The protein encoded by this gene is a lysosomal cysteine protease 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.
^Estrada, S; Nycander M; Hill N J; Craven C J; Waltho J P; Björk I (May 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 (UNITED STATES) 37 (20): 7551–60. doi:10.1021/bi980026r. ISSN0006-2960. PMID9585570.
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. PMID116880.
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. doi:10.1016/0014-5793(92)80339-I. PMID1551416.
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. PMID1939080.
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. doi:10.1016/0003-9861(90)90666-M. PMID2275556.
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. doi:10.1359/jbmr.19188.8.131.527. PMID9076588.
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. doi:10.1074/jbc.273.8.4478. PMID9468501.
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.". Biochemistry37 (15): 5258–66. doi:10.1021/bi972521d. PMID9548757.
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.". Biochemistry37 (20): 7551–60. doi:10.1021/bi980026r. PMID9585570.
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. doi:10.1074/jbc.273.26.16400. PMID9632704.