组织蛋白酶V

组织蛋白酶V, （EC 3.4.22.43，也被称为组织蛋白酶L2或组织蛋白酶U），是一种在人类中由CTSV基因编码的蛋白质。 该蛋白质是木瓜蛋白酶样蛋白酶家族（MEROPS家族C1）的成员，这是一种具有内肽酶活性的溶酶体半胱氨酸蛋白酶。它可能在角膜生理学中起重要作用。该基因在结肠直肠癌和乳癌中表达，但在正常结肠、乳腺或肿瘤周围组织中不表达，这表明该基因在肿瘤过程中可能发挥作用。 组织蛋白酶V可能在圆锥角膜的发病机制中发挥作用。 GRCh38: Ensembl release 89: ENSG00000136943 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000021477 - Ensembl, May 2017 Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.  Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.  Entrez Gene: CTSL2 cathepsin L2.  Brömme D, Li Z, Barnes M, Mehler E. Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry. February 1999, 38 (8): 2377–85. PMID 10029531. doi:10.1021/bi982175f.  Adachi W, Kawamoto S, Ohno I, Nishida K, Kinoshita S, Matsubara K, Okubo K. Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium. Investigative Ophthalmology & Visual Science. September 1998, 39 (10): 1789–96. PMID 9727401.  Santamaría I, Velasco G, Cazorla M, Fueyo A, Campo E, López-Otín C. Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas. Cancer Research. April 1998, 58 (8): 1624–30. PMID 9563472.  Kenney MC, Chwa M, Atilano SR, Tran A, Carballo M, Saghizadeh M, Vasiliou V, Adachi W, Brown DJ. 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. Ophthalmol. Vis. Sci. 2005, 46 (3): 823–832. PMID 15728537. doi:10.1167/iovs.04-0549 .  Santamaría I, Velasco G, Cazorla M, et al. Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas.. Cancer Res. 1998, 58 (8): 1624–30. PMID 9563472.  Adachi W, Kawamoto S, Ohno I, et al. Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium.. Invest. Ophthalmol. Vis. Sci. 1998, 39 (10): 1789–96. PMID 9727401.  Brömme D, Li Z, Barnes M, Mehler E. Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization.. Biochemistry. 1999, 38 (8): 2377–85. PMID 10029531. doi:10.1021/bi982175f.  Itoh R, Kawamoto S, Adachi W, et al. Genomic organization and chromosomal localization of the human cathepsin L2 gene.. DNA Res. 1999, 6 (2): 137–40. PMID 10382972. doi:10.1093/dnares/6.2.137 .  Somoza JR, Zhan H, Bowman KK, et al. Crystal structure of human cathepsin V.. Biochemistry. 2000, 39 (41): 12543–51. PMID 11027133. doi:10.1021/bi000951p.  Strausberg RL, Feingold EA, Grouse LH, et al. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.. Proc. Natl. Acad. Sci. U.S.A. 2003, 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899 .  Bernard D, Méhul B, Thomas-Collignon A, et al. 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. 2003, 120 (4): 592–600. PMID 12648222. doi:10.1046/j.1523-1747.2003.12086.x .  Tolosa E, Li W, Yasuda Y, et al. Cathepsin V is involved in the degradation of invariant chain in human thymus and is overexpressed in myasthenia gravis.. J. Clin. Invest. 2003, 112 (4): 517–26. PMC 171390 . PMID 12925692. doi:10.1172/JCI18028.  Clark HF, Gurney AL, Abaya E, et al. The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.. Genome Res. 2003, 13 (10): 2265–70. PMC 403697 . PMID 12975309. doi:10.1101/gr.1293003.  Humphray SJ, Oliver K, Hunt AR, et al. DNA sequence and analysis of human chromosome 9.. Nature. 2004, 429 (6990): 369–74. Bibcode:2004Natur.429..369H. PMC 2734081 . PMID 15164053. doi:10.1038/nature02465.  Yasuda Y, Li Z, Greenbaum D, et al. Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages.. J. Biol. Chem. 2004, 279 (35): 36761–70. PMID 15192101. doi:10.1074/jbc.M403986200 .  Gerhard DS, Wagner L, Feingold EA, et al. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).. Genome Res. 2004, 14 (10B): 2121–7. PMC 528928 . PMID 15489334. doi:10.1101/gr.2596504.  Hagemann S, Günther T, Dennemärker J, et al. The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles.. Eur. J. Cell Biol. 2005, 83 (11–12): 775–80. PMID 15679121. doi:10.1078/0171-9335-00404.  Cheng T, Hitomi K, van Vlijmen-Willems IM, et al. 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. 2006, 281 (23): 15893–9. PMID 16565075. doi:10.1074/jbc.M600694200 .  Burden RE, Snoddy P, Jefferies CA, et al. Inhibition of cathepsin L-like proteases by cathepsin V propeptide.. Biol. Chem. 2007, 388 (5): 541–5. PMID 17516850. S2CID 6680659. doi:10.1515/BC.2007.053.  Viken MK, Sollid HD, Joner G, et al. Polymorphisms in the cathepsin L2 (CTSL2) gene show association with type 1 diabetes and early-onset myasthenia gravis.. Hum. Immunol. 2007, 68 (9): 748–55. PMID 17869649. doi:10.1016/j.humimm.2007.05.009.  The MEROPS online database for peptidases and their inhibitors: C01.009 （页面存档备份，存于互联网档案馆） 醫學主題詞表（MeSH）：Cathepsin+V