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Gene Review

CTSB  -  cathepsin B

Bos taurus

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Disease relevance of CTSB


Psychiatry related information on CTSB


High impact information on CTSB

  • Cleavage is enhanced by the addition of exogenous bovine cathepsin B and inhibited in the presence of specific cysteine protease inhibitors, but not inhibitors of other proteases [5].
  • The cDNA sequence encoding the precursor of cathepsin B of Schistosoma mansoni was cloned in a modified RNA expression vector pSP65 and the derived RNA expressed in rabbit reticulocyte lysates [5].
  • CONCLUSION: Elevated coefficients of friction in arthritic joints occur concurrently with enhanced proteolytic degradation by up-regulated cathepsin B and other proteases, as well as decreased lubricin synthesis by synovial fibroblasts and superficial zone chondrocytes [6].
  • Cathepsin B regulates the intrinsic angiogenic threshold of endothelial cells [1].
  • Aclacinomycin A had no effect on cathepsin B, stimulated trypsin, and inhibited chymotrypsin and, to a lesser extent, calpain [7].

Biological context of CTSB


Anatomical context of CTSB


Associations of CTSB with chemical compounds

  • An outstanding feature of bovine spleen cathepsin B not observed with the other cathepsins B is the presence of two additional half-cystine residues [9].
  • Identification of the active site cysteine and of the disulfide bonds in the N-terminal part of the molecule of bovine spleen cathepsin B [15].
  • However, at pH 7.0, the stability of cathepsin B decreased with increasing reduction potential and ambient cystine concentration [16].
  • The intra- and interchain thiol-disulfide exchange reactions accompanying the denaturation of cathepsin B were investigated by polyacrylamide gel electrophoresis in SDS and by gel filtration experiments [17].
  • The ability of cystamine, bis-N-aminoethyl disulfide, to inactivate cathepsin B by disulfide exchange is considerably enhanced by the addition of hydrophobic residues which apparently occupy secondary binding sites in the extended active center of the protease [18].

Other interactions of CTSB


Analytical, diagnostic and therapeutic context of CTSB


  1. Cathepsin B regulates the intrinsic angiogenic threshold of endothelial cells. Im, E., Venkatakrishnan, A., Kazlauskas, A. Mol. Biol. Cell (2005) [Pubmed]
  2. Isolation and characterization of cathepsin B from bovine brain. Bradley, J.D., Whitaker, J.N. Neurochem. Res. (1986) [Pubmed]
  3. Suppression of myocardial protein degradation by the protease inhibitor bis[ethyl(2R,3R)-3-[(S)-methyl-1-[4-(2,3,4-tri-methoxy-phenyl-methyl) piperazine-1-ylcarbonyl]butyl-carbonyl]oxiran-2-carboxylat e]sulfate under hypoxia. Toyo-oka, T., Kamishiro, T., Hara, K., Nakamura, N., Kitahara, M., Masaki, T. Arzneimittel-Forschung. (1986) [Pubmed]
  4. Inhibition of cathepsin B reduces beta-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: evidence for cathepsin B as a candidate beta-secretase of Alzheimer's disease. Hook, V., Toneff, T., Bogyo, M., Greenbaum, D., Medzihradszky, K.F., Neveu, J., Lane, W., Hook, G., Reisine, T. Biol. Chem. (2005) [Pubmed]
  5. In vitro translation and processing of cathepsin B of Schistosoma mansoni. Felleisen, R., Klinkert, M.Q. EMBO J. (1990) [Pubmed]
  6. Reduced expression and proteolytic susceptibility of lubricin/superficial zone protein may explain early elevation in the coefficient of friction in the joints of rats with antigen-induced arthritis. Elsaid, K.A., Jay, G.D., Chichester, C.O. Arthritis Rheum. (2007) [Pubmed]
  7. The antitumor drug aclacinomycin A, which inhibits the degradation of ubiquitinated proteins, shows selectivity for the chymotrypsin-like activity of the bovine pituitary 20 S proteasome. Figueiredo-Pereira, M.E., Chen, W.E., Li, J., Johdo, O. J. Biol. Chem. (1996) [Pubmed]
  8. Expression of lysosomal cathepsin B during calf myoblast-myotube differentiation. Characterization of a cDNA encoding bovine cathepsin B. Béchet, D.M., Ferrara, M.J., Mordier, S.B., Roux, M.P., Deval, C.D., Obled, A. J. Biol. Chem. (1991) [Pubmed]
  9. Amino acid sequence of bovine spleen cathepsin B. Meloun, B., Baudys, M., Pohl, J., Pavlík, M., Kostka, V. J. Biol. Chem. (1988) [Pubmed]
  10. Substrate specificity of bovine cathepsin B and its inhibition by CA074, based on crystal structure refinement of the complex. Yamamoto, A., Tomoo, K., Hara, T., Murata, M., Kitamura, K., Ishida, T. J. Biochem. (2000) [Pubmed]
  11. Nucleotide sequence of bovine preprocathepsin B. A study of polymorphism in the protein coding region. Mordier, S., Béchet, D., Roux, M.P., Obled, A., Ferrara, M. Biochim. Biophys. Acta (1993) [Pubmed]
  12. The degradation of proparathormone and parathormone by parathyroid and liver cathepsin B. MacGregor, R.R., Hamilton, J.W., Kent, G.N., Shofstall, R.E., Cohn, D.V. J. Biol. Chem. (1979) [Pubmed]
  13. In vivo inhibition of cathepsin B by peptidyl (acyloxy)methyl ketones. Wagner, B.M., Smith, R.A., Coles, P.J., Copp, L.J., Ernest, M.J., Krantz, A. J. Med. Chem. (1994) [Pubmed]
  14. Partial purification of cathepsin B in the bovine ciliary body and iris. Hayasaka, S., Shiono, T., Hara, S., Fukuyo, T. Invest. Ophthalmol. Vis. Sci. (1983) [Pubmed]
  15. Identification of the active site cysteine and of the disulfide bonds in the N-terminal part of the molecule of bovine spleen cathepsin B. Pohl, J., Baudys, M., Tomásek, V., Kostka, V. FEBS Lett. (1982) [Pubmed]
  16. Cathepsin B stability, but not activity, is affected in cysteine:cystine redox buffers. Pillay, C.S., Dennison, C. Biol. Chem. (2002) [Pubmed]
  17. Identification of the second (buried) cysteine residue and of the C-terminal disulfide bridge of bovine spleen cathepsin B. Baudys, M., Meloun, B., Pohl, J., Kostka, V. Biol. Chem. Hoppe-Seyler (1988) [Pubmed]
  18. Inactivation of cathepsin B by active site-directed disulfide exchange. Application in covalent affinity chromatography. Evans, B., Shaw, E. J. Biol. Chem. (1983) [Pubmed]
  19. Quantitative expression of candidate genes for developmental competence in bovine two-cell embryos. Dode, M.A., Dufort, I., Massicotte, L., Sirard, M.A. Mol. Reprod. Dev. (2006) [Pubmed]
  20. Azapeptides as inhibitors and active site titrants for cysteine proteinases. Xing, R., Hanzlik, R.P. J. Med. Chem. (1998) [Pubmed]
  21. Antigen processing by endosomal proteases determines which sites of sperm-whale myoglobin are eventually recognized by T cells. Van Noort, J.M., Boon, J., Van der Drift, A.C., Wagenaar, J.P., Boots, A.M., Boog, C.J. Eur. J. Immunol. (1991) [Pubmed]
  22. T cell-stimulatory fragments of foot-and-mouth disease virus released by mild treatment with cathepsin D. van Lierop, M.J., van Noort, J.M., Wagenaar, J.P., Rutten, V.P., Langeveld, J., Meloen, R.H., Hensen, E.J. J. Gen. Virol. (1994) [Pubmed]
  23. Crystallization and preliminary X-ray study of the cathepsin B complexed with CA074, a selective inhibitor. Yamamoto, A., Kaji, T., Tomoo, K., Ishida, T., Inoue, M., Murata, M., Kitamura, K. J. Mol. Biol. (1992) [Pubmed]
  24. Hydroxynonenal inactivates cathepsin B by forming Michael adducts with active site residues. Crabb, J.W., O'Neil, J., Miyagi, M., West, K., Hoff, H.F. Protein Sci. (2002) [Pubmed]
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