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Gene Review

CTSV  -  cathepsin V

Bos taurus

Synonyms: CTSL, CTSL1, CTSL2
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High impact information on CTSL

  • This finding in turn indicated that the protease for which MAG was a substrate had cathepsin L-like activity [1].
  • Cathepsin L-like activity in myelin was confirmed by peptidolysis experiments using known cathepsin L substrates [1].
  • 0. Cathepsin S was found to hydrolyse proteins at a similar rate to cathepsin L below pH 7 [2].
  • We show that proBac7 is a monocyte-selective chemoattractant, potentially contributing to the recruitment of these cells to infection sites, whereas proBac5 efficiently inhibits the in vitro activity of cathepsin L, a cysteine proteinase thought to contribute to tissue injury in inflammation [3].
  • The results strongly suggest the involvement of cathepsin B- and cathepsin L-like proteinases in the histolysis of the silk gland during metamorphosis [4].

Biological context of CTSL

  • N-terminal amino acid sequence confirms that cathepsin L and cathepsin S are different enzymes [5].
  • Based on pH profiles of activity, inhibition studies using diethylpyrocarbonate and the diazomethylketone Z-phe-ala-CHN2, and characterising the substrate specificity of the enzymes using fluorogenic peptide substrates we have shown that the 60-90-kDa proteinases are cathepsin L-like proteinases [6].
  • Although to a varying extent, P1, P2 and P3 inhibited papain, cathepsin B and cathepsin L. Analysis of the peptide mixtures of these inhibitors by RP-HPLC after hydrolysis with CNBr or aspartly endoproteinase N together with their amino acid composition revealed that P1, P2 and P3 cysteine proteinase inhibitors are isoforms of the same protein [7].
  • Antibody responses to the 28-30 kDa proteins were not detected in groups B-D until 3 weeks later than those observed in group A. Antibody responses to Fasciola hepatica cathepsin L proteases, which are known to induce protection, were monophasic, of the IgG1 isotype only and were not observed prior to secondary challenge in any of the four groups [8].

Anatomical context of CTSL


Associations of CTSL with chemical compounds

  • The appearance of higher molecular-sized components in the cathepsin L clots suggests that polymerisation involves the formation of molecular interactions that are resistant to boiling in mercaptoethanol and SDS [12].
  • Also, PTP does not exhibit dipeptidycarboxylpeptidase activity, a property of cathepsin B; PTP demonstrates no elastinolytic activity, a characteristic of cathepsin L. Importantly, the sensitivity of PTP to active-site-directed peptide diazomethane inhibitors and E-64c differs from that of cathepsins B, L, and H [13].
  • Both were rapidly inhibited by low concentrations of E-64 or leupeptin, but were unaffected by cathepsin-L-specific inhibitor Z-Phe-Phe-CHN2 [14].

Other interactions of CTSL


Analytical, diagnostic and therapeutic context of CTSL


  1. Determination of a native proteolytic site in myelin-associated glycoprotein. Stebbins, J.W., Jaffe, H., Fales, H.M., Möller, J.R. Biochemistry (1997) [Pubmed]
  2. Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins. Kirschke, H., Wiederanders, B., Brömme, D., Rinne, A. Biochem. J. (1989) [Pubmed]
  3. Chemotactic and protease-inhibiting activities of antibiotic peptide precursors. Verbanac, D., Zanetti, M., Romeo, D. FEBS Lett. (1993) [Pubmed]
  4. Involvement of cathepsin B- and L-like proteinases in silk gland histolysis during metamorphosis of Bombyx mori. Shiba, H., Uchida, D., Kobayashi, H., Natori, M. Arch. Biochem. Biophys. (2001) [Pubmed]
  5. Bovine cathepsins S and L: isolation and amino acid sequences. Dolenc, I., Ritonja, A., Colić, A., Podobnik, M., Ogrinc, T., Turk, V. Biol. Chem. Hoppe-Seyler (1992) [Pubmed]
  6. Fasciola hepatica: a secreted cathepsin L-like proteinase cleaves host immunoglobulin. Smith, A.M., Dowd, A.J., Heffernan, M., Robertson, C.D., Dalton, J.P. Int. J. Parasitol. (1993) [Pubmed]
  7. Purification and characterisation of a polymorphic low M(r) bovine muscle cysteine proteinase inhibitor: structural identity with fatty-acid-binding proteins. Zabari, M., Berri, M., Rouchon, P., Zamora, F., Tassy, C., Ribadeau-Dumas, B., Ouali, A. Biochimie (1993) [Pubmed]
  8. Pre-exposure of cattle to drug-abbreviated Fasciola hepatica infections: the effect upon subsequent challenge infection and the early immune response. Hoyle, D.V., Dalton, J.P., Chase-Topping, M., Taylor, D.W. Vet. Parasitol. (2003) [Pubmed]
  9. Cathepsin S. The cysteine proteinase from bovine lymphoid tissue is distinct from cathepsin L (EC Kirschke, H., Schmidt, I., Wiederanders, B. Biochem. J. (1986) [Pubmed]
  10. Autophagic vacuoles fuse with the prelysosomal compartment in cultured rat fibroblasts. Punnonen, E.L., Autio, S., Kaija, H., Reunanen, H. Eur. J. Cell Biol. (1993) [Pubmed]
  11. Purification and characterization of a new potential in vivo inhibitor of cathepsin L from bovine skeletal muscle. Berri, M., Rouchon, P., Zabari, M., Ouali, A. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (1998) [Pubmed]
  12. Fasciola hepatica cathepsin L proteinase cleaves fibrinogen and produces a novel type of fibrin clot. Dowd, A.J., McGonigle, S., Dalton, J.P. Eur. J. Biochem. (1995) [Pubmed]
  13. Distinct properties of prohormone thiol protease (PTP) compared to cathepsins B, L, and H: evidence for PTP as a novel cysteine protease. Azaryan, A.V., Hook, V.Y. Arch. Biochem. Biophys. (1994) [Pubmed]
  14. Purification and properties of different isoforms of bovine cathepsin B. Deval, C., Bechet, D., Obled, A., Ferrara, M. Biochem. Cell Biol. (1990) [Pubmed]
  15. Human and bovine brain cathepsin L and cathepsin H: purification, physico-chemical properties, and specificity. Azaryan, A., Galoyan, A. Neurochem. Res. (1987) [Pubmed]
  16. Induction of protective immunity in cattle against infection with Fasciola hepatica by vaccination with cathepsin L proteinases and with hemoglobin. Dalton, J.P., McGonigle, S., Rolph, T.P., Andrews, S.J. Infect. Immun. (1996) [Pubmed]
  17. Early immunodiagnosis of fasciolosis in ruminants using recombinant Fasciola hepatica cathepsin L-like protease. Cornelissen, J.B., Gaasenbeek, C.P., Borgsteede, F.H., Holland, W.G., Harmsen, M.M., Boersma, W.J. Int. J. Parasitol. (2001) [Pubmed]
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