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Cathepsin L1
PBB Protein CTSL1 image.jpg
PDB rendering based on 1cjl.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Symbols CTSL1 ; CATL; CTSL; FLJ31037; MEP
External IDs Template:OMIM5 HomoloGene76699
RNA expression pattern
PBB GE CTSL1 202087 s at tn.png
More reference expression data
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Cathepsin L1, also known as CTSL1, is a human gene.[1]

The protein encoded by this gene is a lysosomal cysteine proteinase that plays a major role in intracellular protein catabolism. Its substrates include collagen and elastin, as well as alpha-1 protease inhibitor, a major controlling element of neutrophil elastase activity. The encoded protein has been implicated in several pathologic processes, including myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria. This protein, which is a member of the peptidase C1 family, is a dimer composed of disulfide-linked heavy and light chains, both produced from a single protein precursor. At least two transcript variants encoding the same protein have been found for this gene.[1]


  1. 1.0 1.1 "Entrez Gene: CTSL1 cathepsin L1".

Further reading

  • Smith CG, Smith MT, Besch NF; et al. (1980). "Effect of delta 9-tetrahydrocannabinol (THC) on female reproductive function". Advances in the biosciences. 22-23: 449–67. PMID 116880.
  • Goretzki L, Schmitt M, Mann K; et al. (1992). "Effective activation of the proenzyme form of the urokinase-type plasminogen activator (pro-uPA) by the cysteine protease cathepsin L.". FEBS Lett. 297 (1–2): 112–8. PMID 1551416.
  • Dunn AD, Crutchfield HE, Dunn JT (1991). "Thyroglobulin processing by thyroidal proteases. Major sites of cleavage by cathepsins B, D, and L.". J. Biol. Chem. 266 (30): 20198–204. PMID 1939080.
  • Stearns NA, Dong JM, Pan JX; et al. (1991). "Comparison of cathepsin L synthesized by normal and transformed cells at the gene, message, protein, and oligosaccharide levels". Arch. Biochem. Biophys. 283 (2): 447–57. PMID 2275556.
  • Joseph LJ, Chang LC, Stamenkovich D, Sukhatme VP (1988). "Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts". J. Clin. Invest. 81 (5): 1621–9. PMID 2835398.
  • Ritonja A, Popović T, Kotnik M; et al. (1988). "Amino acid sequences of the human kidney cathepsins H and L.". FEBS Lett. 228 (2): 341–5. PMID 3342889.
  • Gal S, Gottesman MM (1988). "Isolation and sequence of a cDNA for human pro-(cathepsin L)". Biochem. J. 253 (1): 303–6. PMID 3421948.
  • Johnson DA, Barrett AJ, Mason RW (1986). "Cathepsin L inactivates alpha 1-proteinase inhibitor by cleavage in the reactive site region". J. Biol. Chem. 261 (31): 14748–51. PMID 3490478.
  • Mason RW, Walker JE, Northrop FD (1987). "The N-terminal amino acid sequences of the heavy and light chains of human cathepsin L. Relationship to a cDNA clone for a major cysteine proteinase from a mouse macrophage cell line". Biochem. J. 240 (2): 373–7. PMID 3545185.
  • Joseph L, Lapid S, Sukhatme V (1987). "The major ras induced protein in NIH3T3 cells is cathepsin L.". Nucleic Acids Res. 15 (7): 3186. PMID 3550705.
  • Kärgel HJ, Dettmer R, Etzold G; et al. (1982). "Action of rat liver cathepsin L on glucagon". Acta Biol. Med. Ger. 40 (9): 1139–43. PMID 7340337.
  • Chauhan SS, Popescu NC, Ray D; et al. (1993). "Cloning, genomic organization, and chromosomal localization of human cathepsin L.". J. Biol. Chem. 268 (2): 1039–45. PMID 8419312.
  • Bevec T, Stoka V, Pungercic G; et al. (1996). "Major histocompatibility complex class II-associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L.". J. Exp. Med. 183 (4): 1331–8. PMID 8666891.
  • Coulombe R, Grochulski P, Sivaraman J; et al. (1996). "Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment". EMBO J. 15 (20): 5492–503. PMID 8896443.
  • Baumgrass R, Williamson MK, Price PA (1997). "Identification of peptide fragments generated by digestion of bovine and human osteocalcin with the lysosomal proteinases cathepsin B, D, L, H, and S.". J. Bone Miner. Res. 12 (3): 447–55. PMID 9076588.
  • Fujishima A, Imai Y, Nomura T; et al. (1997). "The crystal structure of human cathepsin L complexed with E-64". FEBS Lett. 407 (1): 47–50. PMID 9141479.
  • Ménard R, Carmona E, Takebe S; et al. (1998). "Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro". J. Biol. Chem. 273 (8): 4478–84. PMID 9468501.
  • Schick C, Pemberton PA, Shi GP; et al. (1998). "Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: a kinetic analysis". Biochemistry. 37 (15): 5258–66. doi:10.1021/bi972521d. PMID 9548757.
  • Estrada S, Nycander M, Hill NJ; et al. (1998). "The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin L.". Biochemistry. 37 (20): 7551–60. doi:10.1021/bi980026r. PMID 9585570.
  • Halfon S, Ford J, Foster J; et al. (1998). "Leukocystatin, a new Class II cystatin expressed selectively by hematopoietic cells". J. Biol. Chem. 273 (26): 16400–8. PMID 9632704.

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