2001). Perforin-independent expression of granzyme B and proteinase inhibitor 9 in human testis and placenta suggests a role for granzyme B-mediated proteolysis in reproduction. Mol. Human Reprod. 7, 1133–1142.10.1093/molehr/7.12.1133Suche in Google Scholar PubMed

Hou, Q., Zhao, T., Zhang, H., Lu, H., Zhang, Q., Sun, L., and Fan, Z. (2008). Granzyme H induces apoptosis of target tumor cells characterized by DNA fragmentation and Bid-dependent mitochondrial damage. Mol. Immunol. 45, 1044–1055.10.1016/j.molimm.2007.07.032Suche in Google Scholar PubMed

Hua, G., Wang, S., Zhong, C., Xue, P., and Fan, Z. (2009). Ignition of p53 bomb sensitizes tumor cells to granzyme K-mediated cytolysis. J. Immunol. 182, 2152–2159.10.4049/jimmunol.0802307Suche in Google Scholar PubMed

Huang, R. and Hellman, L. (1994). Genes for mast-cell serine protease and their molecular evolution. Immunogenetics 40, 397–414.10.1007/BF00177823Suche in Google Scholar PubMed

Huang, R.Y., Blom, T., and Hellman, L. (1991). Cloning and structural analysis of MMCP-1, MMCP-4 and MMCP-5, three mouse mast cell-specific serine proteases. Eur. J. Immunol. 21, 1611–1621.10.1002/eji.1830210706Suche in Google Scholar PubMed

Huang, R., Abrink, M., Gobl, A.E., Nilsson, G., Aveskogh, M., Larsson, L.G., Nilsson, K., and Hellman, L. (1993). Expression of a mast cell tryptase in the human monocytic cell lines U-937 and Mono Mac 6. Scand J. Immunol. 38, 359–367.10.1111/j.1365-3083.1993.tb01738.xSuche in Google Scholar PubMed

Huang, C., Wong, G.W., Ghildyal, N., Gurish, M.F., Sali, A., Matsumoto, R., Qiu, W.T., and Stevens, R.L. (1997). The tryptase, mouse mast cell protease 7, exhibits anticoagulant activity in vivo and in vitro due to its ability to degrade fibrinogen in the presence of the diverse array of protease inhibitors in plasma. J. Biol. Chem. 272, 31885–31893.10.1074/jbc.272.50.31885Suche in Google Scholar PubMed

Huang, C., Friend, D.S., Qiu, W.T., Wong, G.W., Morales, G., Hunt, J., and Stevens, R.L. (1998). Induction of a selective and persistent extravasation of neutrophils into the peritoneal cavity by tryptase mouse mast cell protease 6. J. Immunol. 160, 1910–1919.10.4049/jimmunol.160.4.1910Suche in Google Scholar

Huang, C., De Sanctis, G.T., O’Brien, P.J., Mizgerd, J.P., Friend, D.S., Drazen, J.M., Brass, L.F., and Stevens, R.L. (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, 26276–26284.10.1074/jbc.M102356200Suche in Google Scholar PubMed

Hunt, J.E., Stevens, R.L., Austen, K.F., Zhang, J., Xia, Z., and Ghildyal, N. (1996). Natural disruption of the mouse mast cell protease 7 gene in the C57BL/6 mouse. J. Biol. Chem. 271, 2851–2855.10.1074/jbc.271.5.2851Suche in Google Scholar PubMed

Imamura, T., Dubin, A., Moore, W., Tanaka, R., and Travis, J. (1996). Induction of vascular permeability enhancement by human tryptase: dependence on activation of prekallikrein and direct release of bradykinin from kininogens. Lab. Invest. 74, 861–870.Suche in Google Scholar

Irani, A.M., Goldstein, S.M., Wintroub, B.U., Bradford, T., and Schwartz, L.B. (1991). Human mast cell carboxypeptidase. Selective localization to MCTC cells. J. Immunol. 147, 247–253.10.4049/jimmunol.147.1.247Suche in Google Scholar

Irwin, D.M. (2004). Evolution of cow nonstomach lysozyme genes. Genome 47, 1082–1090.10.1139/g04-075Suche in Google Scholar PubMed

Irwin, D.M., Biegel, J.M., and Stewart, C.B. (2011). Evolution of the mammalian lysozyme gene family. Evol. Biol. 11, 1–16.10.1186/1471-2148-11-166Suche in Google Scholar PubMed PubMed Central

Kaiserman, D., Bird, C.H., Sun, J., Matthews, A., Ung, K., Whisstock, J.C., Thompson, P.E., Trapani, J.A., and Bird, P.I. (2006). The major human and mouse granzymes are structurally and functionally divergent. J. Cell Biol. 175, 619–630.10.1083/jcb.200606073Suche in Google Scholar PubMed PubMed Central

Kaminska, R., Helisalmi, P., Harvima, R.J., Naukkarinen, A., Horsmanheimo, M., and Harvima, I.T. (1999). Focal dermal-epidermal separation and fibronectin cleavage in basement membrane by human mast cell tryptase. J. Invest. Dermatol. 113, 567–573.10.1046/j.1523-1747.1999.00738.xSuche in Google Scholar PubMed

Karlson, U. (2003). Cutting edge- cleavage specificity and biochemical characterization of mast cell serine proteases. In: Department of Cell and Molecular Biology (Uppsala: Uppsala University), thesis ISBN 91-554-5699-5.Suche in Google Scholar

Karlson, U., Pejler, G., Froman, G., and Hellman, L. (2002). Rat mast cell protease 4 is a β-chymase with unusually stringent substrate recognition profile. J. Biol. Chem. 277, 18579–18585.10.1074/jbc.M110356200Suche in Google Scholar PubMed

Karlson, U., Pejler, G., Tomasini-Johansson, B., and Hellman, L. (2003). Extended substrate specificity of rat mast cell protease 5, a rodent α-chymase with elastase-like primary specificity. J. Biol. Chem. 278, 39625–39631.10.1074/jbc.M301512200Suche in Google Scholar

Kawabata, K., Hagio, T., and Matsuoka, S. (2002). The role of neutrophil elastase in acute lung injury. Eur. J. Pharmacol. 451, 1–10.10.1016/S0014-2999(02)02182-9Suche in Google Scholar

Kervinen, J., Abad, M., Crysler, C., Kolpak, M., Mahan, A.D., Masucci, J.A., Bayoumy, S., Cummings, M.D., Yao, X., Olson, M., et al. (2008). Structural basis for elastolytic substrate specificity in rodent α-chymases. J. Biol. Chem. 283, 427–436.10.1074/jbc.M707157200Suche in Google Scholar PubMed

Kielty, C.M., Lees, M., Shuttleworth, C.A., and Woolley, D. (1993). Catabolism of intact type VI collagen microfibrils: susceptibility to degradation by serine proteinases. Biochem. Biophys. Res. Commun. 191, 1230–1236.10.1006/bbrc.1993.1349Suche in Google Scholar PubMed

Kitamura, Y., Go, S., and Hatanaka, K. (1978). Decrease of mast cells in W/Wv mice and their increase by bone marrow transplantation. Blood 52, 447–452.10.1182/blood.V52.2.447.447Suche in Google Scholar

Kloog, Y., Ambar, I., Sokolovsky, M., Kochva, E., Wollberg, Z., and Bdolah, A. (1988). Sarafotoxin, a novel vasoconstrictor peptide: phosphoinositide hydrolysis in rat heart and brain. Science 242, 268–270.10.1126/science.2845579Suche in Google Scholar PubMed

Knight, P.A., Wright, S.H., Lawrence, C.E., Paterson, Y.Y., and Miller, H.R. (2000). Delayed expulsion of the nematode Trichinella spiralis in mice lacking the mucosal mast cell-specific granule chymase, mouse mast cell protease-1. J. Exp. Med. 192, 1849–1856.10.1084/jem.192.12.1849Suche in Google Scholar PubMed PubMed Central

Korkmaz, B., Moreau, T., and Gauthier, F. (2008). Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties, activity and physiopathological functions. Biochimie 90, 227–242.10.1016/j.biochi.2007.10.009Suche in Google Scholar PubMed

Korkmaz, B., Jegot, G., Lau, L.C., Thorpe, M., Pitois, E., Juliano, L., Walls, A.F., Hellman, L., and Gauthier, F. (2011). Discriminating between the activities of human cathepsin G and chymase using fluorogenic substrates. FEBS J. 278, 2635–2646.10.1111/j.1742-4658.2011.08189.xSuche in Google Scholar PubMed

Kornegay, J.R., Schilling, J.W., and Wilson, A.C. (1994). Molecular adaptation of a leaf-eating bird: stomach lysozyme of the hoatzin. Mol. Biol. Evol. 11, 921–928.Suche in Google Scholar

Krishnaswamy, G. and Chi, D. (2006). Mast Cells: Methods and Protocols (NJ, USA: Humana Press).10.1385/1592599672Suche in Google Scholar

Kunori, Y., Koizumi, M., Masegi, T., Kasai, H., Kawabata, H., Yamazaki, Y., and Fukamizu, A. (2002). Rodent alpha-chymases are elastase-like proteases. Eur. J. Biochem. 269, 5921–5930.10.1046/j.1432-1033.2002.03316.xSuche in Google Scholar PubMed

Laurell, C.B. (1971). Is emphysema in alpha 1-antitrypsin deficiency a result of autodigestion? Scand. J. Clin. Lab. Invest. 28, 1–3.10.3109/00365517109090655Suche in Google Scholar PubMed

Lee, M., Calabresi, L., Chiesa, G., Franceschini, G., and Kovanen, P.T. (2002a). Mast cell chymase degrades apoE and apoA-II in apoA-I-knockout mouse plasma and reduces its ability to promote cellular cholesterol efflux. Arterioscler. Thromb. Vasc. Biol. 22, 1475–1481.10.1161/01.ATV.0000029782.84357.68Suche in Google Scholar

Lee, M., Sommerhoff, C.P., von Eckardstein, A., Zettl, F., Fritz, H., and Kovanen, P.T. (2002b). Mast cell tryptase degrades HDL and blocks its function as an acceptor of cellular cholesterol. Arterioscler. Thromb. Vasc. Biol. 22, 2086–2091.10.1161/01.ATV.0000041405.07367.B5Suche in Google Scholar PubMed

Lees, M., Taylor, D.J., and Woolley, D.E. (1994). Mast cell proteinases activate precursor forms of collagenase and stromelysin, but not of gelatinases A and B. Eur. J. Biochem. 223, 171–177.10.1111/j.1432-1033.1994.tb18980.xSuche in Google Scholar PubMed

Lieberman, J. (2010). Granzyme A activates another way to die. Immunol. Rev. 235, 93–104.10.1111/j.0105-2896.2010.00902.xSuche in Google Scholar PubMed PubMed Central

Lilla, J.N., Chen, C.C., Mukai, K., BenBarak, M.J., Franco, C.B., Kalesnikoff, J., Yu, M., Tsai, M., Piliponsky, A.M., and Galli, S.J. (2011). Reduced mast cell and basophil numbers and function in Cpa3-Cre; Mcl-1fl/fl mice. Blood 118, 6930–6938.10.1182/blood-2011-03-343962Suche in Google Scholar PubMed PubMed Central

Lindstedt, K.A., Wang, Y., Shiota, N., Saarinen, J., Hyytiainen, M., Kokkonen, J.O., Keski-Oja, J., and Kovanen, P.T. (2001). Activation of paracrine TGF-β1 signaling upon stimulation and degranulation of rat serosal mast cells: a novel function for chymase. FASEB J. 15, 1377–1388.10.1096/fj.00-0273comSuche in Google Scholar PubMed

Lohi, J., Harvima, I., and Keski-Oja, J. (1992). Pericellular substrates of human mast cell tryptase: 72,000 dalton gelatinase and fibronectin. J. Cell Biochem. 50, 337–349.10.1002/jcb.240500402Suche in Google Scholar PubMed

Longley, B.J., Tyrrell, L., Ma, Y., Williams, D.A., Halaban, R., Langley, K., Lu, H.S., and Schechter, N.M. (1997). Chymase cleavage of stem cell factor yields a bioactive, soluble product. Proc. Natl. Acad. Sci. USA 94, 9017–9021.10.1073/pnas.94.17.9017Suche in Google Scholar PubMed PubMed Central

Lunderius, C., Xiang, Z., Nilsson, G., and Hellman, L. (2000). Murine mast cell lines as indicators of early events in mast cell and basophil development. Eur. J. Immunol. 30, 3396–3402.10.1002/1521-4141(2000012)30:12<3396::AID-IMMU3396>3.0.CO;2-OSuche in Google Scholar

Lutzelschwab, C., Pejler, G., Aveskogh, M., and Hellman, L. (1997). Secretory granule proteases in rat mast cells. Cloning of 10 different serine proteases and a carboxypeptidase A from various rat mast cell populations. J. Exp. Med. 185, 13–29.10.1084/jem.185.1.13Suche in Google Scholar

Lutzelschwab, C., Huang, M.R., Kullberg, M.C., Aveskogh, M., and Hellman, L. (1998a). Characterization of mouse mast cell protease-8, the first member of a novel subfamily of mouse mast cell serine proteases, distinct from both the classical chymases and tryptases. Eur. J. Immunol. 28, 1022–1033.10.1002/(SICI)1521-4141(199803)28:03<1022::AID-IMMU1022>3.0.CO;2-1Suche in Google Scholar

Lutzelschwab, C., Lunderius, C., Enerback, L., and Hellman, L. (1998b). A kinetic analysis of the expression of mast cell protease mRNA in the intestines of Nippostrongylus brasiliensis-infected rats. Eur. J. Immunol. 28, 3730–3737.10.1002/(SICI)1521-4141(199811)28:11<3730::AID-IMMU3730>3.0.CO;2-0Suche in Google Scholar

Lyon, M.F. and Glenister, P.H. (1982). A new allele sash (Wsh) at the W-locus and a spontaneous recessive lethal in mice. Genet. Res. 39, 315–322.10.1017/S001667230002098XSuche in Google Scholar

MacDonald, G., Shi, L., Vande Velde, C., Lieberman, J., and Greenberg, A.H. (1999). Mitochondria-dependent and -independent regulation of granzyme B-induced apoptosis. J. Exp. Med. 189, 131–144.10.1084/jem.189.1.131Suche in Google Scholar

Mahrus, S. and Craik, C.S. (2005). Selective chemical functional probes of granzymes A and B reveal granzyme B is a major effector of natural killer cell-mediated lysis of target cells. Chem. Biol. 12, 567–577.10.1016/j.chembiol.2005.03.006Suche in Google Scholar

Mahrus, S., Kisiel, W., and Craik, C.S. (2004). Granzyme M is a regulatory protease that inactivates proteinase inhibitor 9, an endogenous inhibitor of granzyme B. J. Biol. Chem. 279, 54275–54282.10.1074/jbc.M411482200Suche in Google Scholar

Malaviya, R., Ikeda, T., Ross, E., and Abraham, S.N. (1996). Mast cell modulation of neutrophil influx and bacterial clearance at sites of infection through TNF-α. Nature 381, 77–80.10.1038/381077a0Suche in Google Scholar

Martinvalet, D., Zhu, P., and Lieberman, J. (2005). Granzyme A induces caspase-independent mitochondrial damage, a required first step for apoptosis. Immunity 22, 355–370.10.1016/j.immuni.2005.02.004Suche in Google Scholar

Matsumoto, R., Sali, A., Ghildyal, N., Karplus, M., and Stevens, R.L. (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, 19524–19531.10.1074/jbc.270.33.19524Suche in Google Scholar PubMed

McNeil, H.P., Reynolds, D.S., Schiller, V., Ghildyal, N., Gurley, D.S., Austen, K.F., and Stevens, R.L. (1992). Isolation, characterization, and transcription of the gene encoding mouse mast cell protease 7. Proc. Natl. Acad. Sci. USA 89, 11174–11178.10.1073/pnas.89.23.11174Suche in Google Scholar PubMed PubMed Central

Mellon, M.B., Frank, B.T., and Fang, K.C. (2002). Mast cell α-chymase reduces IgE recognition of birch pollen profilin by cleaving antibody-binding epitopes. J. Immunol. 168, 290–297.10.4049/jimmunol.168.1.290Suche in Google Scholar PubMed

Metkar, S.S., Menaa, C., Pardo, J., Wang, B., Wallich, R., Freudenberg, M., Kim, S., Raja, S.M., Shi, L., Simon, M.M., et al. (2008). Human and mouse granzyme A induce a proinflammatory cytokine response. Immunity 29, 720–733.10.1016/j.immuni.2008.08.014Suche in Google Scholar PubMed

Metz, M., Piliponsky, A.M., Chen, C.C., Lammel, V., Abrink, M., Pejler, G., Tsai, M., and Galli, S.J. (2006). Mast cells can enhance resistance to snake and honeybee venoms. Science 313, 526–530.10.1126/science.1128877Suche in Google Scholar PubMed

Mirza, H., Schmidt, V.A., Derian, C.K., Jesty, J., and Bahou, W.F. (1997). Mitogenic responses mediated through the proteinase-activated receptor-2 are induced by expressed forms of mast cell alpha- or beta-tryptases. Blood 90, 3914–3922.10.1182/blood.V90.10.3914Suche in Google Scholar

Miyasaki, K.T., Qu, X.D., Harwig, S.S., Cho, Y., and Lehrer, R.I. (1995). Identification of CG-1, a natural peptide antibiotic derived from human neutrophil cathepsin G. Adv. Dent. Res. 9, 63–66.10.1177/08959374950090011201Suche in Google Scholar PubMed

Miyazaki, M., Takai, S., Jin, D., and Muramatsu, M. (2006). Pathological roles of angiotensin II produced by mast cell chymase and the effects of chymase inhibition in animal models. Pharmacol. Ther. 112, 668–676.10.1016/j.pharmthera.2006.05.008Suche in Google Scholar PubMed

Mizutani, H., Schechter, N., Lazarus, G., Black, R.A., and Kupper, T.S. (1991). Rapid and specific conversion of precursor interleukin 1 beta (IL-1β) to an active IL-1 species by human mast cell chymase. J. Exp. Med. 174, 821–825.10.1084/jem.174.4.821Suche in Google Scholar PubMed PubMed Central

Molino, M., Barnathan, E.S., Numerof, R., Clark, J., Dreyer, M., Cumashi, A., Hoxie, J.A., Schechter, N., Woolkalis, M., and Brass, L.F. (1997). Interactions of mast cell tryptase with thrombin receptors and PAR-2. J. Biol. Chem. 272, 4043–4049.10.1074/jbc.272.7.4043Suche in Google Scholar PubMed

Moraes, T.J., Chow, C.W., and Downey, G.P. (2003). Proteases and lung injury. Crit. Care. Med. 31, S189–S194.10.1097/01.CCM.0000057842.90746.1ESuche in Google Scholar

Mukundan, C., Gurish, M.F., Austen, K.F., Hechtman, H.B., and Friend, D.S. (2001). Mast cell mediation of muscle and pulmonary injury following hindlimb ischemia-reperfusion. J. Histochem. Cytochem. 49, 1055–1056.10.1177/002215540104900813Suche in Google Scholar

Mullbacher, A., Ebnet, K., Blanden, R.V., Hla, R.T., Stehle, T., Museteanu, C., and Simon, M.M. (1996). Granzyme A is critical for recovery of mice from infection with the natural cytopathic viral pathogen, ectromelia. Proc. Natl. Acad. Sci. USA 93, 5783–5787.10.1073/pnas.93.12.5783Suche in Google Scholar

Mullbacher, A., Waring, P., Tha Hla, R., Tran, T., Chin, S., Stehle, T., Museteanu, C., and Simon, M.M. (1999). Granzymes are the essential downstream effector molecules for the control of primary virus infections by cytolytic leukocytes. Proc. Natl. Acad. Sci. USA 96, 13950–13955.10.1073/pnas.96.24.13950Suche in Google Scholar

Muller, U., Sobek, V., Balkow, S., Holscher, C., Mullbacher, A., Museteanu, C., Mossmann, H., and Simon, M.M. (2003). Concerted action of perforin and granzymes is critical for the elimination of Trypanosoma cruzi from mouse tissues, but prevention of early host death is in addition dependent on the FasL/Fas pathway. Eur. J. Immunol. 33, 70–78.10.1002/immu.200390009Suche in Google Scholar

Musch, W., Wege, A.K., Mannel, D.N., and Hehlgans, T. (2008). Generation and characterization of alpha-chymase-Cre transgenic mice. Genesis 46, 163–166.10.1002/dvg.20378Suche in Google Scholar

Nagata, N., Niwa, Y., and Nakaya, Y. (2000). A novel 31-amino-acid-length endothelin, ET-1(1–31), can act as a biologically active peptide for vascular smooth muscle cells. Biochem. Biophys. Res. Commun. 275, 595–600.10.1006/bbrc.2000.3292Suche in Google Scholar

Nakano, A., Kishi, F., Minami, K., Wakabayashi, H., Nakaya, Y., and Kido, H. (1997). Selective conversion of big endothelins to tracheal smooth muscle-constricting 31-amino acid-length endothelins by chymase from human mast cells. J. Immunol. 159, 1987–1992.10.4049/jimmunol.159.4.1987Suche in Google Scholar

Omoto, Y., Tokime, K., Yamanaka, K., Habe, K., Morioka, T., Kurokawa, I., Tsutsui, H., Yamanishi, K., Nakanishi, K., and Mizutani, H. (2006). Human mast cell chymase cleaves pro-IL-18 and generates a novel and biologically active IL-18 fragment. J. Immunol. 177, 8315–8319.10.4049/jimmunol.177.12.8315Suche in Google Scholar

Pao, L.I., Sumaria, N., Kelly, J.M., van Dommelen, S., Cretney, E., Wallace, M.E., Anthony, D.A., Uldrich, A.P., Godfrey, D.I., Papadimitriou, J.M., et al. (2005). Functional analysis of granzyme M and its role in immunity to infection. J. Immunol. 175, 3235–3243.10.4049/jimmunol.175.5.3235Suche in Google Scholar

Pardo, J., Balkow, S., Anel, A., and Simon, M.M. (2002). Granzymes are essential for natural killer cell-mediated and perf-facilitated tumor control. Eur. J. Immunol. 32, 2881–2887.10.1002/1521-4141(2002010)32:10<2881::AID-IMMU2881>3.0.CO;2-KSuche in Google Scholar

Pardo, J., Bosque, A., Brehm, R., Wallich, R., Naval, J., Mullbacher, A., Anel, A., and Simon, M.M. (2004). Apoptotic pathways are selectively activated by granzyme A and/or granzyme B in CTL-mediated target cell lysis. J. Cell Biol. 167, 457–468.10.1083/jcb.200406115Suche in Google Scholar

Pardo, J., Wallich, R., Ebnet, K., Iden, S., Zentgraf, H., Martin, P., Ekiciler, A., Prins, A., Mullbacher, A., Huber, M., et al. (2007). Granzyme B is expressed in mouse mast cells in vivo and in vitro and causes delayed cell death independent of perforin. Cell Death Differ. 14, 1768–1779.10.1038/sj.cdd.4402183Suche in Google Scholar

Pejler, G., Abrink, M., Ringvall, M., and Wernersson, S. (2007). Mast cell proteases. Adv. Immunol. 95, 167–255.10.1016/S0065-2776(07)95006-3Suche in Google Scholar

Pejler, G., Ronnberg, E., Waern, I., and Wernersson, S. (2010). Mast cell proteases: multifaceted regulators of inflammatory disease. Blood 115, 4981–4990.10.1182/blood-2010-01-257287Suche in Google Scholar

Pereira, P.J., Bergner, A., Macedo-Ribeiro, S., Huber, R., Matschiner, G., Fritz, H., Sommerhoff, C.P., and Bode, W. (1998). Human beta-tryptase is a ring-like tetramer with active sites facing a central pore. Nature 392, 306–311.10.1038/32703Suche in Google Scholar

Perera, N.C., Schilling, O., Kittel, H., Back, W., Kremmer, E., and Jenne, D.E. (2012). NSP4, an elastase-related protease in human neutrophils with arginine specificity. Proc. Natl. Acad. Sci. USA 109, 6229–6234.10.1073/pnas.1200470109Suche in Google Scholar

Perona, J.J. and Craik, C.S. (1997). Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold. J. Biol. Chem. 272, 29987–29990.10.1074/jbc.272.48.29987Suche in Google Scholar

Pham, C.T., MacIvor, D.M., Hug, B.A., Heusel, J.W., and Ley, T.J. (1996). Long-range disruption of gene expression by a selectable marker cassette. Proc. Natl. Acad. Sci. USA 93, 13090–13095.10.1073/pnas.93.23.13090Suche in Google Scholar

Piliponsky, A.M., Chen, C.C., Rios, E.J., Treuting, P.M., Lahiri, A., Abrink, M., Pejler, G., Tsai, M., and Galli, S.J. (2012). The chymase mouse mast cell protease 4 degrades TNF, limits inflammation, and promotes survival in a model of sepsis. Am. J. Pathol. 181, 875–886.10.1016/j.ajpath.2012.05.013Suche in Google Scholar

Poe, M., Blake, J.T., Boulton, D.A., Gammon, M., Sigal, N.H., Wu, J.K., and Zweerink, H.J. (1991). Human cytotoxic lymphocyte granzyme B. Its purification from granules and the characterization of substrate and inhibitor specificity. J. Biol. Chem. 266, 98–103.10.1016/S0021-9258(18)52407-8Suche in Google Scholar

Poorafshar, M., Helmby, H., Troye-Blomberg, M., and Hellman, L. (2000). MMCP-8, the first lineage-specific differentiation marker for mouse basophils. Elevated numbers of potent IL-4-producing and MMCP-8-positive cells in spleens of malaria-infected mice. Eur. J. Immunol. 30, 2660–2668.10.1002/1521-4141(200009)30:9<2660::AID-IMMU2660>3.0.CO;2-ISuche in Google Scholar

Prager, E.M. (1996). Adaptive evolution of lysozyme: changes in amino acid sequence, regulation of expression and gene number. EXS 75, 323–345.10.1007/978-3-0348-9225-4_17Suche in Google Scholar

Praveen, K., Evans, D.L., and Jaso-Friedmann, L. (2004). Evidence for the existence of granzyme-like serine proteases in teleost cytotoxic cells. J. Mol. Evol. 58, 449–459.10.1007/s00239-003-2566-7Suche in Google Scholar

Praveen, K., Leary, J.H., 3rd, Evans, D.L., and Jaso-Friedmann, L. (2006a). Molecular characterization and expression of a granzyme of an ectothermic vertebrate with chymase-like activity expressed in the cytotoxic cells of Nile tilapia (Oreochromis niloticus). Immunogenetics 58, 41–55.10.1007/s00251-005-0063-4Suche in Google Scholar

Praveen, K., Leary, J.H., 3rd, Evans, D.L., and Jaso-Friedmann, L. (2006b). Nonspecific cytotoxic cells of teleosts are armed with multiple granzymes and other components of the granule exocytosis pathway. Mol. Immunol. 43, 1152–1162.10.1016/j.molimm.2005.07.027Suche in Google Scholar

Raman, K., Trivedi, N.N., Raymond, W.W., Ganesan, R., Kirchhofer, D., Verghese, G.M., Craik, C.S., Schneider, E.L., Nimishakavi, S., and Caughey, G.H. (2013). Mutational tail loss is an evolutionary mechanism for liberating marapsins and other type I serine proteases from transmembrane anchors. J. Biol. Chem. 288, 10588–10598.10.1074/jbc.M112.449033Suche in Google Scholar

Raymond, W.W., Sommerhoff, C.P., and Caughey, G.H. (2005). Mastin is a gelatinolytic mast cell peptidase resembling a mini-proteasome. Arch. Biochem. Biophys. 435, 311–322.10.1016/j.abb.2004.12.025Suche in Google Scholar

Raymond, W.W., Trivedi, N.N., Makarova, A., Ray, M., Craik, C.S., and Caughey, G.H. (2010). How immune peptidases change specificity: cathepsin G gained tryptic function but lost efficiency during primate evolution. J. Immunol. 185, 5360–5368.10.4049/jimmunol.1002292Suche in Google Scholar

Reber, L.L., Marichal, T., and Galli, S.J. (2012). New models for analyzing mast cell functions in vivo. Trends Immunol. 33, 613–625.10.1016/j.it.2012.09.008Suche in Google Scholar

Reimer, J.M., Enoksson, M., Samollow, P.B., and Hellman, L. (2008). Extended substrate specificity of opossum chymase-implications for the origin of mast cell chymases. Mol. Immunol. 45, 2116–2125.10.1016/j.molimm.2007.10.015Suche in Google Scholar

Reimer, J.M., Samollow, P.B., and Hellman, L. (2010). High degree of conservation of the multigene tryptase locus over the past 150–200 million years of mammalian evolution. Immunogenetics 62, 369–382.10.1007/s00251-010-0443-2Suche in Google Scholar

Revell, P.A., Grossman, W.J., Thomas, D.A., Cao, X., Behl, R., Ratner, J.A., Lu, Z.H., and Ley, T.J. (2005). Granzyme B and the downstream granzymes C and/or F are important for cytotoxic lymphocyte functions. J. Immunol. 174, 2124–2131.10.4049/jimmunol.174.4.2124Suche in Google Scholar

Reynolds, D.S., Stevens, R.L., Lane, W.S., Carr, M.H., Austen, K.F., and Serafin, W.E. (1990). Different mouse mast cell populations express various combinations of at least six distinct mast cell serine proteases. Proc. Natl. Acad. Sci. USA 87, 3230–3234.10.1073/pnas.87.8.3230Suche in Google Scholar

Reynolds, D.S., Gurley, D.S., Austen, K.F., and Serafin, W.E. (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, 3847–3853.10.1016/S0021-9258(19)67871-3Suche in Google Scholar

Rodewald, H.R. and Feyerabend, T.B. (2012). Widespread immunological functions of mast cells: fact or fiction? Immunity 37, 13–24.10.1016/j.immuni.2012.07.007Suche in Google Scholar PubMed

Romero, V., Fellows, E., Jenne, D.E., and Andrade, F. (2009). Cleavage of La protein by granzyme H induces cytoplasmic translocation and interferes with La-mediated HCV-IRES translational activity. Cell Death Differ. 16, 340–348.10.1038/cdd.2008.165Suche in Google Scholar PubMed

Ronnberg, E. and Pejler, G. (2012). Serglycin: the master of the mast cell. Methods Mol. Biol. 836, 201–217.10.1007/978-1-61779-498-8_14Suche in Google Scholar PubMed

Ronnberg, E., Melo, F.R., and Pejler, G. (2012). Mast cell proteoglycans. J. Histochem. Cytochem. 60, 950–962.10.1369/0022155412458927Suche in Google Scholar PubMed PubMed Central

Rottem, M., Okada, T., Goff, J.P., and Metcalfe, D.D. (1994). Mast cells cultured from the peripheral blood of normal donors and patients with mastocytosis originate from a CD34⁺/Fc ε RI- cell population. Blood 84, 2489–2496.10.1182/blood.V84.8.2489.2489Suche in Google Scholar

Rousalova, I. and Krepela, E. (2010). Granzyme B-induced apoptosis in cancer cells and its regulation. Int. J. Oncol. 37, 1361–1378.Suche in Google Scholar

Rukamp, B.J., Kam, C.M., Natarajan, S., Bolton, B.W., Smyth, M.J., Kelly, J.M., and Powers, J.C. (2004). Subsite specificities of granzyme M: a study of inhibitors and newly synthesized thiobenzyl ester substrates. Arch. Biochem. Biophys. 422, 9–22.10.1016/j.abb.2003.12.005Suche in Google Scholar PubMed

Saito, K., Muto, T., Tomimori, Y., Imajo, S., Maruoka, H., Tanaka, T., Yamashiro, K., and Fukuda, Y. (2003). Mouse mast cell protease-1 cleaves angiotensin I to form angiotensin II. Biochem. Biophys. Res. Commun. 302, 773–777.10.1016/S0006-291X(03)00263-8Suche in Google Scholar

Sali, A., Matsumoto, R., McNeil, H.P., Karplus, M., and Stevens, R.L. (1993). Three-dimensional models of four mouse mast cell chymases. Identification of proteoglycan binding regions and protease-specific antigenic epitopes. J. Biol. Chem. 268, 9023–9034.10.1016/S0021-9258(18)52973-2Suche in Google Scholar

Sayama, S., Iozzo, R.V., Lazarus, G.S., and Schechter, N.M. (1987). Human skin chymotrypsin-like proteinase chymase. Subcellular localization to mast cell granules and interaction with heparin and other glycosaminoglycans. J. Biol. Chem. 262, 6808–6815.10.1016/S0021-9258(18)48317-2Suche in Google Scholar

Sayers, T.J., Brooks, A.D., Ward, J.M., Hoshino, T., Bere, W.E., Wiegand, G.W., Kelly, J.M., and Smyth, M.J. (2001). The restricted expression of granzyme M in human lymphocytes. J. Immunol. 166, 765–771.10.4049/jimmunol.166.2.765Suche in Google Scholar

Schechter, I. and Berger, A. (1967). On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157–162.10.1016/S0006-291X(67)80055-XSuche in Google Scholar

Schneider, L.A., Schlenner, S.M., Feyerabend, T.B., Wunderlin, M., and Rodewald, H.R. (2007). Molecular mechanism of mast cell mediated innate defense against endothelin and snake venom sarafotoxin. J. Exp. Med. 204, 2629–2639.10.1084/jem.20071262Suche in Google Scholar

Schwartz, L.B. and Bradford, T.R. (1986). Regulation of tryptase from human lung mast cells by heparin. Stabilization of the active tetramer. J. Biol. Chem. 261, 7372–7379.10.1016/S0021-9258(17)38401-6Suche in Google Scholar

Schwartz, L.B., Bradford, T.R., Littman, B.H., and Wintroub, B.U. (1985). The fibrinogenolytic activity of purified tryptase from human lung mast cells. J. Immunol. 135, 2762–2767.10.4049/jimmunol.135.4.2762Suche in Google Scholar

Schwartz, L.B., Irani, A.M., Roller, K., Castells, M.C., and Schechter, N.M. (1987). Quantitation of histamine, tryptase, and chymase in dispersed human T and TC mast cells. J. Immunol. 138, 2611–2615.10.4049/jimmunol.138.8.2611Suche in Google Scholar

Scudamore, C.L., Thornton, E.M., McMillan, L., Newlands, G.F., and Miller, H.R. (1995). Release of the mucosal mast cell granule chymase, rat mast cell protease-II, during anaphylaxis is associated with the rapid development of paracellular permeability to macromolecules in rat jejunum. J. Exp. Med. 182, 1871–1881.10.1084/jem.182.6.1871Suche in Google Scholar

Secor, V.H., Secor, W.E., Gutekunst, C.A., and Brown, M.A. (2000). Mast cells are essential for early onset and severe disease in a murine model of multiple sclerosis. J. Exp. Med. 191, 813–822.10.1084/jem.191.5.813Suche in Google Scholar

Shafer, W.M., Pohl, J., Onunka, V.C., Bangalore, N., and Travis, J. (1991). Human lysosomal cathepsin G and granzyme B share a functionally conserved broad spectrum antibacterial peptide. J. Biol. Chem. 266, 112–116.10.1016/S0021-9258(18)52409-1Suche in Google Scholar

Shafer, W.M., Katzif, S., Bowers, S., Fallon, M., Hubalek, M., Reed, M.S., Veprek, P., and Pohl, J. (2002). Tailoring an antibacterial peptide of human lysosomal cathepsin G to enhance its broad-spectrum action against antibiotic-resistant bacterial pathogens. Curr. Pharm. Des. 8, 695–702.10.2174/1381612023395376Suche in Google Scholar

Shi, L., Wu, L., Wang, S., and Fan, Z. (2009). Granzyme F induces a novel death pathway characterized by Bid-independent cytochrome c release without caspase activation. Cell Death Differ. 16, 1694–1706.10.1038/cdd.2009.101Suche in Google Scholar

Shin, K., Watts, G.F., Oettgen, H.C., Friend, D.S., Pemberton, A.D., Gurish, M.F., and Lee, D.M. (2008). Mouse mast cell tryptase mMCP-6 is a critical link between adaptive and innate immunity in the chronic phase of Trichinella spiralis infection. J. Immunol. 180, 4885–4891.10.4049/jimmunol.180.7.4885Suche in Google Scholar

Shresta, S., MacIvor, D.M., Heusel, J.W., Russell, J.H., and Ley, T.J. (1995). Natural killer and lymphokine-activated killer cells require granzyme B for the rapid induction of apoptosis in susceptible target cells. Proc. Natl. Acad. Sci. USA 92, 5679–5683.10.1073/pnas.92.12.5679Suche in Google Scholar

Smyth, M.J., O’Connor, M.D., Trapani, J.A., Kershaw, M.H., and Brinkworth, R.I. (1996). A novel substrate-binding pocket interaction restricts the specificity of the human NK cell-specific serine protease, Met-ase-1. J. Immunol. 156, 4174–4181.10.4049/jimmunol.156.11.4174Suche in Google Scholar

Sorensen, O.E., Follin, P., Johnsen, A.H., Calafat, J., Tjabringa, G.S., Hiemstra, P.S., and Borregaard, N. (2001). Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 97, 3951–3959.10.1182/blood.V97.12.3951Suche in Google Scholar

Soto, D., Malmsten, C., Blount, J.L., Muilenburg, D.J., and Caughey, G.H. (2002). Genetic deficiency of human mast cell α-tryptase. Clin. Exp. Allergy 32, 1000–1006.10.1046/j.1365-2222.2002.01416.xSuche in Google Scholar

Sperr, W.R., Jordan, J.H., Baghestanian, M., Kiener, H.P., Samorapoompichit, P., Semper, H., Hauswirth, A., Schernthaner, G.H., Chott, A., Natter, S., et al. (2001). Expression of mast cell tryptase by myeloblasts in a group of patients with acute myeloid leukemia. Blood 98, 2200–2209.10.1182/blood.V98.7.2200Suche in Google Scholar

Stack, M.S. and Johnson, D.A. (1994). Human mast cell tryptase activates single-chain urinary-type plasminogen activator (pro-urokinase). J. Biol. Chem. 269, 9416–9419.10.1016/S0021-9258(17)36896-5Suche in Google Scholar

Standish, A.J. and Weiser, J.N. (2009). Human neutrophils kill Streptococcus pneumoniae via serine proteases. J. Immunol. 183, 2602–2609.10.4049/jimmunol.0900688Suche in Google Scholar PubMed

Stelekati, E., Bahri, R., D’Orlando, O., Orinska, Z., Mittrucker, H.W., Langenhaun, R., Glatzel, M., Bollinger, A., Paus, R., and Bulfone-Paus, S. (2009). Mast cell-mediated antigen presentation regulates CD8⁺ T cell effector functions. Immunity 31, 665–676.10.1016/j.immuni.2009.08.022Suche in Google Scholar PubMed

Stevens, R.L. and Adachi, R. (2007). Protease-proteoglycan complexes of mouse and human mast cells and importance of their β-tryptase-heparin complexes in inflammation and innate immunity. Immunol. Rev. 217, 155–167.10.1111/j.1600-065X.2007.00525.xSuche in Google Scholar

Stevens, R.L., Friend, D.S., McNeil, H.P., Schiller, V., Ghildyal, N., and Austen, K.F. (1994). Strain-specific and tissue-specific expression of mouse mast cell secretory granule proteases. Proc. Natl. Acad. Sci. USA 91, 128–132.10.1073/pnas.91.1.128Suche in Google Scholar

Stevens, R.L., Qui, D., McNeil, H.P., Friend, D.S., Hunt, J.E., Austen, K.F., and Zhang, J. (1996). Transgenic mice that possess a disrupted mast cell protease 5 gene cannot store carboxypeptidase A in their granules. FASEB J. 10, A1307.Suche in Google Scholar

Stewart, C.B., Schilling, J.W., and Wilson, A.C. (1987). Adaptive evolution in the stomach lysozymes of foregut fermenters. Nature 330, 401–404.10.1038/330401a0Suche in Google Scholar

Sundstrom, G., Larsson, T.A., Brenner, S., Venkatesh, B., and Larhammar, D. (2008). Evolution of the neuropeptide Y family: new genes by chromosome duplications in early vertebrates and in teleost fishes. Gen. Comp. Endocrinol. 155, 705–716.10.1016/j.ygcen.2007.08.016Suche in Google Scholar

Susanto, O., Trapani, J.A., and Brasacchio, D. (2012). Controversies in granzyme biology. Tissue Antigens 80, 477–487.10.1111/tan.12014Suche in Google Scholar

Sutton, V.R., Vaux, D.L., and Trapani, J.A. (1997). Bcl-2 prevents apoptosis induced by perforin and granzyme B, but not that mediated by whole cytotoxic lymphocytes. J. Immunol. 158, 5783–5790.10.4049/jimmunol.158.12.5783Suche in Google Scholar

Taipale, J., Lohi, J., Saarinen, J., Kovanen, P.T., and Keski-Oja, J. (1995). Human mast cell chymase and leukocyte elastase release latent transforming growth factor-β1 from the extracellular matrix of cultured human epithelial and endothelial cells. J. Biol. Chem. 270, 4689–4696.10.1074/jbc.270.9.4689Suche in Google Scholar

Takai, S., Sakaguchi, M., Jin, D., Yamada, M., Kirimura, K., and Miyazaki, M. (2001). Different angiotensin II-forming pathways in human and rat vascular tissues. Clin. Chim. Acta 305, 191–195.10.1016/S0009-8981(01)00379-5Suche in Google Scholar

Tam, E.K. and Caughey, G.H. (1990). Degradation of airway neuropeptides by human lung tryptase. Am. J. Respir. Cell. Mol. Biol. 3, 27–32.10.1165/ajrcmb/3.1.27Suche in Google Scholar PubMed

Tani, K., Ogushi, F., Kido, H., Kawano, T., Kunori, Y., Kamimura, T., Cui, P., and Sone, S. (2000). Chymase is a potent chemoattractant for human monocytes and neutrophils. J. Leukoc. Biol. 67, 585–589.10.1002/jlb.67.4.585Suche in Google Scholar PubMed

Tchougounova, E., Pejler, G., and Abrink, M. (2003). The chymase, mouse mast cell protease 4, constitutes the major chymotrypsin-like activity in peritoneum and ear tissue. A role for mouse mast cell protease 4 in thrombin regulation and fibronectin turnover. J. Exp. Med. 198, 423–431.10.1084/jem.20030671Suche in Google Scholar PubMed PubMed Central

Tchougounova, E., Lundequist, A., Fajardo, I., Winberg, J.O., Abrink, M., and Pejler, G. (2005). A key role for mast cell chymase in the activation of pro-matrix metalloprotease-9 and pro-matrix metalloprotease-2. J. Biol. Chem. 280, 9291–9296.10.1074/jbc.M410396200Suche in Google Scholar

Terakawa, M., Tomimori, Y., Goto, M., and Fukuda, Y. (2006). Mast cell chymase induces expression of chemokines for neutrophils in eosinophilic EoL-1 cells and mouse peritonitis eosinophils. Eur. J. Pharmacol. 538, 175–181.10.1016/j.ejphar.2006.03.053Suche in Google Scholar

Thakurdas, S.M., Melicoff, E., Sansores-Garcia, L., Moreira, D.C., Petrova, Y., Stevens, R.L., and Adachi, R. (2007). The mast cell-restricted tryptase mMCP-6 has a critical immunoprotective role in bacterial infections. J. Biol. Chem. 282, 20809–20815.10.1074/jbc.M611842200Suche in Google Scholar

Thorpe, M., Yu, J., Boinapally, V., Ahooghalandari, P., Kervinen, J., Garavilla, L.D., and Hellman, L. (2012). Extended cleavage specificity of the mast cell chymase from the crab-eating macaque (Macaca fascicularis): an interesting animal model for the analysis of the function of the human mast cell chymase. Int. Immunol. 24, 771–782.10.1093/intimm/dxs081Suche in Google Scholar

Tkalcevic, J., Novelli, M., Phylactides, M., Iredale, J.P., Segal, A.W., and Roes, J. (2000). Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G. Immunity 12, 201–210.10.1016/S1074-7613(00)80173-9Suche in Google Scholar

Trivedi, N.N., Tong, Q., Raman, K., Bhagwandin, V.J., and Caughey, G.H. (2007). Mast cell α and β tryptases changed rapidly during primate speciation and evolved from γ-like transmembrane peptidases in ancestral vertebrates. J. Immunol. 179, 6072–6079.10.4049/jimmunol.179.9.6072Suche in Google Scholar PubMed PubMed Central

Trivedi, N.N., Raymond, W.W., and Caughey, G.H. (2008). Chimerism, point mutation, and truncation dramatically transformed mast cell delta-tryptases during primate evolution. J. Allergy Clin. Immunol. 121, 1262–1268.10.1016/j.jaci.2008.01.019Suche in Google Scholar PubMed

Trivedi, N.N., Tamraz, B., Chu, C., Kwok, P.Y., and Caughey, G.H. (2009). Human subjects are protected from mast cell tryptase deficiency despite frequent inheritance of loss-of-function mutations. J. Allergy Clin. Immunol. 124, 1099–1105, e1091–e1094.10.1016/j.jaci.2009.07.026Suche in Google Scholar PubMed PubMed Central

Tschopp, C.M., Spiegl, N., Didichenko, S., Lutmann, W., Julius, P., Virchow, J.C., Hack, C.E., and Dahinden, C.A. (2006). Granzyme B, a novel mediator of allergic inflammation: its induction and release in blood basophils and human asthma. Blood 108, 2290–2299.10.1182/blood-2006-03-010348Suche in Google Scholar PubMed

Ugajin, T., Kojima, T., Mukai, K., Obata, K., Kawano, Y., Minegishi, Y., Eishi, Y., Yokozeki, H., and Karasuyama, H. (2009). Basophils preferentially express mouse mast cell protease 11 among the mast cell tryptase family in contrast to mast cells. J. Leukoc. Biol. 86, 1417–1425.10.1189/jlb.0609400Suche in Google Scholar PubMed

Van Damme, P., Maurer-Stroh, S., Hao, H., Colaert, N., Timmerman, E., Eisenhaber, F., Vandekerckhove, J., and Gevaert, K. (2010). The substrate specificity profile of human granzyme A. Biol. Chem. 391, 983–997.Suche in Google Scholar

van Domselaar, R. and Bovenschen, N. (2011). Cell death-independent functions of granzymes: hit viruses where it hurts. Rev. Med. Virol. 21, 301–314.10.1002/rmv.697Suche in Google Scholar

Velin, D., Bachmann, D., Bouzourene, H., and Michetti, P. (2005). Mast cells are critical mediators of vaccine-induced Helicobacter clearance in the mouse model. Gastroenterology 129, 142–155.10.1053/j.gastro.2005.04.010Suche in Google Scholar

Vethanayagam, R.R., Almyroudis, N.G., Grimm, M.J., Lewandowski, D.C., Pham, C.T., Blackwell, T.S., Petraitiene, R., Petraitis, V., Walsh, T.J., Urban, C.F., et al. (2011). Role of NADPH oxidase versus neutrophil proteases in antimicrobial host defense. PLoS One 6, e28149.10.1371/journal.pone.0028149Suche in Google Scholar

Voehringer, D. (2013). Protective and pathological roles of mast cells and basophils. Nat. Rev. Immunol. 13, 362–375.10.1038/nri3427Suche in Google Scholar

Waern, I., Jonasson, S., Hjoberg, J., Bucht, A., Abrink, M., Pejler, G., and Wernersson, S. (2009). Mouse mast cell protease 4 is the major chymase in murine airways and has a protective role in allergic airway inflammation. J. Immunol. 183, 6369–6376.10.4049/jimmunol.0900180Suche in Google Scholar

Waern, I., Karlsson, I., Thorpe, M., Schlenner, S.M., Feyerabend, T.B., Rodewald, H.R., Abrink, M., Hellman, L., Pejler, G., and Wernersson, S. (2012). Mast cells limit extracellular levels of IL-13 via a serglycin proteoglycan-serine protease axis. Biol. Chem. 393, 1555–1567.10.1515/hsz-2012-0189Suche in Google Scholar

Wastling, J.M., Knight, P., Ure, J., Wright, S., Thornton, E.M., Scudamore, C.L., Mason, J., Smith, A., and Miller, H.R. (1998). Histochemical and ultrastructural modification of mucosal mast cell granules in parasitized mice lacking the β-chymase, mouse mast cell protease-1. Am. J. Pathol. 153, 491–504.10.1016/S0002-9440(10)65592-7Suche in Google Scholar

Wernersson, S., Reimer, J.M., Poorafshar, M., Karlson, U., Wermenstam, N., Bengten, E., Wilson, M., Pilstrom, L., and Hellman, L. (2006). Granzyme-like sequences in bony fish shed light on the emergence of hematopoietic serine proteases during vertebrate evolution. Dev. Comp. Immunol. 30, 901–918.10.1016/j.dci.2005.10.014Suche in Google Scholar PubMed

Wintroub, B.U., Schechter, N.B., Lazarus, G.S., Kaempfer, C.E., and Schwartz, L.B. (1984). Angiotensin I conversion by human and rat chymotryptic proteinases. J. Invest. Dermatol. 83, 336–339.10.1111/1523-1747.ep12264144Suche in Google Scholar PubMed

Wong, G.W., Yasuda, S., Morokawa, N., Li, L., and Stevens, R.L. (2004). Mouse chromosome 17A3.3 contains 13 genes that encode functional tryptic-like serine proteases with distinct tissue and cell expression patterns. J. Biol. Chem. 279, 2438–2452.10.1074/jbc.M308209200Suche in Google Scholar PubMed

Xu, X., Zhang, D., Lyubynska, N., Wolters, P.J., Killeen, N.P., Baluk, P., McDonald, D.M., Hawgood, S., and Caughey, G.H. (2006). Mast cells protect mice from Mycoplasma pneumonia. Am. J. Respir. Crit. Care. Med. 173, 219–225.10.1164/rccm.200507-1034OCSuche in Google Scholar PubMed PubMed Central

Zhao, W., Oskeritzian, C.A., Pozez, A.L., and Schwartz, L.B. (2005). Cytokine production by skin-derived mast cells: endogenous proteases are responsible for degradation of cytokines. J. Immunol. 175, 2635–2642.10.4049/jimmunol.175.4.2635Suche in Google Scholar PubMed