组织蛋白酶F
位於11號人類染色體的基因
组织蛋白酶F（英文：Cathepsin F）是一种在人体中由CTSF基因编码的蛋白质。[6][7][8]
| 组织蛋白酶F | |||||||||||||||||||||||||
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| 识别号 | |||||||||||||||||||||||||
| 别名 | CTSF；, CATSF, CLN13, cathepsin F | ||||||||||||||||||||||||
| 外部ID | OMIM：603539 MGI：1861434 HomoloGene：31194 GeneCards：CTSF | ||||||||||||||||||||||||
| 相关疾病 | |||||||||||||||||||||||||
| neuronal ceroid lipofuscinosis 13、adult neuronal ceroid lipofuscinosis[1] | |||||||||||||||||||||||||
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| 直系同源 | |||||||||||||||||||||||||
| 物种 | 人类 | 小鼠 | |||||||||||||||||||||||
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| 蛋白序列 | |||||||||||||||||||||||||
| 基因位置（UCSC） | Chr 11: 66.56 – 66.57 Mb | Chr 19: 4.91 – 4.91 Mb | |||||||||||||||||||||||
| PubMed查找 | [4] | [5] | |||||||||||||||||||||||
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木瓜样蛋白酶是半胱氨酸蛋白酶家族，代表溶酶体蛋白水解系统的主要成分。通常，组织蛋白酶包含一个信号肽，然后是一个前肽，再然后是一个催化活性成熟区。组织蛋白酶F前体非常长的（251个氨基酸残基）前区包含一个与组织蛋白酶L样酶的前段相似的C端结构域、一个50个残基的柔性连接肽和N端结构域预计采用胱抑素样折叠组织蛋白酶F前区在木瓜蛋白酶家族半胱氨酸蛋白酶中是独一无二的，因为它包含这个额外的N端片段，预计与胱抑素超家族的半胱氨酸蛋白酶抑制剂具有结构相似性。这种胱抑素样结构域包含一些已知对抑制活性很重要的元素。CTSF编码预测的484个氨基酸的蛋白质，其中包含19个残基信号肽。组织蛋白酶F含有五个潜在的N-连接糖基化位点，它可能通过甘露糖6-磷酸受体途径靶向内体/溶酶体区室。组织蛋白酶F基因普遍表达，它定位于染色体11q13，接近编码组织蛋白酶W的基因。[8]
泰国肝吸虫的免疫诊断
编辑组织蛋白酶F可用作测试泰国肝吸虫造成的疾病的替代方法。[9]近年来，泰国肝吸虫的诊断一直通过大便检查来完成，被认为是“金标准”方法。然而，基于粪便的诊断可能是不可靠的[10]，尽管它是一种非侵入性方法。进行的实验表明，通过使用重组DNA技术和组织蛋白酶F半胱氨酸蛋白酶，可以产生更可靠的结果。
组织蛋白酶F在虾夷盘扇贝中的表达
编辑最近的实验表明在虾夷盘扇贝中发现了组织蛋白酶F。[11]在虾夷盘扇贝的各个胚胎发育阶段鉴定组织蛋白酶F基因具有重要意义。组织蛋白酶F基因在先天免疫反应中具有重要作用。虾夷盘扇贝一直因细菌性疾病而遭受高死亡率。组织蛋白酶F的发现可以领导进一步的研究和解决虾夷盘扇贝死亡率问题的方法。
参考文献
编辑- ^ 與组织蛋白酶F相關的疾病；在維基數據上查看/編輯參考.
- ^ 2.0 2.1 2.2 GRCh38: Ensembl release 89: ENSG00000174080 - Ensembl, May 2017
- ^ 3.0 3.1 3.2 GRCm38: Ensembl release 89: ENSMUSG00000083282 - 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.
- ^ Wang B, Shi GP, Yao PM, Li Z, Chapman HA, Bromme D. Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization. J Biol Chem. Dec 1998, 273 (48): 32000–8. PMID 9822672. doi:10.1074/jbc.273.48.32000
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- ^ Santamaria I, Velasco G, Pendas AM, Paz A, Lopez-Otin C. Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain. J Biol Chem. Jun 1999, 274 (20): 13800–9. PMID 10318784. doi:10.1074/jbc.274.20.13800 .
- ^ 8.0 8.1 Entrez Gene: CTSF cathepsin F.
- ^ Teimoori, Salma; Arimatsu, Yuji; Laha, Thewarach; Kaewkes, Sasithorn; Sereerak, Piya; Tangkawattana, Sirikachorn; Brindley, Paul J; Sripa, Banchob. Immunodiagnosis of opisthorchiasis using parasite cathepsin F. Parasitology Research. December 2015, 114 (12): 4571–4578. ISSN 0932-0113. PMC 4917378 . PMID 26344868. doi:10.1007/s00436-015-4703-9 （英语）.
- ^ Korkmaz, Huseyin; Findik, Duygu; Ugurluoglu, Ceyha; Terzi, Yuksel. Reliability of stool antigen tests: investigation of the diagnostic value of a new immunochromatographic Helicobacter pylori approach in dyspeptic patients. Asian Pacific Journal of Cancer Prevention. 2015, 16 (2): 657–660. ISSN 2476-762X. PMID 25684503. doi:10.7314/apjcp.2015.16.2.657 .
- ^ Guo, Haobing; Li, Yangping; Zhang, Meiwei; Li, Ruojiao; Li, Wanru; Lou, Jiarun; Bao, Zhenmin; Wang, Yangfan. Expression of Cathepsin F in response to bacterial challenges in Yesso scallop Patinopecten yessoensis. Fish & Shellfish Immunology. September 2018, 80: 141–147 [2022-10-27]. PMID 29879509. S2CID 47014597. doi:10.1016/j.fsi.2018.06.005. （原始内容存档于2022-08-06） （英语）.
拓展阅读
编辑- Nägler DK, Sulea T, Ménard R. Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen.. Biochem. Biophys. Res. Commun. 1999, 257 (2): 313–8. PMID 10198209. doi:10.1006/bbrc.1999.0461.
- Wex T, Levy B, Wex H, Brömme D. Human cathepsins F and W: A new subgroup of cathepsins.. Biochem. Biophys. Res. Commun. 1999, 259 (2): 401–7. PMID 10362521. doi:10.1006/bbrc.1999.0700.
- Wex T, Wex H, Brömme D. The human cathepsin F gene--a fusion product between an ancestral cathepsin and cystatin gene.. Biol. Chem. 2000, 380 (12): 1439–42. PMID 10661872. S2CID 28469574. doi:10.1515/BC.1999.185.
- Shi GP, Bryant RA, Riese R, et al. Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages.. J. Exp. Med. 2000, 191 (7): 1177–86. PMC 2193169 . PMID 10748235. doi:10.1084/jem.191.7.1177.
- Deussing J, Tisljar K, Papazoglou A, Peters C. Mouse cathepsin F: cDNA cloning, genomic organization and chromosomal assignment of the gene.. Gene. 2000, 251 (2): 165–73. PMID 10876093. doi:10.1016/S0378-1119(00)00196-7.
- 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 .
- Oörni K, Sneck M, Brömme D, et al. Cysteine protease cathepsin F is expressed in human atherosclerotic lesions, is secreted by cultured macrophages, and modifies low density lipoprotein particles in vitro.. J. Biol. Chem. 2004, 279 (33): 34776–84. PMID 15184381. doi:10.1074/jbc.M310814200 .
- 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.
- Vazquez-Ortiz G, Pina-Sanchez P, Vazquez K, et al. Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer.. BMC Cancer. 2006, 5 (1): 68. PMC 1175083 . PMID 15989693. doi:10.1186/1471-2407-5-68.
- Kaakinen R, Lindstedt KA, Sneck M, et al. Angiotensin II increases expression and secretion of cathepsin F in cultured human monocyte-derived macrophages: an angiotensin II type 2 receptor-mediated effect.. Atherosclerosis. 2007, 192 (2): 323–7. PMID 16963053. doi:10.1016/j.atherosclerosis.2006.08.001.
