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 peptidaseC1 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.
↑Kenney MC, Chwa M, Atilano SR, Tran A, Carballo M, Saghizadeh M, Vasiliou V, Adachi W, Brown DJ (2005). "Increased levels of catalase and cathepsin V/L2 but decreased TIMP-1 in keratoconus corneas: evidence that oxidative stress plays a role in this disorder". Invest. Ophthal. Vis. Sci. 46: 823–832. doi:10.1167/iovs.04-0549. PMID15728537.
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. PMID9563472.
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. PMID9727401.
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. PMID10029531.
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. PMID10382972.
Somoza JR, Zhan H, Bowman KK, et al. (2000). "Crystal structure of human cathepsin V.". Biochemistry. 39 (41): 12543–51. doi:10.1021/bi000951p. PMID11027133.
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. PMID12648222.
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. PMID15192101.
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. PMID15679121.
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. PMID16565075.
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. PMID17516850.
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. PMID17869649.
