組織蛋白酶V
組織蛋白酶V, （EC 3.4.22.43，也被稱為組織蛋白酶L2或組織蛋白酶U），是一種在人類中由CTSV基因編碼的蛋白質。[5][6][7][8]
該蛋白質是木瓜蛋白酶樣蛋白酶家族（MEROPS家族C1）的成員，這是一種具有內肽酶活性的溶體半胱胺酸蛋白酶。它可能在角膜生理學中起重要作用。該基因在結腸直腸癌和乳癌中表現，但在正常結腸、乳腺或腫瘤周圍組織中不表現，這表明該基因在腫瘤過程中可能發揮作用。
臨床意義
參考文獻
- ^ 1.0 1.1 1.2 GRCh38: Ensembl release 89: ENSG00000136943 - Ensembl, May 2017
- ^ 2.0 2.1 2.2 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
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閱讀
- 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.
外部連結
- The MEROPS online database for peptidases and their inhibitors: C01.009 （頁面存檔備份，存於網際網路檔案館）
- 醫學主題詞表（MeSH）：Cathepsin+V
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