组织蛋白酶F

组织蛋白酶F
已知的结构
PDB	直系同源搜索: PDBe RCSB
PDBID列表
	1M6D
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
基因位置（人类）
染色体	11号染色体
终止	66,568,879 bp
基因位置（小鼠）
染色体	小鼠19号染色体
终止	4,910,946 bp
RNA表达模式
	查阅更多表达数据
基因本体
分子功能	• 肽酶活性; • 半胱氨酸型肽酶活性; • 水解酶活性; • cysteine-type endopeptidase activity;
细胞组分	• 细胞外囊泡; • 溶酶体; • lysosomal lumen; • 外排体; • 细胞外空间; • collagen-containing extracellular matrix;
生物学过程	• proteolysis involved in cellular protein catabolic process; • antigen processing and presentation of exogenous peptide antigen via MHC class II; • 蛋白酶解;
	Sources:Amigo / QuickGO
直系同源
	8722
	56464
	ENSG00000174080
	ENSMUSG00000083282
	Q9UBX1
	Q9R013
	NM_003793
	NM_019861
	NP_003784
	NP_063914
	维基数据
查看/编辑人类	查看/编辑小鼠

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]

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

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

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

^ 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 .
^ 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

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.

外部链接

The MEROPS online database for peptidases and their inhibitors: C01.018^{[失效链接]}

[1] 與组织蛋白酶F相關的疾病；在維基數據上查看/編輯參考.

[refGRCh38Ensembl-2] 2.0 ^2.1 ^2.2 GRCh38: Ensembl release 89: ENSG00000174080 - Ensembl, May 2017

[refGRCm38Ensembl-3] 3.0 ^3.1 ^3.2 GRCm38: Ensembl release 89: ENSMUSG00000083282 - Ensembl, May 2017

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

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

[pmid9822672-6] 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 .

[pmid10318784-7] 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 .

[entrez-8] 8.0 ^8.1 Entrez Gene: CTSF cathepsin F.

[9] 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）.

[10] 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 .

[11] 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）.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

查论编蛋白酶类：半胱氨酸蛋白酶类（EC 3.4.22)
胱天蛋白酶	胱天蛋白酶1 胱天蛋白酶2 胱天蛋白酶3 胱天蛋白酶4 胱天蛋白酶5 胱天蛋白酶6 胱天蛋白酶7 胱天蛋白酶8 胱天蛋白酶9 胱天蛋白酶10 胱天蛋白酶11 胱天蛋白酶12 胱天蛋白酶13 胱天蛋白酶14
来自果实	木瓜蛋白酶无花果蛋白酶（英语：Ficain）凤梨蛋白酶猕猴桃蛋白酶
钙蛋白酶	CAPN1 CAPN2 CAPN3 CAPN5 CAPN6 CAPN7 CAPN8 CAPN9 CAPN10 CAPN11 CAPN12 CAPN13 CAPN14 CAPNS1 CAPNS2
组织蛋白酶	B C F H K L1/L2 O S T W Z
其它	梭菌蛋白酶癌性促凝物质分离酶（英语：Separase） Autophagin Cruzipain 3C样蛋白酶
EC 1.1/2/3/4/5/6/7/8/9/10/11/12/13/14/15/16/17/18/19/20/21/22 · 2.1/2/3/4/5/6/7(2.7.10/11-12)/8/9 · 3.1/2/3/4(3.4.21/22/23/24)/5/6/7/8/9/10/11/12/13 · 4.1/2/3/4/5/6 · 5.1/2/3/4/5/99 · 6.1-3（英语：Template:Ligases CO CS and CN）/4/5-6

查论编酶
活性	活性位点结合位点催化三联体负氧离子洞酶催化混杂（英语：Enzyme promiscuity）催化最适酶（英语：Catalytically perfect enzyme）辅因子辅酶酶促反应
调节	别构调节协同性（英语：Cooperativity）酶抑制剂酶激活剂
分类	EC编号蛋白质超家族蛋白质家族酶列表
动力学	酶动力学伊迪-霍夫斯蒂图（英语：Eadie–Hofstee diagram）哈尼斯-伍尔夫图（英语：Hanes–Woolf plot）双倒数图米氏动力学
类型	EC1 氧化还原酶（列表（英语：List of EC numbers (EC 1)）） EC2 转移酶（列表（英语：List of EC numbers (EC 2)）） EC3 水解酶（列表（英语：List of EC numbers (EC 3)）） EC4 裂合酶（列表（英语：List of EC numbers (EC 4)）） EC5 异构酶（列表（英语：List of EC numbers (EC 5)）） EC6 连接酶（列表（英语：List of EC numbers (EC 6)）） EC7 移位酶（英语：Translocase）（列表（英语：List of EC numbers (EC 7)））