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Gene Review

CTSL2  -  cathepsin L2

Gallus gallus

Synonyms: CTSL, CTSL1
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Disease relevance of CTSL1


High impact information on CTSL1

  • Like the analogous diazomethyl ketones 4 and 5, these inhibitors were also found to inactivate cathepsin L in common with other inhibitors under current investigation [2].
  • The complete amino acid sequence of cathepsin L has been determined and consists of 215 residues [3].
  • Cathepsin L exhibited a single band of Mr 27,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions, presented a high affinity for the substrate Z-Phe-Arg-NMec, was very unstable at neutral pH, and was inhibited by Z-Phe-Phe-CHN2 [3].
  • Cathepsin L was purified from chicken liver lysosomes by a two-step procedure [3].
  • 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) [4].

Biological context of CTSL1


Associations of CTSL1 with chemical compounds


Analytical, diagnostic and therapeutic context of CTSL1

  • Antibodies, raised in chickens (IgY) and rabbits (IgG) against the lysosomal proteinase cathepsin L, targeted the enzyme in an ELISA and Western blot [7].
  • The secondary structure of the recently sequenced chicken liver cathepsin L (EC has been studied both by circular dichroism and a predictive method [8].


  1. Cathepsin B and L activities in isolated osteoclasts. Rifkin, B.R., Vernillo, A.T., Kleckner, A.P., Auszmann, J.M., Rosenberg, L.R., Zimmerman, M. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  2. Inactivation of calpain by peptidyl fluoromethyl ketones. Angliker, H., Anagli, J., Shaw, E. J. Med. Chem. (1992) [Pubmed]
  3. Purification and amino acid sequence of chicken liver cathepsin L. Dufour, E., Obled, A., Valin, C., Béchet, D., Ribadeau-Dumas, B., Huet, J.C. Biochemistry (1987) [Pubmed]
  4. 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]
  5. Sequence homologies, hydrophobic profiles and secondary structures of cathepsins B, H and L: comparison with papain and actinidin. Dufour, E. Biochimie (1988) [Pubmed]
  6. Proteolytic specificity of chicken cathepsin L on bovine beta-casein. Dufour, E., Ribadeau-Dumas, B. Biosci. Rep. (1988) [Pubmed]
  7. Localization of an immunoinhibitory epitope of the cysteine proteinase, cathepsin L. Coetzer, T.H., Pike, R.N., Dennison, C. Immunol. Invest. (1992) [Pubmed]
  8. Delineation of chicken cathepsin L secondary structure; relationship between pH dependence activity and helix content. Dufour, E., Dive, V., Toma, F. Biochim. Biophys. Acta (1988) [Pubmed]
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