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Gene Review

Ctsl  -  cathepsin L

Mus musculus

Synonyms: 1190035F06Rik, Cat L, Cathepsin L, Cathepsin L1, Ctsl1, ...
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Disease relevance of Ctsl


High impact information on Ctsl


Chemical compound and disease context of Ctsl

  • In contrast, Moloney murine sarcoma virus-transformed BALB/3T3 fibroblasts (MMSV) secreted greatly increased amounts of latent cathepsin B (17-fold) and latent cathepsin L (27-fold), and moderately increased amounts of active beta-glucuronidase (2-fold) in a manner which was not further increased by monensin [8].
  • At the same time, a marked increase in cathepsin B and cathepsin L activity in LS lymphosarcoma was found, indicating the involvement of apoptosis in the mechanism of antitumor action of cyclophosphamide [9].
  • Development of metastases was not associated with changes in cathepsin B activity in the liver, while activity of cathepsin L decreased only during the early period (4 days) after injection of gadolinium chloride [10].
  • We found that only 5 min of incubation at 37 degrees C were required for nearly 100% of B. burgdorferi to enter a lysosomal glycoprotein-positive compartment, whereas 60 min were required for 90% of the spirochetes to appear in a cathepsin L-positive compartment under the same conditions [11].
  • CpG dinucleotides, not methylated in any melanoma cells analysed, were methylated in a B lymphoma cell line, which poorly express cathepsin L. Our data demonstrate that in lymphoma cells, cathepsin L silencing was methylation-dependent [12].

Biological context of Ctsl


Anatomical context of Ctsl


Associations of Ctsl with chemical compounds

  • A protein affinity strategy employing recombinant CTLA-2beta helped us to determine that cathepsin L, a cysteine protease, is one of its targets in the pregnant uterus [19].
  • In summary, these data establish that podocyte foot process effacement is a migratory event involving a novel interplay between cathepsin L and alpha(3) integrin [2].
  • Isolated podocytes from mice lacking cathepsin L are protected from cell puromycin aminonucleoside-induced cell detachment [2].
  • The selective suppression of cathepsin-L activity appeared not to be dependent on Ca(2+), since treatment of the cells with thapsigargin suppressed both cathepsin-B and -L activity [1].
  • A calcium antagonist, nifedipine, specifically suppressed cathepsin-L activity and mRNA expression, but not that of cathepsin-B in cultured gingival fibroblasts [1].

Regulatory relationships of Ctsl


Other interactions of Ctsl

  • We conclude that AEP is essential for processing of Cat L but not for class II MHC-restricted Ag presentation [15].
  • Synthesis and secretion of CAL were up-regulated by 1alpha,25-(OH)2D3, but neither those of CAK, dominant relative to CAL, nor CAB, barely detectable, levels changed in the experiments [22].
  • These results show that neither cathepsin L nor S is required for activation of DPPI and suggest that one or more additional proteases is responsible [23].
  • Active cathepsin L was highest at Day 9.5 in visceral yolk sac, a stage at which it has been shown that proteolysis in this organ is required for production of amino acids for embryonic protein synthesis [24].
  • RESULTS: Expression of mRNAs for receptors of the growth factors, the proteinases and their inhibitors were confirmed. bFGF increased the secretion of cathepsin L (5.04-fold at 20 ng/mL), but did not alter the secretion of its extracellular inhibitor, cystatin C [25].

Analytical, diagnostic and therapeutic context of Ctsl


  1. Cathepsin-L, a key molecule in the pathogenesis of drug-induced and I-cell disease-mediated gingival overgrowth: a study with cathepsin-L-deficient mice. Nishimura, F., Naruishi, H., Naruishi, K., Yamada, T., Sasaki, J., Peters, C., Uchiyama, Y., Murayama, Y. Am. J. Pathol. (2002) [Pubmed]
  2. Podocyte migration during nephrotic syndrome requires a coordinated interplay between cathepsin L and alpha3 integrin. Reiser, J., Oh, J., Shirato, I., Asanuma, K., Hug, A., Mundel, T.M., Honey, K., Ishidoh, K., Kominami, E., Kreidberg, J.A., Tomino, Y., Mundel, P. J. Biol. Chem. (2004) [Pubmed]
  3. Study of the functional share of lysosomal cathepsins by the development of specific inhibitors. Katunuma, N., Matsui, A., Kakegawa, T., Murata, E., Asao, T., Ohba, Y. Adv. Enzyme Regul. (1999) [Pubmed]
  4. Cathepsin L is required for endothelial progenitor cell-induced neovascularization. Urbich, C., Heeschen, C., Aicher, A., Sasaki, K., Bruhl, T., Farhadi, M.R., Vajkoczy, P., Hofmann, W.K., Peters, C., Pennacchio, L.A., Abolmaali, N.D., Chavakis, E., Reinheckel, T., Zeiher, A.M., Dimmeler, S. Nat. Med. (2005) [Pubmed]
  5. Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus. Nakagawa, T., Roth, W., Wong, P., Nelson, A., Farr, A., Deussing, J., Villadangos, J.A., Ploegh, H., Peters, C., Rudensky, A.Y. Science (1998) [Pubmed]
  6. Thymocyte expression of cathepsin L is essential for NKT cell development. Honey, K., Benlagha, K., Beers, C., Forbush, K., Teyton, L., Kleijmeer, M.J., Rudensky, A.Y., Bendelac, A. Nat. Immunol. (2002) [Pubmed]
  7. A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor. Goulet, B., Baruch, A., Moon, N.S., Poirier, M., Sansregret, L.L., Erickson, A., Bogyo, M., Nepveu, A. Mol. Cell (2004) [Pubmed]
  8. 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]
  9. 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]
  10. Effect of liver macrophage depression on the development of liver metastases of HA-1 tumor in mice. Zhanaeva, S.Y., Korolenko, T.A., Nikitenko, E.V., Alekseenko, T.V., Dergunova, M.A., Il'nitskaya, S.I., Kaledin, V.I., Plotnikova, G.I., Petrova, E.A. Bull. Exp. Biol. Med. (2004) [Pubmed]
  11. The fate of Borrelia burgdorferi, the agent for Lyme disease, in mouse macrophages. Destruction, survival, recovery. Montgomery, R.R., Nathanson, M.H., Malawista, S.E. J. Immunol. (1993) [Pubmed]
  12. Expression of cathepsin L in human tumor cells is under the control of distinct regulatory mechanisms. Jean, D., Rousselet, N., Frade, R. Oncogene (2006) [Pubmed]
  13. Progesterone-regulated genes in the ovulation process: ADAMTS-1 and cathepsin L proteases. Robker, R.L., Russell, D.L., Espey, L.L., Lydon, J.P., O'Malley, B.W., Richards, J.S. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  14. 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]
  15. Asparagine endopeptidase is not essential for class II MHC antigen presentation but is required for processing of cathepsin L in mice. Maehr, R., Hang, H.C., Mintern, J.D., Kim, Y.M., Cuvillier, A., Nishimura, M., Yamada, K., Shirahama-Noda, K., Hara-Nishimura, I., Ploegh, H.L. J. Immunol. (2005) [Pubmed]
  16. Purification and characterization of procathepsin L, a self-processing zymogen of guinea pig spermatozoa that acts on a cathepsin D assay substrate. McDonald, J.K., Emerick, J.M. Arch. Biochem. Biophys. (1995) [Pubmed]
  17. Cathepsin-L influences the expression of extracellular matrix in lymphoid organs and plays a role in the regulation of thymic output and of peripheral T cell number. Lombardi, G., Burzyn, D., Mundiñano, J., Berguer, P., Bekinschtein, P., Costa, H., Castillo, L.F., Goldman, A., Meiss, R., Piazzon, I., Nepomnaschy, I. J. Immunol. (2005) [Pubmed]
  18. A role for cathepsin L and cathepsin S in peptide generation for MHC class II presentation. Hsieh, C.S., deRoos, P., Honey, K., Beers, C., Rudensky, A.Y. J. Immunol. (2002) [Pubmed]
  19. Induction of cytotoxic T-lymphocyte antigen-2beta, a cysteine protease inhibitor in decidua: a potential regulator of embryo implantation. Cheon, Y.P., DeMayo, F.J., Bagchi, M.K., Bagchi, I.C. J. Biol. Chem. (2004) [Pubmed]
  20. Cathepsin S regulates the expression of cathepsin L and the turnover of gamma-interferon-inducible lysosomal thiol reductase in B lymphocytes. Honey, K., Duff, M., Beers, C., Brissette, W.H., Elliott, E.A., Peters, C., Maric, M., Cresswell, P., Rudensky, A. J. Biol. Chem. (2001) [Pubmed]
  21. Cathepsin L regulates CD4+ T cell selection independently of its effect on invariant chain: a role in the generation of positively selecting peptide ligands. Honey, K., Nakagawa, T., Peters, C., Rudensky, A. J. Exp. Med. (2002) [Pubmed]
  22. Regulation of collagenolytic protease secretion through c-Src in osteoclasts. Furuyama, N., Fujisawa, Y. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  23. Cathepsins L and S are not required for activation of dipeptidyl peptidase I (cathepsin C) in mice. Mallen-St Clair, J., Shi, G.P., Sutherland, R.E., Chapman, H.A., Caughey, G.H., Wolters, P.J. Biol. Chem. (2006) [Pubmed]
  24. Expression of cysteine proteases in extraembryonic tissues during mouse embryogenesis. Sol-Church, K., Shipley, J., Beckman, D.A., Mason, R.W. Arch. Biochem. Biophys. (1999) [Pubmed]
  25. Selective modulation of the secretion of proteinases and their inhibitors by growth factors in cultured differentiated podocytes. Asanuma, K., Shirato, I., Ishidoh, K., Kominami, E., Tomino, Y. Kidney Int. (2002) [Pubmed]
  26. Collagenolytic cysteine proteinases of bone tissue. Cathepsin B, (pro)cathepsin L and a cathepsin L-like 70 kDa proteinase. Delaissé, J.M., Ledent, P., Vaes, G. Biochem. J. (1991) [Pubmed]
  27. Dilated cardiomyopathy in mice deficient for the lysosomal cysteine peptidase cathepsin L. Stypmann, J., Gläser, K., Roth, W., Tobin, D.J., Petermann, I., Matthias, R., Mönnig, G., Haverkamp, W., Breithardt, G., Schmahl, W., Peters, C., Reinheckel, T. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  28. Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter. Yasothornsrikul, S., Greenbaum, D., Medzihradszky, K.F., Toneff, T., Bundey, R., Miller, R., Schilling, B., Petermann, I., Dehnert, J., Logvinova, A., Goldsmith, P., Neveu, J.M., Lane, W.S., Gibson, B., Reinheckel, T., Peters, C., Bogyo, M., Hook, V. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
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