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Gene Review

Ctsb  -  cathepsin B

Mus musculus

Synonyms: CB, Cathepsin B, Cathepsin B1
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Disease relevance of Ctsb


Psychiatry related information on Ctsb


High impact information on Ctsb

  • The activity of the lysosomal proteinase cathepsin B is significantly elevated in a variant of the B16 melanoma with high metastatic potential [6].
  • The cathepsin B activity is localized to the lysosomes of the tumor cells [6].
  • Since homogenates of leupeptin-treated muscles had decreased cathepsin B activity, this lysosomal protease may play a role in protein turnover in normal and diseased muscles [7].
  • Mutants of cathepsins B or S impaired tumor formation and angiogenesis, while cathepsin B or L knockouts retarded cell proliferation and tumor growth [8].
  • The cysteine protease cathepsin B (CatB) is associated with amyloid plaques in AD brains and has been suspected to increase Abeta production [5].

Chemical compound and disease context of Ctsb


Biological context of Ctsb


Anatomical context of Ctsb

  • Our aim was to ascertain if Ctsb inactivation attenuates liver injury, inflammation, and fibrogenesis after bile duct ligation (BDL) [1].
  • Both genetic and pharmacologic inhibition of Ctsb in the BDL mouse reduced (a). hepatic inflammation, as assessed by transcripts for CXC chemokines and neutrophil infiltration, and (b). fibrogenesis, as assessed by transcripts for stellate cell activation and sirius red staining for hepatic collagen deposition [1].
  • In contrast, hepatocyte apoptosis and liver damage were reduced in Ctsb(-/-) and cathepsin B inhibitor-treated mice fed the MCD diet following CI/WR injury [17].
  • Impaired proteolysis resulted in the persistence of thyroglobulin in the thyroids of mice with deficiencies in cathepsin B or L [18].
  • Native-gel electrophoresis and gel filtration chromatography demonstrate that, in both cell lines, the double-chain form of cathepsin B is sequestered in a large molecular weight complex that renders this form of the enzyme inactive [2].

Associations of Ctsb with chemical compounds

  • Cathepsin B is the major cysteine protease in the RPE and choroid [14].
  • Moreover, CA-074, a specific cathepsin B inhibitor, also abolished the neurotoxic effects caused by Abeta42-activated BV2 cells [19].
  • Recent studies suggested that N-acetylcysteine enhances the extracellular degradation of PDGF-beta receptor by cathepsin B, thus suggesting that the absence of PDGF-beta receptors in quiescent cells is due to an active process of elimination and not to a lack of expression [20].
  • It is shown that MGX (methylglyoxal), GO (glyoxal) and glycolaldehyde, but not hydroxyacetone and glucose, inhibit catB (cathepsin B), catL (cathepsin L) and catS (cathepsin S) activity in macrophage cell lysates, in a concentration-dependent manner [21].
  • Although inhibitors of cathepsin B (leupeptin, antipain, N alpha-p-tosyl-L-lysine chloromethyl ketone, and chymostatin) were able to inhibit the release of monoiodotyrosine from treated cells in a time- and concentration-dependent manner, they had little effect on the processing step that apparently inactivates 125I-EGF [22].
  • Cathepsin B and MMP-2 activities were decreased in Pseudomonas-infected NE knockout mice compared with wild-type littermates [23].

Physical interactions of Ctsb

  • Cathepsin B expression is under transcriptional control in murine melanomas and the major promoter contains potential binding sites for the Sp1 transcription factor [24].

Enzymatic interactions of Ctsb


Regulatory relationships of Ctsb


Other interactions of Ctsb


Analytical, diagnostic and therapeutic context of Ctsb


  1. Cathepsin B inactivation attenuates hepatic injury and fibrosis during cholestasis. Canbay, A., Guicciardi, M.E., Higuchi, H., Feldstein, A., Bronk, S.F., Rydzewski, R., Taniai, M., Gores, G.J. J. Clin. Invest. (2003) [Pubmed]
  2. Cathepsin B Is Inhibited in Mutant Cells Selected during Persistent Reovirus Infection. Ebert, D.H., Kopecky-Bromberg, S.A., Dermody, T.S. J. Biol. Chem. (2004) [Pubmed]
  3. TNF-alpha-mediated lysosomal permeabilization is FAN and caspase 8/Bid dependent. Werneburg, N., Guicciardi, M.E., Yin, X.M., Gores, G.J. Am. J. Physiol. Gastrointest. Liver Physiol. (2004) [Pubmed]
  4. Role of cathepsin B in intracellular trypsinogen activation and the onset of acute pancreatitis. Halangk, W., Lerch, M.M., Brandt-Nedelev, B., Roth, W., Ruthenbuerger, M., Reinheckel, T., Domschke, W., Lippert, H., Peters, C., Deussing, J. J. Clin. Invest. (2000) [Pubmed]
  5. Antiamyloidogenic and neuroprotective functions of cathepsin B: implications for Alzheimer's disease. Mueller-Steiner, S., Zhou, Y., Arai, H., Roberson, E.D., Sun, B., Chen, J., Wang, X., Yu, G., Esposito, L., Mucke, L., Gan, L. Neuron (2006) [Pubmed]
  6. Lysosomal cathepsin B: correlation with metastatic potential. Sloane, B.F., Dunn, J.R., Honn, K.V. Science (1981) [Pubmed]
  7. Leupeptin, a protease inhibitor, decreases protein degradation in normal and diseased muscles. Libby, P., Goldberg, A.L. Science (1978) [Pubmed]
  8. Distinct roles for cysteine cathepsin genes in multistage tumorigenesis. Gocheva, V., Zeng, W., Ke, D., Klimstra, D., Reinheckel, T., Peters, C., Hanahan, D., Joyce, J.A. Genes Dev. (2006) [Pubmed]
  9. Tumor cell-derived and macrophage-derived cathepsin B promotes progression and lung metastasis of mammary cancer. Vasiljeva, O., Papazoglou, A., Krüger, A., Brodoefel, H., Korovin, M., Deussing, J., Augustin, N., Nielsen, B.S., Almholt, K., Bogyo, M., Peters, C., Reinheckel, T. Cancer Res. (2006) [Pubmed]
  10. Cystatin C in LS lymphosarcoma and HA-1 hepatoma treated with Ukrain and cyclophosphamide and involvement of apoptosis. Korolenko, T.A., Poteryaeva, O.N., Djanayeva, S.J., Svechnikova, I.G., Kaledin, V.I., Timofeyeva, O.A., Filipenko, M.L., Nowicky, J. Drugs under experimental and clinical research. (2000) [Pubmed]
  11. Differences in targeting and secretion of cathepsins B and L by BALB/3T3 fibroblasts and Moloney murine sarcoma virus-transformed BALB/3T3 fibroblasts. Achkar, C., Gong, Q.M., Frankfater, A., Bajkowski, A.S. J. Biol. Chem. (1990) [Pubmed]
  12. Pancreatic ascites as a powerful inducer of inflammatory cytokines. The role of known vs unknown factors. Denham, W., Yang, J., Fink, G., Zervos, E.E., Carter, G., Norman, J. Archives of surgery (Chicago, Ill. : 1960) (1997) [Pubmed]
  13. Antimetastatic activity of adriamycin in combinations with proteinase inhibitors in mice. Leto, G., Tumminello, F.M., Gebbia, N., Woynarowska, B., Bernacki, R.J. Anticancer Res. (1990) [Pubmed]
  14. Regulation of cysteine cathepsin expression by oxidative stress in the retinal pigment epithelium/choroid of the mouse. Alizadeh, P., Smit-McBride, Z., Oltjen, S.L., Hjelmeland, L.M. Exp. Eye Res. (2006) [Pubmed]
  15. Gene trapping in differentiating cell lines: regulation of the lysosomal protease cathepsin B in skeletal myoblast growth and fusion. Gogos, J.A., Thompson, R., Lowry, W., Sloane, B.F., Weintraub, H., Horwitz, M. J. Cell Biol. (1996) [Pubmed]
  16. The expression and function of cystatin C and cathepsin B and cathepsin L during mouse embryo implantation and placentation. Afonso, S., Romagnano, L., Babiarz, B. Development (1997) [Pubmed]
  17. Cathepsin B inactivation attenuates hepatocyte apoptosis and liver damage in steatotic livers after cold ischemia-warm reperfusion injury. Baskin-Bey, E.S., Canbay, A., Bronk, S.F., Werneburg, N., Guicciardi, M.E., Nyberg, S.L., Gores, G.J. Am. J. Physiol. Gastrointest. Liver Physiol. (2005) [Pubmed]
  18. Thyroid functions of mouse cathepsins B, K, and L. Friedrichs, B., Tepel, C., Reinheckel, T., Deussing, J., von Figura, K., Herzog, V., Peters, C., Saftig, P., Brix, K. J. Clin. Invest. (2003) [Pubmed]
  19. Identification of cathepsin B as a mediator of neuronal death induced by Abeta-activated microglial cells using a functional genomics approach. Gan, L., Ye, S., Chu, A., Anton, K., Yi, S., Vincent, V.A., von Schack, D., Chin, D., Murray, J., Lohr, S., Patthy, L., Gonzalez-Zulueta, M., Nikolich, K., Urfer, R. J. Biol. Chem. (2004) [Pubmed]
  20. PI3K is involved in PDGF-beta receptor upregulation post-PDGF-BB treatment in mouse HSC. Lechuga, C.G., Hern??ndez-Nazara, Z.H., Hern??ndez, E., Bustamante, M., Desierto, G., Cotty, A., Dharker, N., Choe, M., Rojkind, M. Am. J. Physiol. Gastrointest. Liver Physiol. (2006) [Pubmed]
  21. Evidence for inactivation of cysteine proteases by reactive carbonyls via glycation of active site thiols. Zeng, J., Dunlop, R.A., Rodgers, K.J., Davies, M.J. Biochem. J. (2006) [Pubmed]
  22. Intracellular processing of epidermal growth factor and its effect on ligand-receptor interactions. Wiley, H.S., VanNostrand, W., McKinley, D.N., Cunningham, D.D. J. Biol. Chem. (1985) [Pubmed]
  23. Neutrophil elastase up-regulates cathepsin B and matrix metalloprotease-2 expression. Geraghty, P., Rogan, M.P., Greene, C.M., Boxio, R.M., Poiriert, T., O'Mahony, M., Belaaouaj, A., O'Neill, S.J., Taggart, C.C., McElvaney, N.G. J. Immunol. (2007) [Pubmed]
  24. Sp1 regulates cathepsin B transcription and invasiveness in murine B16 melanoma cells. Szpaderska, A.M., Silberman, S., Ahmed, Y., Frankfater, A. Anticancer Res. (2004) [Pubmed]
  25. Murine myeloid leukemia: in vivo suppression by sericystatin A, a proteinase inhibitor from leukocytes. Pavelić, K., Sirotković, M., Kopitar, M., Pavelić, J., Vuk-Pavlović, S. European journal of cancer & clinical oncology. (1983) [Pubmed]
  26. The cathepsin B inhibitor z-FA.fmk inhibits cytokine production in macrophages stimulated by lipopolysaccharide. Schotte, P., Schauvliege, R., Janssens, S., Beyaert, R. J. Biol. Chem. (2001) [Pubmed]
  27. Cathepsin B-inhibitor promotes the development of Th1 type protective T cells in mice infected with Leishmania major. Maekawa, Y., Himeno, K., Katunuma, N. J. Med. Invest. (1997) [Pubmed]
  28. Co-operation between plasmin and elastase in elastin degradation by intact murine macrophages. Chapman, H.A., Stone, O.L. Biochem. J. (1984) [Pubmed]
  29. Cathepsin B knockout mice are resistant to tumor necrosis factor-alpha-mediated hepatocyte apoptosis and liver injury: implications for therapeutic applications. Guicciardi, M.E., Miyoshi, H., Bronk, S.F., Gores, G.J. Am. J. Pathol. (2001) [Pubmed]
  30. Cathepsin B-mediated activation of the proinflammatory caspase-11. Schotte, P., Van Criekinge, W., Van de Craen, M., Van Loo, G., Desmedt, M., Grooten, J., Cornelissen, M., De Ridder, L., Vandekerckhove, J., Fiers, W., Vandenabeele, P., Beyaert, R. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  31. Laminar shear stress inhibits cathepsin L activity in endothelial cells. Platt, M.O., Ankeny, R.F., Jo, H. Arterioscler. Thromb. Vasc. Biol. (2006) [Pubmed]
  32. Activation of proinflammatory caspases by cathepsin B in focal cerebral ischemia. Benchoua, A., Braudeau, J., Reis, A., Couriaud, C., Onténiente, B. J. Cereb. Blood Flow Metab. (2004) [Pubmed]
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