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Ctsc  -  cathepsin C

Mus musculus

Synonyms: AI047818, Cathepsin C, Cathepsin J, DPP-I, DPP1, ...
 
 
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Disease relevance of Ctsc

 

High impact information on Ctsc

 

Biological context of Ctsc

  • The deduced amino acid sequence of S. japonicum cathepsin C comprised 458 amino acid residues; 22 NH2-terminal residues corresponding to the signal peptide, 199 residues corresponding to the propeptide and 237 COOH-terminal residues corresponding to the mature enzyme region [6].
  • The preproenzyme shared only 59% identity with the sequence for a cathepsin C reported from Schistosoma mansoni, differing from it in active-site residues and in its potential N-glycosylation sites [6].
  • DPPI therefore plays an essential role in the in vivo processing and activation of granzymes A and B, which are required for cytotoxic lymphocyte granule-mediated apoptosis [7].
  • Using fluorescence in situ chromosome hybridization, we localized murine DPPI to chromosome 7D3-E1 [8].
  • The DPPI gene consists of seven exons and 6 introns, and spans approximately 20 kilobases [8].
 

Anatomical context of Ctsc

  • Specifically, there is no accumulation of neutrophils in the joints of DPPI(-/-) mice [1].
  • DPPI activity, and the relative size and amounts of DPPI heavy and light chains, were identical in mast cells from wild-type and cathepsin L/S double-null mice [9].
  • In this report, we show that cytotoxic lymphocytes derived from DPPI-/- mice contain normal amounts of granzymes A and B, but these molecules retain their prodipeptide domains and are inactive [7].
  • CONCLUSION: These results indicate that DPPI regulates a critical step in the development of CIA that is independent of T cell and B cell functions [10].
  • We have isolated a cDNA coding for murine DPPI from mouse thymus and spleen cDNA libraries [8].
 

Associations of Ctsc with chemical compounds

  • The cysteine protease dipeptidyl peptidase I (DPPI) activates granule-associated immune-cell serine proteases [9].
  • These findings indicate that DPPI is not essential for mMCP-6 activation but does influence the total amount of active mMCP-6 in mast cells and therefore may be an important, but not exclusive mechanism for tryptase activation [11].
  • The absence of DPPI and chymase activity does not affect the growth, granularity, or staining characteristics of BMMCs and, despite prior predictions, does not alter IgE-mediated exocytosis of histamine [11].
  • Using DPPI cDNA, we obtained two BAC (Bacterial Artificial Chromosome) clones that contained the murine DPPI locus [8].
  • Leupeptin administration induced a strong inhibition of cathepsin B and a moderate inhibition of cathepsin C and acid autolytic rate in mouse liver 1 hr after injection [4].
  • These findings suggest that DPPI and/or granule-associated serine proteases are necessary for neutrophil recruitment into the diseased aorta and that these proteases act to amplify vascular wall inflammation that leads to AAAs [12].
 

Regulatory relationships of Ctsc

 

Other interactions of Ctsc

  • Furthermore, the activity of DPPI-dependent chymase was preserved in tissues of cathepsin L/S double-null mice [9].
  • Remarkably, deleting IL-6 expression in DPPI(-/-) mice eliminates the survival advantage [2].
  • CTL express high levels of dipeptidyl peptidase I (DPPI), a granule thiol protease able to convert the zymogen precursors of granzymes A and B into active proteases [14].
  • Cytotoxic assays with DPPI-/- effector cells reveal severe defects in the induction of target cell apoptosis (as measured by [(125)I]UdR release) at both early and late time points; this defect is comparable to that detected in perforin-/- or granzyme A-/- x B-/- cytotoxic lymphocytes [7].
  • Furthermore, SDF-1/CXCL12 induced chemotaxis of ESCs, and chemotaxis could be enhanced by diprotin A inhibition of CD26/dipeptidylpeptidase IV [15].
 

Analytical, diagnostic and therapeutic context of Ctsc

References

  1. 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]
  2. Mast cell dipeptidyl peptidase I mediates survival from sepsis. Mallen-St Clair, J., Pham, C.T., Villalta, S.A., Caughey, G.H., Wolters, P.J. J. Clin. Invest. (2004) [Pubmed]
  3. Identification of an alternative splicing variant of cathepsin C/dipeptidyl-peptidase I. Matsui, K., Yuyama, N., Akaiwa, M., Yoshida, N.L., Maeda, M., Sugita, Y., Izuhara, K. Gene (2002) [Pubmed]
  4. Acid proteolytic activities in mouse liver and muscle tissues after treatment with protease inhibitor leupeptin. Salminen, A., Kihlström, M., Vihko, V. Comp. Biochem. Physiol. C, Comp. Pharmacol. Toxicol. (1984) [Pubmed]
  5. 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]
  6. Cathepsin C from Schistosoma japonicum--cDNA encoding the preproenzyme and its phylogenetic relationships. Hola-Jamriska, L., Tort, J.F., Dalton, J.P., Day, S.R., Fan, J., Aaskov, J., Brindley, P.J. Eur. J. Biochem. (1998) [Pubmed]
  7. Dipeptidyl peptidase I is required for the processing and activation of granzymes A and B in vivo. Pham, C.T., Ley, T.J. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  8. Molecular cloning, chromosomal localization, and expression of murine dipeptidyl peptidase I. Pham, C.T., Armstrong, R.J., Zimonjic, D.B., Popescu, N.C., Payan, D.G., Ley, T.J. J. Biol. Chem. (1997) [Pubmed]
  9. Cathepsins L and S are not required for activation of dipeptidyl peptidase I (cathepsin C) in mice. Mallen-St Clair, J., Shi, G.P., Sutherland, R.E., Chapman, H.A., Caughey, G.H., Wolters, P.J. Biol. Chem. (2006) [Pubmed]
  10. Dipeptidyl peptidase I regulates the development of collagen-induced arthritis. Hu, Y., Pham, C.T. Arthritis Rheum. (2005) [Pubmed]
  11. Dipeptidyl peptidase I is essential for activation of mast cell chymases, but not tryptases, in mice. Wolters, P.J., Pham, C.T., Muilenburg, D.J., Ley, T.J., Caughey, G.H. J. Biol. Chem. (2001) [Pubmed]
  12. Critical role of dipeptidyl peptidase I in neutrophil recruitment during the development of experimental abdominal aortic aneurysms. Pagano, M.B., Bartoli, M.A., Ennis, T.L., Mao, D., Simmons, P.M., Thompson, R.W., Pham, C.T. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
  13. Residual active granzyme B in cathepsin C-null lymphocytes is sufficient for perforin-dependent target cell apoptosis. Sutton, V.R., Waterhouse, N.J., Browne, K.A., Sedelies, K., Ciccone, A., Anthony, D., Koskinen, A., Mullbacher, A., Trapani, J.A. J. Cell Biol. (2007) [Pubmed]
  14. A selective inhibitor of dipeptidyl peptidase I impairs generation of CD8+ T cell cytotoxic effector function. Thiele, D.L., McGuire, M.J., Lipsky, P.E. J. Immunol. (1997) [Pubmed]
  15. SDF-1/CXCL12 enhances survival and chemotaxis of murine embryonic stem cells and production of primitive and definitive hematopoietic progenitor cells. Guo, Y., Hangoc, G., Bian, H., Pelus, L.M., Broxmeyer, H.E. Stem Cells (2005) [Pubmed]
 
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