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Gene Review

Ctrl  -  chymotrypsin-like

Mus musculus

Synonyms: 0910001G08Rik, 1810004D15Rik, AV005227, Ctra-1, Ctra1, ...
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Disease relevance of Ctrl


High impact information on Ctrl

  • Three distinct peptidase activities of this enzyme complex (trypsin-like, chymotrypsin-like, and peptidylglutamyl-peptide hydrolyzing activities) were inhibited by lactacystin, the first two irreversibly and all at different rates [6].
  • IFN-gamma stimulation results in a downregulation of the chymotrypsin-like Suc-LLVY-MCA peptide hydrolyzing activity of 20S proteasomes whereas the trypsin-like activity remains unaffected [7].
  • When tested as a substrate a synthetic 25-mer polypeptide whose sequence covers the antigenic nonapeptide YPHFMPTNL of the MCMV pp89, 20S proteasomes of IFN-gamma-induced cells exhibit altered chymotrypsin-like cleavage site preferences [7].
  • RESULTS: VSL#3 produces soluble factors that inhibit the chymotrypsin-like activity of the proteasome in gut epithelial cells [8].
  • Although halomethyl ketone derivatives of phenylalanine were originally designed and used for affinity labeling of the active site of chymotrypsin and similar enzymes, no evidence was found for a chymotrypsin-like activity of interferons [9].

Chemical compound and disease context of Ctrl


Biological context of Ctrl


Anatomical context of Ctrl

  • A 334+/-44% increase (P<0.001 versus Ctrl) in relative retention of (111)In-RP782 was confirmed by gamma well counting of myocardium [16].
  • Subsequent to target cell binding, but prior to programming for lysis by Ca2+, NK cell lytic activity could be suppressed by inhibitors of chymotrypsin-like, but not trypsin-like proteases, in contrast to CTL [17].
  • Subunit rLMP7 of the multicatalytic proteinase (MCP), which has been associated with chymotrypsin-like proteinase activity, was examined in rat liver and hepatocyte-derived cell lines. rLMP7 was detected in both nucleus and cytosol in liver by immunohistochemistry and immunoblotting, using a peptide-specific anti-rLMP7 antibody [18].
  • Both agents completely attenuated total protein degradation in murine myotubes at all concentrations of PIF, and attenuated the PIF-induced increase in expression of the ubiquitin-proteasome proteolytic pathway, as determined by the 'chymotrypsin-like' enzyme activity, proteasome subunits and E2(14k) [19].
  • In both myoblasts and myotubes protein degradation was accompanied by an increased expression of the alpha-type subunits of the 20S proteasome as well as functional activity of the proteasome, as determined by the 'chymotrypsin-like' enzyme activity [20].

Associations of Ctrl with chemical compounds


Regulatory relationships of Ctrl

  • These studies suggest that specific inhibition of the chymotrypsin-like activity of the proteasome is sufficient to prevent signal-induced NF-kappa B activation and that the proteasome is a novel target for the identification of agents that may be useful in the treatment of diseases whose etiology is dependent upon the activation of NF-kappa B [26].
  • Cloning and characterization of mouse klk27, a novel tissue kallikrein expressed in testicular Leydig cells and exhibiting chymotrypsin-like specificity [27].

Other interactions of Ctrl


Analytical, diagnostic and therapeutic context of Ctrl

  • Furthermore, WA potently inhibits the chymotrypsin-like activity of a purified rabbit 20S proteasome (IC50=4.5 microM) and 26S proteasome in human prostate cancer cultures (at 5-10 microM) and xenografts (4-8 mg/kg/day) [32].
  • While LMF had no effect on the lysosomal enzymes, cathepsins B and L, there was a decrease in proteasome activity, as determined both by the 'chymotrypsin-like' enzyme activity, as well as expression of proteasome alpha-type subunits, determined by Western blotting [33].
  • Trypsin-like and chymotrypsin-like esteroprotease isozymes of the mouse submandibular gland were separated by isoelectric focusing [10].
  • Basic isozymes of chymotrypsin-like esteroprotease from mouse submandibular glands were purified 60-80-fold by a rather simple procedure consisting of CM-Sepharose CL6B chromatography and gel filtration on Sephadex G-100 [34].


  1. Delayed expulsion of the nematode Trichinella spiralis in mice lacking the mucosal mast cell-specific granule chymase, mouse mast cell protease-1. Knight, P.A., Wright, S.H., Lawrence, C.E., Paterson, Y.Y., Miller, H.R. J. Exp. Med. (2000) [Pubmed]
  2. Mechanism of attenuation of skeletal muscle protein catabolism in cancer cachexia by eicosapentaenoic acid. Whitehouse, A.S., Smith, H.J., Drake, J.L., Tisdale, M.J. Cancer Res. (2001) [Pubmed]
  3. Myostatin gene deletion prevents glucocorticoid-induced muscle atrophy. Gilson, H., Schakman, O., Combaret, L., Lause, P., Grobet, L., Attaix, D., Ketelslegers, J.M., Thissen, J.P. Endocrinology (2007) [Pubmed]
  4. Determinants of mouse hepatitis virus 3C-like proteinase activity. Lu, Y., Denison, M.R. Virology (1997) [Pubmed]
  5. Alphavirus replication in cultured cells and infected animals is inhibited by antiproteinase agents. Zhirnov, O.P., Ovcharenko, A.V., Melnikova, E.E., Bukrinskaya, A.G., Gaidamovich SYa, n.u.l.l. Antiviral Res. (1986) [Pubmed]
  6. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Fenteany, G., Standaert, R.F., Lane, W.S., Choi, S., Corey, E.J., Schreiber, S.L. Science (1995) [Pubmed]
  7. Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes. Boes, B., Hengel, H., Ruppert, T., Multhaup, G., Koszinowski, U.H., Kloetzel, P.M. J. Exp. Med. (1994) [Pubmed]
  8. Probiotics inhibit nuclear factor-kappaB and induce heat shock proteins in colonic epithelial cells through proteasome inhibition. Petrof, E.O., Kojima, K., Ropeleski, M.J., Musch, M.W., Tao, Y., De Simone, C., Chang, E.B. Gastroenterology (2004) [Pubmed]
  9. Inactivation of interferons: halomethyl ketone derivatives of phenylalanine as affinity labels. McCray, J.W., Weil, R. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  10. Induction of various androgen-dependent esteroproteases (trypsin-like and chymotrypsin-like enzymes) by tri-iodo-L-thyronine in the submandibular glands of female mice and mice with testicular feminization. Hosoi, K., Kida, T., Ueha, T. J. Biochem. (1981) [Pubmed]
  11. Genetic and biochemical characterization of a new chymotrypsin isozyme of the house mouse, CTRA-1. von Deimling, O.H., Gröning, J., Gaa, A. Biochem. Genet. (1991) [Pubmed]
  12. Deletion of Smad2 in mouse liver reveals novel functions in hepatocyte growth and differentiation. Ju, W., Ogawa, A., Heyer, J., Nierhof, D., Yu, L., Kucherlapati, R., Shafritz, D.A., Böttinger, E.P. Mol. Cell. Biol. (2006) [Pubmed]
  13. Thrombin is inactivated by mast cell secretory granule chymase. Pejler, G., Karlström, A. J. Biol. Chem. (1993) [Pubmed]
  14. Pathways for degradation of the catalytic subunit of cAMP-dependent protein kinase differ in wild-type and kinase-negative S49 mouse lymphoma cells. Lee, S.L., Steinberg, R.A. J. Biol. Chem. (1996) [Pubmed]
  15. Complete genomic sequence and phylogenetic analysis of the lactate dehydrogenase-elevating virus (LDV). Godeny, E.K., Chen, L., Kumar, S.N., Methven, S.L., Koonin, E.V., Brinton, M.A. Virology (1993) [Pubmed]
  16. Noninvasive targeted imaging of matrix metalloproteinase activation in a murine model of postinfarction remodeling. Su, H., Spinale, F.G., Dobrucki, L.W., Song, J., Hua, J., Sweterlitsch, S., Dione, D.P., Cavaliere, P., Chow, C., Bourke, B.N., Hu, X.Y., Azure, M., Yalamanchili, P., Liu, R., Cheesman, E.H., Robinson, S., Edwards, D.S., Sinusas, A.J. Circulation (2005) [Pubmed]
  17. Studies on the mechanism of NK cell lysis. Quan, P.C., Ishizaka, T., Bloom, B.R. J. Immunol. (1982) [Pubmed]
  18. Studies on rLMP7, a beta-subunit of the multicatalytic proteinase. Ren, L., Clawson, G.A. Exp. Cell Res. (1997) [Pubmed]
  19. Induction of proteasome expression in skeletal muscle is attenuated by inhibitors of NF-kappaB activation. Wyke, S.M., Russell, S.T., Tisdale, M.J. Br. J. Cancer (2004) [Pubmed]
  20. Development of an in-vitro model system to investigate the mechanism of muscle protein catabolism induced by proteolysis-inducing factor. Gomes-Marcondes, M.C., Smith, H.J., Cooper, J.C., Tisdale, M.J. Br. J. Cancer (2002) [Pubmed]
  21. Combination efficacy of doxorubicin and adenoviral methioninase gene therapy with prodrug selenomethionine. Gupta, A., Miki, K., Xu, M., Yamamoto, N., Moossa, A.R., Hoffman, R.M. Anticancer Res. (2003) [Pubmed]
  22. Peroxynitrite alters the catalytic activity of rodent liver proteasome in vitro and in vivo. Osna, N.A., Haorah, J., Krutik, V.M., Donohue, T.M. Hepatology (2004) [Pubmed]
  23. Serine proteases in rodent hippocampus. Davies, B.J., Pickard, B.S., Steel, M., Morris, R.G., Lathe, R. J. Biol. Chem. (1998) [Pubmed]
  24. Cytoplasmic trafficking of minute virus of mice: low-pH requirement, routing to late endosomes, and proteasome interaction. Ros, C., Burckhardt, C.J., Kempf, C. J. Virol. (2002) [Pubmed]
  25. Proteinases are involved in both DNA fragmentation and membrane damage during CTL-mediated target cell killing. Helgason, C.D., Atkinson, E.A., Pinkoski, M.J., Bleackley, R.C. Exp. Cell Res. (1995) [Pubmed]
  26. A new structural class of proteasome inhibitors that prevent NF-kappa B activation. Lum, R.T., Kerwar, S.S., Meyer, S.M., Nelson, M.G., Schow, S.R., Shiffman, D., Wick, M.M., Joly, A. Biochem. Pharmacol. (1998) [Pubmed]
  27. Cloning and characterization of mouse klk27, a novel tissue kallikrein expressed in testicular Leydig cells and exhibiting chymotrypsin-like specificity. Matsui, H., Moriyama, A., Takahashi, T. Eur. J. Biochem. (2000) [Pubmed]
  28. The proteasome as a lipopolysaccharide-binding protein in macrophages: differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events. Qureshi, N., Perera, P.Y., Shen, J., Zhang, G., Lenschat, A., Splitter, G., Morrison, D.C., Vogel, S.N. J. Immunol. (2003) [Pubmed]
  29. Myonase is localized in skeletal muscle myofibrils. Hori, S., Yamada, M., Ohtani, S., Hori, C., Yokomizo, T., Webb, T., Shimokawa, T. J. Biochem. (2002) [Pubmed]
  30. Increased expression of the ubiquitin-proteasome pathway in murine myotubes by proteolysis-inducing factor (PIF) is associated with activation of the transcription factor NF-kappaB. Whitehouse, A.S., Tisdale, M.J. Br. J. Cancer (2003) [Pubmed]
  31. Expression and utilization of chymotrypsin-like but not trypsin-like serine protease enzymes by nonspecific T killer cells activated by anti-CD3 monoclonal antibody. Kaiser, M., Hoskin, D.W. Cell. Immunol. (1992) [Pubmed]
  32. The tumor proteasome is a primary target for the natural anticancer compound Withaferin A isolated from "Indian winter cherry". Yang, H., Shi, G., Dou, Q.P. Mol. Pharmacol. (2007) [Pubmed]
  33. Effect of a tumour-produced lipid-mobilizing factor on protein synthesis and degradation. Islam-Ali, B.S., Tisdale, M.J. Br. J. Cancer (2001) [Pubmed]
  34. Basic isozymes of chymotrypsin-like esteroprotease from the mouse submandibular gland. Takuma, T., Ichida, T., Kumegawa, M. Biochim. Biophys. Acta (1983) [Pubmed]
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