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Gene Review

Ctsc  -  cathepsin C

Rattus norvegicus

Synonyms: CATC, Cathepsin C, Cathepsin J, DPP-I, DPPI, ...
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Disease relevance of Ctsc


High impact information on Ctsc


Biological context of Ctsc

  • Our results show that at least one of the three glycosylation sites in the propeptide must be glycosylated in order to obtain targeting and maturation of cathepsin C [8].
  • The primary structure and tissue distribution of cathepsin C [9].
  • The reactivity of endoglycosidase H and N-glycanase and analysis of phosphorylation indicated that both precursor and mature cathepsin C are phosphorylated and N-glycosylated to give a high-mannose-type [10].
  • We present evidence that the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) is a site for protein splicing of cathepsin C: (i) maturation of the enzyme in COS 7 cells is a two-step process starting within the ERGIC, and (ii) the intermediately processed polypeptide retains both termini of the proenzyme and lacks an internal fragment [11].

Anatomical context of Ctsc


Associations of Ctsc with chemical compounds

  • Cathepsin C, therefore, is a member of the papain family, although its propeptide region is much longer than those of other cysteine proteinases and shows no significant amino acid sequence similarity to any other cysteine proteinase [5].
  • In order to assess some aspects of this contribution, we transiently expressed mutant molecules of rat cathepsin C either lacking three of the four glycosylation sites, partially deleted in the proregion, or mutated at tryptophan 39 also located in the proregion, and studied their biosynthesis [8].
  • Cathepsin C activity is reduced when thioethylamine hydrochloride is omitted from the incubation medium [14].
  • 1 mM-ZnSO4 considerably inhibits the cathepsin C total activity, measured with Gly-L-Phe-2-NNap as the substrate, in the presence of Triton X-100 [14].
  • Dipeptidyl peptidase I (DPPI, cathepsin C) is a lysosomal cysteine protease that can activate zymogens of several different serine proteases by one step or sequential removal of dipeptides from the N-termini of the pro-protease protein substrates [15].

Other interactions of Ctsc

  • It was separated from cathepsin J using a Sephacryl S-200 gel-filtration column and was further separated from cathepsin H by DEAE-Sephadex A-50 anion-exchange column chromatography [16].
  • The present immunohistochemical study further examined the localization of lysosomal aminopeptidases, cathepsin C, and tripeptidyl peptidase I (TPP-I) in the rat lung [12].
  • Subpopulations of CVs prepared by either procedure showed similar results, when examined for their relative proportion of cathepsin C and cathepsin D precursors [4].

Analytical, diagnostic and therapeutic context of Ctsc


  1. Mutation analysis of the cathepsin C gene in Indian families with Papillon-Lefèvre syndrome. Selvaraju, V., Markandaya, M., Prasad, P.V., Sathyan, P., Sethuraman, G., Srivastava, S.C., Thakker, N., Kumar, A. BMC Med. Genet. (2003) [Pubmed]
  2. Hydrolase activities in the rat aorta. II. Effects of hypertension alone and in combination with diabetes mellitus. Wolinsky, H., Capron, L., Goldfischer, S., Capron, F., Coltoff-Schiller, B., Kasak, L.E. Circ. Res. (1978) [Pubmed]
  3. Synthesis, transport and processing of cathepsin C in Morris hepatoma 7777 cells and rat hepatocytes. Mainferme, F., Wattiaux, R., von Figura, K. Eur. J. Biochem. (1985) [Pubmed]
  4. Lysosomal enzyme precursors in coated vesicles derived from the exocytic and endocytic pathways. Lemansky, P., Hasilik, A., von Figura, K., Helmy, S., Fishman, J., Fine, R.E., Kedersha, N.L., Rome, L.H. J. Cell Biol. (1987) [Pubmed]
  5. Molecular cloning of cDNA for rat cathepsin C. Cathepsin C, a cysteine proteinase with an extremely long propeptide. Ishidoh, K., Muno, D., Sato, N., Kominami, E. J. Biol. Chem. (1991) [Pubmed]
  6. Purification and characterization of autophagosomes from rat hepatocytes. Strømhaug, P.E., Berg, T.O., Fengsrud, M., Seglen, P.O. Biochem. J. (1998) [Pubmed]
  7. Use of glycyl-L-phenylalanine 2-naphthylamide, a lysosome-disrupting cathepsin C substrate, to distinguish between lysosomes and prelysosomal endocytic vacuoles. Berg, T.O., Strømhaug, E., Løvdal, T., Seglen, O., Berg, T. Biochem. J. (1994) [Pubmed]
  8. Importance of the propeptide in the biosynthetic maturation of rat cathepsin C. Santilman, V., Jadot, M., Mainferme, F. Eur. J. Cell Biol. (2002) [Pubmed]
  9. The primary structure and tissue distribution of cathepsin C. Kominami, E., Ishido, K., Muno, D., Sato, N. Biol. Chem. Hoppe-Seyler (1992) [Pubmed]
  10. Processing and transport of the precursor of cathepsin C during its transfer into lysosomes. Muno, D., Ishidoh, K., Ueno, T., Kominami, E. Arch. Biochem. Biophys. (1993) [Pubmed]
  11. Evidence for protein splicing in the endoplasmic reticulum-Golgi intermediate compartment. Demirov, D., Sarafian, V., Kremensky, I., Ganev, V. Biochim. Biophys. Acta (1999) [Pubmed]
  12. Specific localization of lysosomal aminopeptidases in type II alveolar epithelial cells of the rat lung. Yayoi, Y., Ohsawa, Y., Koike, M., Zhang, G., Kominami, E., Uchiyama, Y. Arch. Histol. Cytol. (2001) [Pubmed]
  13. Fluorescence demonstration of dipeptidyl peptidase I (cathepsin C) in skeletal, cardiac, and vascular smooth muscles. Stauber, W.T., Ong, S.H. J. Histochem. Cytochem. (1982) [Pubmed]
  14. Intralysosomal hydrolysis of glycyl-L-phenylalanine 2-naphthylamide. Jadot, M., Colmant, C., Wattiaux-De Coninck, S., Wattiaux, R. Biochem. J. (1984) [Pubmed]
  15. Design and evaluation of inhibitors for dipeptidyl peptidase I (Cathepsin C). Kam, C.M., Götz, M.G., Koot, G., McGuire, M., Thiele, D., Hudig, D., Powers, J.C. Arch. Biochem. Biophys. (2004) [Pubmed]
  16. Involvement of a cystatin-alpha-sensitive cysteine proteinase in the degradation of native L-lactate dehydrogenase and serum albumin by rat liver or kidney lysosomes. Ohshita, T., Kido, H. Eur. J. Biochem. (1994) [Pubmed]
  17. Endocytosis of superoxide dismutase by rat liver. Li, L., Wattiaux-De Coninck, S., Wattiaux, R. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
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