Cathepsin L2
Cathepsin L2, also known as cathepsin V and encoded by the CTSL2 gene, is a human gene.[1]
The protein encoded by this gene, a member of the peptidase C1 family, is a lysosomal cysteine proteinase that may play an important role in corneal physiology. This gene is expressed in colorectal and breast carcinomas but not in normal colon, mammary gland, or peritumoral tissues, suggesting a possible role for this gene in tumor processes.
Clinical significance
Cathepsin L2 may play a role in the pathogenesis of keratoconus.[2]
References
- ^ "Entrez Gene: CTSL2 cathepsin L2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1515.
- ^ Kenney, M. C.; Chwa, M.; Atilano, S. R.; Tran, A.; Carballo, M.; Saghizadeh, M.; Vasiliou, V.; Adachi, W.; Brown, D. J. : Increased levels of catalase and cathepsin V/L2 but decreased TIMP-1 in keratoconus corneas: evidence that oxidative stress plays an role in this disorder. Invest. Ophthal. Vis. Sci. 46: 823-832, 2005. PMID 15728537
External links
- The MEROPS online database for peptidases and their inhibitors: C01.009
Further reading
- Santamaría I, Velasco G, Cazorla M, et al. (1998). "Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas.". Cancer Res. 58 (8): 1624–30. PMID 9563472.
- Adachi W, Kawamoto S, Ohno I, et al. (1998). "Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium.". Invest. Ophthalmol. Vis. Sci. 39 (10): 1789–96. PMID 9727401.
- Brömme D, Li Z, Barnes M, Mehler E (1999). "Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization.". Biochemistry 38 (8): 2377–85. doi:10.1021/bi982175f. PMID 10029531.
- Itoh R, Kawamoto S, Adachi W, et al. (1999). "Genomic organization and chromosomal localization of the human cathepsin L2 gene.". DNA Res. 6 (2): 137–40. doi:10.1093/dnares/6.2.137. PMID 10382972.
- Somoza JR, Zhan H, Bowman KK, et al. (2000). "Crystal structure of human cathepsin V.". Biochemistry 39 (41): 12543–51. doi:10.1021/bi000951p. PMID 11027133.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Bernard D, Méhul B, Thomas-Collignon A, et al. (2003). "Analysis of proteins with caseinolytic activity in a human stratum corneum extract revealed a yet unidentified cysteine protease and identified the so-called "stratum corneum thiol protease" as cathepsin l2.". J. Invest. Dermatol. 120 (4): 592–600. doi:10.1046/j.1523-1747.2003.12086.x. PMID 12648222.
- Tolosa E, Li W, Yasuda Y, et al. (2003). "Cathepsin V is involved in the degradation of invariant chain in human thymus and is overexpressed in myasthenia gravis.". J. Clin. Invest. 112 (4): 517–26. doi:10.1172/JCI200318028. PMID 12925692.
- Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=403697.
- Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9.". Nature 429 (6990): 369–74. doi:10.1038/nature02465. PMC 2734081. PMID 15164053. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2734081.
- Yasuda Y, Li Z, Greenbaum D, et al. (2004). "Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages.". J. Biol. Chem. 279 (35): 36761–70. doi:10.1074/jbc.M403986200. PMID 15192101.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- Hagemann S, Günther T, Dennemärker J, et al. (2005). "The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles.". Eur. J. Cell Biol. 83 (11-12): 775–80. doi:10.1078/0171-9335-00404. PMID 15679121.
- Cheng T, Hitomi K, van Vlijmen-Willems IM, et al. (2006). "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.". J. Biol. Chem. 281 (23): 15893–9. doi:10.1074/jbc.M600694200. PMID 16565075.
- Burden RE, Snoddy P, Jefferies CA, et al. (2007). "Inhibition of cathepsin L-like proteases by cathepsin V propeptide.". Biol. Chem. 388 (5): 541–5. doi:10.1515/BC.2007.053. PMID 17516850.
- Viken MK, Sollid HD, Joner G, et al. (2007). "Polymorphisms in the cathepsin L2 (CTSL2) gene show association with type 1 diabetes and early-onset myasthenia gravis.". Hum. Immunol. 68 (9): 748–55. doi:10.1016/j.humimm.2007.05.009. PMID 17869649.
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1fh0: CRYSTAL STRUCTURE OF HUMAN CATHEPSIN V COMPLEXED WITH AN IRREVERSIBLE VINYL SULFONE INHIBITOR
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