CTSL1

Cathepsin L1, also known as CTSL1, is a human gene.cite web | title = Entrez Gene: CTSL1 cathepsin L1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1514| accessdate = ]

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: CTSL1 cathepsin L1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1514| accessdate = ]

References

Further reading

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

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