• 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 • 精子发生 • 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
^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.
阅读
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.
外部链接
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）
组织蛋白酶v, 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, 已知的結構pdb直系同源搜索, pdbe, rcsbpdbid列表1fh0, 3h6s, 3kfq識別號别名ctsv, cathepsin, catl2, ctsl2, ctsu外部idomim, 603308, 88564, homologene, 76699, genecards, ctsv基因位置, 人类, 染色体9號染色體, 基因座9q22, 33起始97, 终止97, 基因位置, 小鼠, 染色体小鼠13号染. 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 5 6 7 8 组织蛋白酶V已知的結構PDB直系同源搜索 PDBe RCSBPDBID列表1FH0 3H6S 3KFQ識別號别名CTSV cathepsin V CATL2 CTSL2 CTSU外部IDOMIM 603308 MGI 88564 HomoloGene 76699 GeneCards CTSV基因位置 人类 染色体9號染色體 1 基因座9q22 33起始97 029 677 bp 1 终止97 156 556 bp 1 基因位置 小鼠 染色体小鼠13号染色体 2 基因座13 B3 13 33 26 cM起始64 507 151 bp 2 终止64 518 704 bp 2 RNA表达模式查阅更多表达数据基因本體分子功能 半胱氨酸型肽酶活性 peptide binding 肽酶活性 血浆蛋白结合 aminopeptidase activity 水解酶活性 serine type endopeptidase activity cysteine type endopeptidase activity cysteine type carboxypeptidase activity histone binding kininogen binding 大分子复合物结合細胞組分 細胞質 細胞本體 apical part of cell secretory granule 細胞外區域 微绒毛 液胞 lysosomal lumen neuron projection 溶酶体 external side of plasma membrane 細胞外空間 细胞核 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 精子发生 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 reorganizationSources Amigo QuickGO直系同源物種人類小鼠Entrez151513039EnsemblENSG00000136943ENSMUSG00000021477UniProtO60911P06797mRNA 序列NM 001333 NM 001201575NM 009984蛋白序列NP 001188504 NP 001324NP 034114基因位置 UCSC Chr 9 97 03 97 16 MbChr 13 64 51 64 52 MbPubMed 查找 3 4 維基數據檢視 編輯人類檢視 編輯小鼠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 目录 1 临床意义 2 参考文献 3 阅读 4 外部链接临床意义 编辑组织蛋白酶V可能在圆锥角膜的发病机制中发挥作用 9 参考文献 编辑 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 Bromme 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 amp Visual Science September 1998 39 10 1789 96 PMID 9727401 Santamaria I Velasco G Cazorla M Fueyo A Campo E Lopez Otin 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 阅读 编辑Santamaria 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 Bromme 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 Mehul 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 Gunther T Dennemarker 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 外部链接 编辑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 取自 https zh wikipedia org w index php title 组织蛋白酶V amp oldid 75102791, 维基百科，wiki，书籍，书籍，图书馆，
