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Gene Review

Ctsg  -  cathepsin G

Mus musculus

Synonyms: Cathepsin G, VSP, Vimentin-specific protease
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Disease relevance of Ctsg


High impact information on Ctsg

  • Serine protease cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering [6].
  • Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G [2].
  • We examined the role of leukocytic neutral proteinases by comparing the glomerular damage and albuminuria after injection of rabbit anti-mouse GBM antibodies in normal control mice (C57BL/6J, +/+) and in beige mice (C57BL/6J,bg/bg) in which PMN are deficient of the neutral proteinases elastase and cathepsin G [7].
  • Elicited peritoneal neutrophils of beige (Chediak-Higashi) mice essentially lack activities of the neutral serine proteinases elastase and cathepsin G, which may explain the increased susceptibility to infection of beige mice and Chediak-Higashi patients [8].
  • The results of several experiments indicate that neutrophils were the sole source of elastase and cathepsin G in bone marrow [8].

Chemical compound and disease context of Ctsg

  • Using a murine model of endobronchial inflammation, we found that a different neutrophil-derived serine protease, cathepsin G, inhibited the host's ability to clear Pseudomonas from the lung, based on a 1-log reduction in bacteria recovered from cathepsin G-deficient mice [5].

Biological context of Ctsg

  • Hematopoiesis in cathepsin G-/- mice is normal, and the mice have no overt abnormalities in blood clotting [1].
  • Neutrophils derived from cathepsin G-/- mice have normal morphology and azurophil granule composition; these neutrophils also display normal phagocytosis and superoxide production and have normal chemotactic responses to C5a, fMLP, and interleukin-8 [1].
  • In contrast, a targeted mutation of the promyelocyte-specific cathepsin G gene (which lies just 3' to the granzyme genes in the same cluster) had minimal effects on upstream granzyme gene expression [9].
  • Because the transgene includes only 6 kb of regulatory sequences from the human cathepsin G locus, we hypothesized that sequences required for high-level expression of the transgene might be located elsewhere in the cathepsin G locus and that a knock-in model might yield much higher expression levels and higher penetrance of disease [3].
  • 2. Although the murine orthologue of human granzyme H has not yet been identified, murine granzymes C, D, E, F, and G also lie between the murine granzyme B and cathepsin G genes on murine chromosome 14; murine granzymes C, D, and F are also highly expressed in LAK cells, but minimally in cytotoxic T lymphocytes (CTL) [10].

Anatomical context of Ctsg


Associations of Ctsg with chemical compounds

  • This protective effect correlates with the inactivation of neutrophil-derived serine proteases, since NE(-/-) x CG(-/-) mice are equally resistant to arthritis induction by anti-collagen antibodies [12].
  • Cartilage proteoglycan depletion was quantified by measuring the decrease in safranin O staining intensity, and this, too, was unaltered in mice lacking elastase and cathepsin G [13].
  • Elastase and cathepsin G activities were assayed with the specific synthetic substrates MeO-Suc-Ala-Ala-Pro-Val-MCA and Suc-Ala-Ala-Pro-Phe-pNA, respectively [14].
  • Complex formation is maximal at a 1:1 molar ratio of cathepsin G to alpha 1-antichymotrypsin (alpha 1-ACT) as revealed by sodium dodecyl sulfate-gel electrophoresis and autoradiography [15].
  • Injection of cathepsin G in BALB/c mice immunized with keyhole limpet hemocyanin (KLH) adsorbed to aluminum hydroxide resulted in a significantly increased production of KLH-specific IgG1 and IgG2a antibodies [16].

Other interactions of Ctsg


Analytical, diagnostic and therapeutic context of Ctsg


  1. Normal neutrophil function in cathepsin G-deficient mice. MacIvor, D.M., Shapiro, S.D., Pham, C.T., Belaaouaj, A., Abraham, S.N., Ley, T.J. Blood (1999) [Pubmed]
  2. Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G. Tkalcevic, J., Novelli, M., Phylactides, M., Iredale, J.P., Segal, A.W., Roes, J. Immunity (2000) [Pubmed]
  3. High-penetrance mouse model of acute promyelocytic leukemia with very low levels of PML-RARalpha expression. Westervelt, P., Lane, A.A., Pollock, J.L., Oldfather, K., Holt, M.S., Zimonjic, D.B., Popescu, N.C., DiPersio, J.F., Ley, T.J. Blood (2003) [Pubmed]
  4. Mutants of plasminogen activator inhibitor-1 designed to inhibit neutrophil elastase and cathepsin G are more effective in vivo than their endogenous inhibitors. Stefansson, S., Yepes, M., Gorlatova, N., Day, D.E., Moore, E.G., Zabaleta, A., McMahon, G.A., Lawrence, D.A. J. Biol. Chem. (2004) [Pubmed]
  5. Cathepsin-G Interferes with Clearance of Pseudomonas aeruginosa from Mouse Lungs. Sedor, J., Hogue, L., Akers, K., Boslaugh, S., Schreiber, J., Ferkol, T. Pediatr. Res. (2007) [Pubmed]
  6. Serine protease cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering. Raptis, S.Z., Shapiro, S.D., Simmons, P.M., Cheng, A.M., Pham, C.T. Immunity (2005) [Pubmed]
  7. Antiglomerular basement membrane nephritis in beige mice. Deficiency of leukocytic neutral proteinases prevents the induction of albuminuria in the heterologous phase. Schrijver, G., Schalkwijk, J., Robben, J.C., Assmann, K.J., Koene, R.A. J. Exp. Med. (1989) [Pubmed]
  8. Elastase and cathepsin G activities are present in immature bone marrow neutrophils and absent in late marrow and circulating neutrophils of beige (Chediak-Higashi) mice. Takeuchi, K.H., McGarry, M.P., Swank, R.T. J. Exp. Med. (1987) [Pubmed]
  9. Long-range disruption of gene expression by a selectable marker cassette. Pham, C.T., MacIvor, D.M., Hug, B.A., Heusel, J.W., Ley, T.J. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  10. The 5' flanking region of the human granzyme H gene directs expression to T/natural killer cell progenitors and lymphokine-activated killer cells in transgenic mice. MacIvor, D.M., Pham, C.T., Ley, T.J. Blood (1999) [Pubmed]
  11. Expression of cathepsin G-like and alpha 1-antichymotrypsin-like proteins in reactive astrocytes. Abraham, C.R., Kanemaru, K., Mucke, L. Brain Res. (1993) [Pubmed]
  12. Dipeptidyl peptidase I activates neutrophil-derived serine proteases and regulates the development of acute experimental arthritis. Adkison, A.M., Raptis, S.Z., Kelley, D.G., Pham, C.T. J. Clin. Invest. (2002) [Pubmed]
  13. Pathogenesis of antigen-induced arthritis in mice deficient in neutrophil elastase and cathepsin G. Pettipher, R., Edwards, J., Cruwys, S., Jessup, E., Beesley, J., Henderson, B. Am. J. Pathol. (1990) [Pubmed]
  14. Lysosomal elastase and cathepsin G in beige mice. Neutrophils of beige (Chediak-Higashi) mice selectively lack lysosomal elastase and cathepsin G. Takeuchi, K., Wood, H., Swank, R.T. J. Exp. Med. (1986) [Pubmed]
  15. A receptor for cathepsin G:alpha 1-antichymotrypsin complexes on mouse spinal cord astrocytes. Chen, M., Conn, K.J., Festoff, B.W. Neurology (1993) [Pubmed]
  16. The neutrophil granule protein cathepsin G activates murine T lymphocytes and upregulates antigen-specific IG production in mice. Tani, K., Murphy, W.J., Chertov, O., Oppenheim, J.J., Wang, J.M. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  17. Characterization of cDNA clones encoding mouse proteinase 3 (myeloblastine) and cathepsin G. Aveskogh, M., Lützelschwab, C., Huang, M.R., Hellman, L. Immunogenetics (1997) [Pubmed]
  18. Deficient transcription of mouse mast cell protease 4 gene in mutant mice of mi/mi genotype. Jippo, T., Lee, Y.M., Katsu, Y., Tsujino, K., Morii, E., Kim, D.K., Kim, H.M., Kitamura, Y. Blood (1999) [Pubmed]
  19. Neutrophil lysosomal dysfunctions in mutant C57 Bl/6J mice: interstrain variations in content of lysosomal elastase, cathepsin G and their inhibitors. Gardi, C., Cavarra, E., Calzoni, P., Marcolongo, P., de Santi, M., Martorana, P.A., Lungarella, G. Biochem. J. (1994) [Pubmed]
  20. Granzyme-like sequences in bony fish shed light on the emergence of hematopoietic serine proteases during vertebrate evolution. Wernersson, S., Reimer, J.M., Poorafshar, M., Karlson, U., Wermenstam, N., Bengtén, E., Wilson, M., Pilström, L., Hellman, L. Dev. Comp. Immunol. (2006) [Pubmed]
  21. Trichuris suis: a secretory chymotrypsin/elastase inhibitor with potential as an immunomodulator. Rhoads, M.L., Fetterer, R.H., Hill, D.E., Urban, J.F. Exp. Parasitol. (2000) [Pubmed]
  22. Molecular cloning, chromosomal location, and tissue-specific expression of the murine cathepsin G gene. Heusel, J.W., Scarpati, E.M., Jenkins, N.A., Gilbert, D.J., Copeland, N.G., Shapiro, S.D., Ley, T.J. Blood (1993) [Pubmed]
  23. Genomic organization and chromosomal localization of the human cathepsin G gene. Hohn, P.A., Popescu, N.C., Hanson, R.D., Salvesen, G., Ley, T.J. J. Biol. Chem. (1989) [Pubmed]
  24. Neutrophils in beige mice secrete normal amounts of cathepsin G and a 46 kDa latent form of elastase that can be activated extracellularly by proteolytic activity. Cavarra, E., Martorana, P.A., Cortese, S., Gambelli, F., Di Simplicio, P., Lungarella, G. Biol. Chem. (1997) [Pubmed]
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