組織蛋白酶V

組織蛋白酶V
已知的結構
PDB	直系同源搜索: PDBe RCSB
PDBID列表
	1FH0、3H6S、3KFQ
識別號
別名	CTSV；, cathepsin V, CATL2, CTSL2, CTSU
外部ID	OMIM：603308 MGI：88564 HomoloGene：76699 GeneCards：CTSV
基因位置（人類）
染色體	9號染色體
終止	97,156,556 bp
基因位置（小鼠）
染色體	小鼠13號染色體
終止	64,518,704 bp
RNA表達模式
	查閱更多表達數據
基因本體
分子功能	• 半胱氨酸型肽酶活性; • peptide binding; • 肽酶活性; • 血漿蛋白結合; • aminopeptidase activity; • 水解酶活性; • serine-type endopeptidase activity; • cysteine-type endopeptidase activity; • cysteine-type carboxypeptidase activity; • histone binding; • kininogen binding; • 大分子複合物結合;
細胞組分	• 細胞質; • 細胞本體; • apical part of cell; • secretory granule; • 細胞外區域; • 微絨毛; • 液胞; • lysosomal lumen; • neuron projection; • 溶酶體; • external side of plasma membrane; • 細胞外空間; • 細胞核; • 核仁; • cytoplasmic vesicle;
生物學過程	• male gonad development; • response to organic cyclic compound; • antigen processing and presentation of exogenous peptide antigen via MHC class II; • cellular response to starvation; • extracellular matrix disassembly; • response to glucocorticoid; • response to glucose; • Sertoli cell differentiation; • response to gonadotropin; • 蛋白酶解; • cell communication; • 蛻膜化; • 精子發生; • multicellular organism aging; • proteolysis involved in cellular protein catabolic process; • nerve development; • autophagic cell death; • response to odorant; • regulation of keratinocyte differentiation; • negative regulation of keratinocyte proliferation; • protein processing; • protein autoprocessing; • hair follicle morphogenesis; • regulation of actin cytoskeleton reorganization;
	Sources:Amigo / QuickGO
直系同源
	1515
	13039
	ENSG00000136943
	ENSMUSG00000021477
	O60911
	P06797
	NM_001333; NM_001201575
	NM_009984
	NP_001188504; NP_001324
	NP_034114
	維基數據
檢視/編輯人類	檢視/編輯小鼠

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酶體半胱氨酸蛋白酶。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達，但在正常結腸、乳腺或腫瘤周圍組織中不表達，這表明該基因在腫瘤過程中可能發揮作用。

臨床意義

組織蛋白酶V可能在圓錐角膜的發病機制中發揮作用。^[9]

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  .

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

[refGRCh38Ensembl-1] 1.0 ^1.1 ^1.2 GRCh38: Ensembl release 89: ENSG00000136943 - Ensembl, May 2017

[refGRCm38Ensembl-2] 2.0 ^2.1 ^2.2 GRCm38: Ensembl release 89: ENSMUSG00000021477 - Ensembl, May 2017

[3] Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] Entrez Gene: CTSL2 cathepsin L2.

[6] 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.

[7] 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.

[8] 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.

[Kenney05-9] 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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