Gene Review:
CTSL - cathepsin L
Homo sapiens
Synonyms:
CATL, CTSL1, Cathepsin L, Cathepsin L1, FLJ31037, ...
- Cathepsins B, L and D in inflammatory bowel disease macrophages and potential therapeutic effects of cathepsin inhibition in vivo. Menzel, K., Hausmann, M., Obermeier, F., Schreiter, K., Dunger, N., Bataille, F., Falk, W., Scholmerich, J., Herfarth, H., Rogler, G. Clin. Exp. Immunol. (2006)
- Prognostic impact of cysteine proteases cathepsin B and cathepsin L in pancreatic adenocarcinoma. Niedergethmann, M., Wostbrock, B., Sturm, J.W., Willeke, F., Post, S., Hildenbrand, R. Pancreas (2004)
- Cathepsin B, L, and S cleave and inactivate secretory leucoprotease inhibitor. Taggart, C.C., Lowe, G.J., Greene, C.M., Mulgrew, A.T., O'Neill, S.J., Levine, R.L., McElvaney, N.G. J. Biol. Chem. (2001)
- Marked increases in cathepsin B and L activities distinguish papillary carcinoma of the thyroid from normal thyroid or thyroid with non-neoplastic disease. Shuja, S., Murnane, M.J. Int. J. Cancer (1996)
- Expression of Cathepsin B and L antigen and activity is associated with early colorectal cancer progression. Troy, A.M., Sheahan, K., Mulcahy, H.E., Duffy, M.J., Hyland, J.M., O'Donoghue, D.P. Eur. J. Cancer (2004)
- Suppression of lymphocyte and neutrophil functions by Pseudomonas aeruginosa mucoid exopolysaccharide (alginate): reversal by physicochemical, alginase, and specific monoclonal antibody treatments. Mai, G.T., Seow, W.K., Pier, G.B., McCormack, J.G., Thong, Y.H. Infect. Immun. (1993)
- Crural amyotrophy associated with a parietal lesion: a case report. Pozzessere, G., Valle, E., Tomaselli, M., D'Alessio, M., Bianco, F., Pierelli, F., Morocutti, C. Acta neurologica Belgica. (1995)
- Motor responses evoked by magnetic brain stimulation in Huntington's disease. Meyer, B.U., Noth, J., Lange, H.W., Bischoff, C., Machetanz, J., Weindl, A., Röricht, S., Benecke, R., Conrad, B. Electroencephalography and clinical neurophysiology. (1992)
- Major histocompatibility complex class II-associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L. Bevec, T., Stoka, V., Pungercic, G., Dolenc, I., Turk, V. J. Exp. Med. (1996)
- Uptake of extracellular enzyme by a novel pathway is a major determinant of cathepsin L levels in human macrophages. Reilly, J.J., Chen, P., Sailor, L.Z., Mason, R.W., Chapman, H.A. J. Clin. Invest. (1990)
- Cathepsin B- and L-like activities at local gingival sites of chronic periodontitis patients. Eley, B.M., Cox, S.W. Journal of clinical periodontology. (1991)
- Immunohistochemical localization of cathepsin L and cystatin A in normal skin and skin tumors. Palungwachira, P., Kakuta, M., Yamazaki, M., Yaguchi, H., Tsuboi, R., Takamori, K., Ogawa, H. J. Dermatol. (2002)
- Cysteine and metalloproteinase activities in serum of Duchenne muscular dystrophic genotypes. Sohar, I., Laszlo, A., Gaal, K., Mechler, F. Biol. Chem. Hoppe-Seyler (1988)
- Characterization of downstream Ras signals that induce alternative protease-dependent invasive phenotypes. Silberman, S., Janulis, M., Schultz, R.M. J. Biol. Chem. (1997)
- Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice. Sevenich, L., Pennacchio, L.A., Peters, C., Reinheckel, T. Biol. Chem. (2006)
- Hurpin is a selective inhibitor of lysosomal cathepsin L and protects keratinocytes from ultraviolet-induced apoptosis. Welss, T., Sun, J., Irving, J.A., Blum, R., Smith, A.I., Whisstock, J.C., Pike, R.N., von Mikecz, A., Ruzicka, T., Bird, P.I., Abts, H.F. Biochemistry (2003)
- Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processing. Dahl, S.W., Halkier, T., Lauritzen, C., Dolenc, I., Pedersen, J., Turk, V., Turk, B. Biochemistry (2001)
- Amino acid sequences of the human kidney cathepsins H and L. Ritonja, A., Popović, T., Kotnik, M., Machleidt, W., Turk, V. FEBS Lett. (1988)
- Collagenase, cathepsin B and cathepsin L gene expression in the synovial membrane of patients with early inflammatory arthritis. Cunnane, G., FitzGerald, O., Hummel, K.M., Gay, R.E., Gay, S., Bresnihan, B. Rheumatology (Oxford, England) (1999)
- Colocalization of cystatin M/E and cathepsin V in lamellar granules and corneodesmosomes suggests a functional role in epidermal differentiation. Zeeuwen, P.L., Ishida-Yamamoto, A., van Vlijmen-Willems, I.M., Cheng, T., Bergers, M., Iizuka, H., Schalkwijk, J. J. Invest. Dermatol. (2007)
- Comparative responsiveness of HL-60, HL-60R, and HL-60R+ (LRARSN) cells to retinoic acid, calcitriol, 9 cis-retinoic acid, and sodium butyrate. Atkins, K.B., Troen, B.R. Blood (1995)
- Strong immunoreactivity of cathepsin L at the site of rimmed vacuoles in diseased muscles. Jimi, T., Satoh, Y., Takeda, A., Shibuya, S., Wakayama, Y., Sugita, K. Brain (1992)
- Cathepsin L inactivates alpha 1-proteinase inhibitor by cleavage in the reactive site region. Johnson, D.A., Barrett, A.J., Mason, R.W. J. Biol. Chem. (1986)
- Cathepsin L activity in alveolar macrophages of rats: response to cigarette smoke. Lesser, M., Galicki, N., Cardozo, C., Gariola, C.G. Am. J. Respir. Cell Mol. Biol. (1989)
- Kininogen-derived peptides for investigating the putative vasoactive properties of human cathepsins K and L. Desmazes, C., Galineau, L., Gauthier, F., Brömme, D., Lalmanach, G. Eur. J. Biochem. (2003)
- Serum concentration and circadian profiles of cathepsins B, H and L, and their inhibitors, stefins A and B, in asthma. Cimerman, N., Mesko Brguljan, P., Krasovec, M., Suskovic, S., Kos, J. Clin. Chim. Acta (2001)
- Characterization by spectroscopic, kinetic and equilibrium methods of the interaction between recombinant human cystatin A (stefin A) and cysteine proteinases. Pol, E., Olsson, S.L., Estrada, S., Prasthofer, T.W., Björk, I. Biochem. J. (1995)
- Cathepsin L, but not cathepsin B, is a potential kininogenase. Desmazes, C., Gauthier, F., Lalmanach, G. Biol. Chem. (2001)
- Human proteoglycan testican-1 inhibits the lysosomal cysteine protease cathepsin L. Bocock, J.P., Edgell, C.J., Marr, H.S., Erickson, A.H. Eur. J. Biochem. (2003)
- Recombinant human cathepsin X is a carboxymonopeptidase only: a comparison with cathepsins B and L. Puzer, L., Cotrin, S.S., Cezari, M.H., Hirata, I.Y., Juliano, M.A., Stefe, I., Turk, D., Turk, B., Juliano, L., Carmona, A.K. Biol. Chem. (2005)
- Substrate specificity of recombinant cysteine proteinase, CPB, of Leishmania mexicana. Alves, L.C., Judice, W.A., St Hilaire, P.M., Meldal, M., Sanderson, S.J., Mottram, J.C., Coombs, G.H., Juliano, L., Juliano, M.A. Mol. Biochem. Parasitol. (2001)
- O-Linked glycans control glycoprotein processing by antigen-presenting cells: a biochemical approach to the molecular aspects of MUC1 processing by dendritic cells. Hanisch, F.G., Schwientek, T., Von Bergwelt-Baildon, M.S., Schultze, J.L., Finn, O. Eur. J. Immunol. (2003)
- 3-hydroxy-3-methylglutaryl coenzyme A reductase is sterol-dependently cleaved by cathepsin L-type cysteine protease in the isolated endoplasmic reticulum. Moriyama, T., Wada, M., Urade, R., Kito, M., Katunuma, N., Ogawa, T., Simoni, R.D. Arch. Biochem. Biophys. (2001)
- Naegleria fowleri: characterization of a secreted histolytic cysteine protease. Aldape, K., Huizinga, H., Bouvier, J., McKerrow, J. Exp. Parasitol. (1994)
- Effective activation of the proenzyme form of the urokinase-type plasminogen activator (pro-uPA) by the cysteine protease cathepsin L. Goretzki, L., Schmitt, M., Mann, K., Calvete, J., Chucholowski, N., Kramer, M., Günzler, W.A., Jänicke, F., Graeff, H. FEBS Lett. (1992)
- The inhibition of cathepsin S by its propeptide--specificity and mechanism of action. Maubach, G., Schilling, K., Rommerskirch, W., Wenz, I., Schultz, J.E., Weber, E., Wiederanders, B. Eur. J. Biochem. (1997)
- Squamous cell carcinoma antigen is a potent inhibitor of cysteine proteinase cathepsin L. Takeda, A., Yamamoto, T., Nakamura, Y., Takahashi, T., Hibino, T. FEBS Lett. (1995)
- The role of the kininogens as cysteine proteinase inhibitors in local and systemic inflammation. Assfalg-Machleidt, I., Billing, A., Fröhlich, D., Nast-Kolb, D., Joka, T., Jochum, M., Machleidt, W. Agents Actions Suppl. (1992)
- Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification. Cheng, T., Hitomi, K., van Vlijmen-Willems, I.M., de Jongh, G.J., Yamamoto, K., Nishi, K., Watts, C., Reinheckel, T., Schalkwijk, J., Zeeuwen, P.L. J. Biol. Chem. (2006)
- Engineering the S2 subsite specificity of human cathepsin S to a cathepsin L- and cathepsin B-like specificity. Brömme, D., Bonneau, P.R., Lachance, P., Storer, A.C. J. Biol. Chem. (1994)
- Identification of peptide fragments generated by digestion of bovine and human osteocalcin with the lysosomal proteinases cathepsin B, D, L, H, and S. Baumgrass, R., Williamson, M.K., Price, P.A. J. Bone Miner. Res. (1997)
- Cathepsin L is capable of truncating cystatin C of 11 N-terminal amino acids. Popovic, T., Cimerman, N., Dolenc, I., Ritonja, A., Brzin, J. FEBS Lett. (1999)