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Gene Review

CTSB  -  cathepsin B

Gallus gallus

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Disease relevance of CTSB

  • The structure of the compound seemed to be responsible for the effects measured since compounds used to represent constituents of Zeolite A (silicon dioxide and aluminum chloride) failed to inhibit bone resorption or reduce the level of secreted cathepsin B enzyme activity [1].
  • Breast muscle (BM) weight, leg muscle (LM) weight, whole body weight, and BM and LM cathepsin B and L activities were obtained on 12 birds/treatment [2].

High impact information on CTSB

  • At higher concentrations (10-100 mM), the chymotrypsin substrates N alpha-p-tosyl-L-arginine methyl ester and tryptophan methyl ester and the cathepsin B inhibitor leupeptin also inhibit [3H] 1,25(OH)2D3 binding to its receptor [3].
  • Osteoclasts were transiently transfected and secretions of cathepsin B/K and tartrate-resistant acid phosphatase (TRAP) were monitored [4].
  • In basal-lateral membranes, enhanced CB activity was detectable 10 h after 1,25(OH)2D3 in vivo, rose to 155% of -D levels at 15 h, and to 245% of controls in fractions from +D birds, whereas acid phosphatase was 75%, 81%, and 125% of controls, respectively, at these times.(ABSTRACT TRUNCATED AT 250 WORDS)[5]
  • Peptidyl acyloxymethyl ketones, previously established as potent inactivators of the lysosomal cysteine proteinase cathepsin B, were evaluated against smooth-muscle calpain, a member of the family of Ca(2+)-dependent cysteine proteinases [6].
  • Ki values for the inhibition of cysteine proteinases were as follows: papain (less than 1 X 10(-11)M), cathepsin B (8 X 10(-10)M), cathepsin H (about 2 X 10(-8)M) and cathepsin L (about 3 X 10(-12)M) [7].

Biological context of CTSB


Anatomical context of CTSB

  • In osteoclasts and cultured macrophages, which produce large quantities of cathepsin B, mRNAs of 1.8 and 2.4 kb are produced in approximately equal quantities, while cells producing smaller quantities of the enzyme produce predominantly the 2.4 kb form [8].
  • After 30 min of calcium transport, endocytic vesicles prepared from either vitamin D-deficient or 1,25(OH)2D3-treated birds had recovered cathepsin B activity to pretransport levels [10].
  • In sections prepared after 3 min of calcium absorption, cathepsin B staining was localized near the basal and lateral membranes of the epithelial cells [10].
  • In the absence of calcium transport, cathepsin B-specific activity was enhanced in whole homogenates, endocytic vesicles, and a lysosomal fraction prepared from intestinal epithelium of 1,25(OH)2D3-treated chicks, relative to vitamin D-deficient controls [10].
  • Hybridization of RNA extracted from the L6 myogenic cell line with cathepsin B cDNA showed an increase in the level of cathepsin B mRNA [11].

Associations of CTSB with chemical compounds


Other interactions of CTSB


Analytical, diagnostic and therapeutic context of CTSB


  1. Zeolite A inhibits osteoclast-mediated bone resorption in vitro. Schütze, N., Oursler, M.J., Nolan, J., Riggs, B.L., Spelsberg, T.C. J. Cell. Biochem. (1995) [Pubmed]
  2. The effect of cimaterol and its withdrawal on carcass composition and meat tenderness of broiler chickens. Gwartney, B.L., Calkins, C.R., Jones, S.J. J. Anim. Sci. (1991) [Pubmed]
  3. Differential effects of protease inhibitors on 1,25-dihydroxyvitamin D3 receptors. Norman, A.W., Hunziker, W., Walters, M.R., Bishop, J.E. J. Biol. Chem. (1983) [Pubmed]
  4. The Src signaling pathway regulates osteoclast lysosomal enzyme secretion and is rapidly modulated by estrogen. Pascoe, D., Oursler, M.J. J. Bone Miner. Res. (2001) [Pubmed]
  5. Rapid action of 1,25-dihydroxyvitamin D3 on calcium transport in perfused chick duodenum: effect of inhibitors. Nemere, I., Norman, A.W. J. Bone Miner. Res. (1987) [Pubmed]
  6. Comparative behaviour of calpain and cathepsin B toward peptidyl acyloxymethyl ketones, sulphonium methyl ketones and other potential inhibitors of cysteine proteinases. Pliura, D.H., Bonaventura, B.J., Smith, R.A., Coles, P.J., Krantz, A. Biochem. J. (1992) [Pubmed]
  7. Cystatin, a protein inhibitor of cysteine proteinases. Improved purification from egg white, characterization, and detection in chicken serum. Anastasi, A., Brown, M.A., Kembhavi, A.A., Nicklin, M.J., Sayers, C.A., Sunter, D.C., Barrett, A.J. Biochem. J. (1983) [Pubmed]
  8. Avian cathepsin B cDNA: sequence and demonstration that mRNAs of two sizes are produced in cell types producing large quantities of the enzyme. Dong, S.S., Stransky, G.I., Whitaker, C.H., Jordan, S.E., Schlesinger, P.H., Edwards, J.C., Blair, H.C. Biochim. Biophys. Acta (1995) [Pubmed]
  9. Purification and properties of embryonic cysteine proteinase which participates in yolk-lysis of Xenopus laevis. Yoshizaki, N., Moriyama, A., Yonezawa, S. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (1998) [Pubmed]
  10. Redistribution of cathepsin B activity from the endosomal-lysosomal pathway in chick intestine within 3 min of calcium absorption. Nemere, I., Norman, A.W. Mol. Cell. Endocrinol. (1991) [Pubmed]
  11. mRNA levels of cathepsins B and D during myogenesis. Colella, R., Roisen, F.J., Bird, J.W. Biomed. Biochim. Acta (1986) [Pubmed]
  12. A comparison of four cathepsins (B, L, N and S) with collagenolytic activity from rabbit spleen. Maciewicz, R.A., Etherington, D.J. Biochem. J. (1988) [Pubmed]
  13. Proteolysis of liver acetyl coenzyme A carboxylase by cathepsin B. Wada, K., Tanabe, T. FEBS Lett. (1985) [Pubmed]
  14. Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization. Ishiura, S., Murofushi, H., Suzuki, K., Imahori, K. J. Biochem. (1978) [Pubmed]
  15. Effects of thyroid hormones on myofibrillar proteolysis and activities of calpain, proteasome, and cathepsin in primary cultured chick muscle cells. Nakashima, K., Ohtsuka, A., Hayashi, K. J. Nutr. Sci. Vitaminol. (1998) [Pubmed]
  16. Effects of serum deprivation on expression of proteolytic-related genes in chick myotube cultures. Nakashima, K., Yamazaki, M., Abe, H. Biosci. Biotechnol. Biochem. (2005) [Pubmed]
  17. Recombinant Q53E- and Q53N--chicken egg white cystatin variants inhibit papain, actinidin and cathepsin B. Genenger, G., Lenzen, S., Mentele, R., Assfalg-Machleidt, I., Auerswald, E.A. Biomed. Biochim. Acta (1991) [Pubmed]
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