Cleaved SLPI, a novel biomarker of chymase activity. Search in Google ScholarД«elkowski, S.M., Masucci, J., Mahan, A., Kervinen, J., Olson, M., de Garavilla, L., and DвЂ™Andrea, M.R. Characterization of cDNA clones encoding mouse proteinase 3 (myeloblastine) and cathepsin G. Search in Google ScholarДЄveskogh, M., Lutzelschwab, C., Huang, M.R., and Hellman, L. Granzyme H destroys the function of critical adenoviral proteins required for viral DNA replication and granzyme B inhibition.

Search in Google ScholarДЄndrade, F., Fellows, E., Jenne, D.E., Rosen, A., and Young, C.S. Arg143 and Lys192 of the human mast cell chymase mediate the preference for acidic amino acids in position P2вЂІ of substrates. Search in Google ScholarДЄndersson, M.K., Thorpe, M., and Hellman, L. The extended substrate specificity of the human mast cell chymase reveals a serine protease with well-defined substrate recognition profile. Search in Google ScholarДЄndersson, M.K., Enoksson, M., Gallwitz, M., and Hellman, L. Extended cleavage specificity of mMCP-1, the major mucosal mast cell protease in mouse-high specificity indicates high substrate selectivity. Search in Google ScholarДЄndersson, M.K., Pemberton, A.D., Miller, H.R., and Hellman, L. The extended cleavage specificity of the rodent ОІ-chymases rMCP-1 and mMCP-4 reveal major functional similarities to the human mast cell chymase. Search in Google ScholarДЄndersson, M.K., Karlson, U., and Hellman, L. Mast cell chymase reduces the toxicity of Gila monster venom, scorpion venom, and vasoactive intestinal polypeptide in mice. Search in Google ScholarДЄkahoshi, 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. Mutations in Arg143 and Lys192 of the human mast cell chymase markedly affect the activity of five potent human chymase inhibitors. Search in Google ScholarДЄhooghalandari, P., Hanke, N., Thorpe, M., Witte, A., Messinger, J., and Hellman, L. Mast cell protease 5 mediates ischemia-reperfusion injury of mouse skeletal muscle. The in vivo substrates and functions are a particular challenging issue because several of these enzymes have a relatively broad specificity and may therefore cleave a wide range of different substrates.Д¬orresponding author: Lars Hellman, Department of Cell and Molecular Biology, Biomedical Center, Uppsala University, Box 596, S-751 24 Uppsala, Sweden, e-mail: 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. This review focuses on the appearance of these proteases during vertebrate evolution, their primary and extended cleavage specificities, and their potential in vivo substrates. T cells and NK cells express between 5 and 14 different granzymes, depending on the species, and these enzymes have tryptase, asp-ase, chymase, and met-ase specificities. Neutrophils have several enzymes with chymase, elastase, and tryptase specificities. Mast cells primarily express chymases and tryptases with chymotryptic or tryptic primary cleavage specificities, respectively. A very broad spectrum of primary cleavage specificities has also been observed, including chymase, tryptase, asp-ase, elastase, and met-ase specificities, which highlights the large flexibility in the active site of these proteases. A number of very diverse functions have been identified for these proteases, including apoptosis induction, blood pressure regulation, inactivation of insect and snake toxins, intestinal parasite expulsion, killing of bacteria and fungi, induction, mobilization, or degradation of cytokines, and the degradation of connective tissue components. In mast cells, these proteases can account for up to 35% of the total cellular protein, and the absolute majority of these belong to the chymotrypsin-related serine protease family. Cells from several of the hematopoietic cell lineages including mast cells, basophils, neutrophils, cytotoxic T cells, and natural killer (NK) cells store proteases at very high levels within their cytoplasmic granules.

Qwock platypus evolution