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Gene Review

CTSZ  -  cathepsin Z

Homo sapiens

Synonyms: CTSX, Cathepsin P, Cathepsin X, Cathepsin Z
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Disease relevance of CTSZ


High impact information on CTSZ

  • Here we show that a cathepsin-Z-related glycoprotein binds to the recycling, mannose-specific membrane lectin ERGIC-53 [4].
  • Mutation of the lectin domain of ERGIC-53 selectively decreased YFP complementation with cathepsin Z [5].
  • The integrin-binding motifs RGD and ECD, present in the pro- and in mature forms of cathepsin X, respectively, suggest that this enzyme might have a function in cell signaling and adhesion [6].
  • Our results indicate that active cathepsin X mediates the function of beta(2) integrin receptors during cell adhesion and that it could also be involved in other processes associated with beta(2) integrin receptors such as phagocytosis and T cell activation [6].
  • Using confocal microscopy, we demonstrated that the pro-form of cathepsin X was co-localized with beta(2) and beta(3) integrin subunits and its mature form solely with the beta(2) integrin subunit with the most intense signal in cell-cell junctions in differentiated U-937 cells and in co-cultures with endothelial cells [6].

Chemical compound and disease context of CTSZ


Biological context of CTSZ


Anatomical context of CTSZ

  • A polymorphism was again identified within the CTSZ 3' untranslated region and used to demonstrate biallelic expression in fetal tissues [8].
  • Acidification of cells inhibited the association of ERGIC-53 with the known cargo cathepsin Z-related protein and dissociation of this glycoprotein in the ERGIC was impaired by organelle neutralization that did not impair the transport of a control protein [12].
  • Recently, we identified increased cathepsin X expression in H. pylori-infected gastric mucosa [2].
  • Cathepsin X was predominantly expressed by macrophages in the mucosal stroma and in glands of the antral mucosa [2].
  • In vitro cell culture experiments revealed that intercellular signalling between pathogenicity island (PAI)-positive H. pylori-infected epithelial cells and macrophages via soluble factors in the culture medium seems to be responsible for increased expression of cathepsin X in monocytes [2].

Associations of CTSZ with chemical compounds

  • Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions [9].
  • Cathepsin X also cleaved substrates with amide-blocked C-terminal carboxyl group with rates similar to those of the unblocked substrates [13].

Physical interactions of CTSZ


Other interactions of CTSZ

  • Cathepsin X was similar to cathepsin B and found to be a carboxypeptidase with preference for a positively charged Arg in P1 position [13].

Analytical, diagnostic and therapeutic context of CTSZ


  1. Tissue expression and immunolocalization of a novel human cathepsin P. Pungercar, J., Viyjak, A., Ivanovski, G., Krizaj, I. Pflugers Arch. (2000) [Pubmed]
  2. Up-regulation of cathepsin X in Helicobacter pylori gastritis and gastric cancer. Krueger, S., Kalinski, T., Hundertmark, T., Wex, T., Küster, D., Peitz, U., Ebert, M., Nägler, D.K., Kellner, U., Malfertheiner, P., Naumann, M., Röcken, C., Roessner, A. J. Pathol. (2005) [Pubmed]
  3. Up-regulation of cathepsin X in prostate cancer and prostatic intraepithelial neoplasia. Nägler, D.K., Krüger, S., Kellner, A., Ziomek, E., Menard, R., Buhtz, P., Krams, M., Roessner, A., Kellner, U. Prostate (2004) [Pubmed]
  4. The lectin ERGIC-53 is a cargo transport receptor for glycoproteins. Appenzeller, C., Andersson, H., Kappeler, F., Hauri, H.P. Nat. Cell Biol. (1999) [Pubmed]
  5. Capturing protein interactions in the secretory pathway of living cells. Nyfeler, B., Michnick, S.W., Hauri, H.P. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  6. Carboxypeptidase cathepsin X mediates beta2-integrin-dependent adhesion of differentiated U-937 cells. Obermajer, N., Premzl, A., Zavasnik Bergant, T., Turk, B., Kos, J. Exp. Cell Res. (2006) [Pubmed]
  7. RNA interference targeting cathepsin L and Z-like cysteine proteases of Onchocerca volvulus confirmed their essential function during L3 molting. Lustigman, S., Zhang, J., Liu, J., Oksov, Y., Hashmi, S. Mol. Biochem. Parasitol. (2004) [Pubmed]
  8. Characterization of TH1 and CTSZ, two non-imprinted genes downstream of GNAS1 in chromosome 20q13. Bonthron, D.T., Hayward, B.E., Moran, V., Strain, L. Hum. Genet. (2000) [Pubmed]
  9. Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions. Nägler, D.K., Ménard, R. FEBS Lett. (1998) [Pubmed]
  10. Defining the substrate specificity of mouse cathepsin P. Puzer, L., Barros, N.M., Oliveira, V., Juliano, M.A., Lu, G., Hassanein, M., Juliano, L., Mason, R.W., Carmona, A.K. Arch. Biochem. Biophys. (2005) [Pubmed]
  11. Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease. Guncar, G., Klemencic, I., Turk, B., Turk, V., Karaoglanovic-Carmona, A., Juliano, L., Turk, D. Structure (2000) [Pubmed]
  12. pH-induced conversion of the transport lectin ERGIC-53 triggers glycoprotein release. Appenzeller-Herzog, C., Roche, A.C., Nufer, O., Hauri, H.P. J. Biol. Chem. (2004) [Pubmed]
  13. Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase. Klemencic, I., Carmona, A.K., Cezari, M.H., Juliano, M.A., Juliano, L., Guncar, G., Turk, D., Krizaj, I., Turk, V., Turk, B. Eur. J. Biochem. (2000) [Pubmed]
  14. Cargo Selectivity of the ERGIC-53/MCFD2 Transport Receptor Complex. Nyfeler, B., Zhang, B., Ginsburg, D., Kaufman, R.J., Hauri, H.P. Traffic (2006) [Pubmed]
  15. Identification and molecular cloning of cathepsin P, a novel human putative cysteine protease of the papain family. Pungercar, J., Ivanovski, G. Pflugers Arch. (2000) [Pubmed]
  16. Cathepsins X and B can be differentiated through their respective mono- and dipeptidyl carboxypeptidase activities. Therrien, C., Lachance, P., Sulea, T., Purisima, E.O., Qi, H., Ziomek, E., Alvarez-Hernandez, A., Roush, W.R., Ménard, R. Biochemistry (2001) [Pubmed]
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