组织蛋白酶S：修订间差异

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虽然早已认识到在[[抗原呈遞|抗原呈递]]中的作用<ref>{{cite journal |vauthors=Liu W, Spero DM |date=July 2004 |title=Cysteine protease cathepsin S as a key step in antigen presentation |journal=Drug News & Perspectives |volume=17 |issue=6 |pages=357–363 |doi=10.1358/dnp.2004.17.6.829027 |pmid=15334187}}</ref><ref>{{cite journal |display-authors=6 |vauthors=Baranov MV, Bianchi F, Schirmacher A, van Aart MA, Maassen S, Muntjewerff EM, Dingjan I, Ter Beest M, Verdoes M, Keyser SG, Bertozzi CR, Diederichsen U, van den Bogaart G |date=January 2019 |title=The Phosphoinositide Kinase PIKfyve Promotes Cathepsin-S-Mediated Major Histocompatibility Complex Class II Antigen Presentation |journal=iScience |volume=11 |pages=160–177 |bibcode=2019iSci...11..160B |doi=10.1016/j.isci.2018.12.015 |pmc=6319320 |pmid=30612035}}</ref>，但现在已经了解组织蛋白酶S在瘙痒和疼痛或伤害感受中起作用。<ref>{{cite journal |display-authors=6 |vauthors=Tu NH, Inoue K, Chen E, Anderson BM, Sawicki CM, Scheff NN, Tran HD, Kim DH, Alemu RG, Yang L, Dolan JC, Liu CZ, Janal MN, Latorre R, Jensen DD, Bunnett NW, Edgington-Mitchell LE, Schmidt BL |date=September 2021 |title=Cathepsin S Evokes PAR<sub>2</sub>-Dependent Pain in Oral Squamous Cell Carcinoma Patients and Preclinical Mouse Models |journal=Cancers |volume=13 |issue=18 |pages=4697 |doi=10.3390/cancers13184697 |pmc=8466361 |pmid=34572924 |doi-access=free}}</ref> 伤害性活性是由组织蛋白酶S通过激活[[G蛋白偶联受体]]家族的{{link-en|蛋白酶激活受体|Protease-activated receptor}}2和4成员作为[[细胞信号传送|信号分子]]而产生的。<ref name="ReferenceA">{{cite journal |vauthors=Reddy VB, Sun S, Azimi E, Elmariah SB, Dong X, Lerner EA |date=July 2015 |title=Redefining the concept of protease-activated receptors: cathepsin S evokes itch via activation of Mrgprs |journal=Nature Communications |volume=6 |pages=7864 |bibcode=2015NatCo...6.7864R |doi=10.1038/ncomms8864 |pmc=4520244 |pmid=26216096}}</ref>
虽然早已认识到在[[抗原呈遞|抗原呈递]]中的作用<ref>{{cite journal |vauthors=Liu W, Spero DM |date=July 2004 |title=Cysteine protease cathepsin S as a key step in antigen presentation |journal=Drug News & Perspectives |volume=17 |issue=6 |pages=357–363 |doi=10.1358/dnp.2004.17.6.829027 |pmid=15334187}}</ref><ref>{{cite journal |display-authors=6 |vauthors=Baranov MV, Bianchi F, Schirmacher A, van Aart MA, Maassen S, Muntjewerff EM, Dingjan I, Ter Beest M, Verdoes M, Keyser SG, Bertozzi CR, Diederichsen U, van den Bogaart G |date=January 2019 |title=The Phosphoinositide Kinase PIKfyve Promotes Cathepsin-S-Mediated Major Histocompatibility Complex Class II Antigen Presentation |journal=iScience |volume=11 |pages=160–177 |bibcode=2019iSci...11..160B |doi=10.1016/j.isci.2018.12.015 |pmc=6319320 |pmid=30612035}}</ref>，但现在已经了解组织蛋白酶S在瘙痒和疼痛或伤害感受中起作用。<ref>{{cite journal |display-authors=6 |vauthors=Tu NH, Inoue K, Chen E, Anderson BM, Sawicki CM, Scheff NN, Tran HD, Kim DH, Alemu RG, Yang L, Dolan JC, Liu CZ, Janal MN, Latorre R, Jensen DD, Bunnett NW, Edgington-Mitchell LE, Schmidt BL |date=September 2021 |title=Cathepsin S Evokes PAR<sub>2</sub>-Dependent Pain in Oral Squamous Cell Carcinoma Patients and Preclinical Mouse Models |journal=Cancers |volume=13 |issue=18 |pages=4697 |doi=10.3390/cancers13184697 |pmc=8466361 |pmid=34572924 |doi-access=free}}</ref> 伤害性活性是由组织蛋白酶S通过激活[[G蛋白偶联受体]]家族的{{link-en|蛋白酶激活受体|Protease-activated receptor}}2和4成员作为[[细胞信号传送|信号分子]]而产生的。<ref name="ReferenceA">{{cite journal |vauthors=Reddy VB, Sun S, Azimi E, Elmariah SB, Dong X, Lerner EA |date=July 2015 |title=Redefining the concept of protease-activated receptors: cathepsin S evokes itch via activation of Mrgprs |journal=Nature Communications |volume=6 |pages=7864 |bibcode=2015NatCo...6.7864R |doi=10.1038/ncomms8864 |pmc=4520244 |pmid=26216096}}</ref>


组织蛋白酶S由抗原呈递细胞表达，包括[[巨噬细胞]]、[[B细胞]]、[[樹突狀細胞|树突状细胞]]和[[小胶质细胞]]。<ref>{{cite journal |vauthors=Reich M, Zou F, Sieńczyk M, Oleksyszyn J, Boehm BO, Burster T |date=2011 |title=Invariant chain processing is independent of cathepsin variation between primary human B cells/dendritic cells and B-lymphoblastoid cells |journal=Cellular Immunology |volume=269 |issue=2 |pages=96–103 |doi=10.1016/j.cellimm.2011.03.012 |pmid=21543057}}</ref><ref>{{cite journal |display-authors=6 |vauthors=Rupanagudi KV, Kulkarni OP, Lichtnekert J, Darisipudi MN, Mulay SR, Schott B, Gruner S, Haap W, Hartmann G, Anders HJ |date=February 2015 |title=Cathepsin S inhibition suppresses systemic lupus erythematosus and lupus nephritis because cathepsin S is essential for MHC class II-mediated CD4 T cell and B cell priming |url=https://epub.ub.uni-muenchen.de/37251/1/452.pdf |journal=Annals of the Rheumatic Diseases |volume=74 |issue=2 |pages=452–463 |doi=10.1136/annrheumdis-2013-203717 |pmid=24300027 |s2cid=22126353}}</ref>组织蛋白酶S由一些[[上皮組織|上皮]]细胞表达。<ref>{{cite journal |vauthors=da Costa AC, Santa-Cruz F, Mattos LA, Rêgo Aquino MA, Martins CR, Bandeira Ferraz ÁA, Figueiredo JL |date=February 2020 |title=Cathepsin S as a target in gastric cancer |journal=Molecular and Clinical Oncology |volume=12 |issue=2 |pages=99–103 |doi=10.3892/mco.2019.1958 |pmc=6951222 |pmid=31929878}}</ref>在用[[γ-干扰素]]刺激后，其在人[[角质形成细胞]]中的表达显着增加，并且由于[[促炎性细胞因子]]的刺激，其在[[銀屑病|银屑病]]角质形成细胞中的表达升高。<ref>{{cite journal |display-authors=6 |vauthors=Schönefuss A, Wendt W, Schattling B, Schulten R, Hoffmann K, Stuecker M, Tigges C, Lübbert H, Stichel C |date=August 2010 |title=Upregulation of cathepsin S in psoriatic keratinocytes |journal=Experimental Dermatology |volume=19 |issue=8 |pages=e80–e88 |doi=10.1111/j.1600-0625.2009.00990.x |pmid=19849712 |s2cid=31731844}}</ref>相反，{{link-en|皮质胸腺上皮细胞|Cortical thymic epithelial cells}}不表达组织蛋白酶S。<ref>{{cite journal |display-authors=6 |vauthors=Kiuchi S, Tomaru U, Ishizu A, Imagawa M, Kiuchi T, Iwasaki S, Suzuki A, Otsuka N, Deguchi T, Shimizu T, Marukawa K, Matsuno Y, Kasahara M |date=February 2017 |title=Expression of cathepsins V and S in thymic epithelial tumors |journal=Human Pathology |volume=60 |pages=66–74 |doi=10.1016/j.humpath.2016.09.027 |pmid=27771373}}</ref><ref>{{cite journal |vauthors=Beers C, Burich A, Kleijmeer MJ, Griffith JM, Wong P, Rudensky AY |date=February 2005 |title=Cathepsin S controls MHC class II-mediated antigen presentation by epithelial cells in vivo |journal=Journal of Immunology |volume=174 |issue=3 |pages=1205–1212 |doi=10.4049/jimmunol.174.3.1205 |pmid=15661874 |s2cid=30821915}}</ref>


虽然许多溶酶体蛋白酶的最适pH值是[[酸|酸性]]的<ref>{{cite journal |vauthors=Wilkinson RD, Williams R, Scott CJ, Burden RE |date=August 2015 |title=Cathepsin S: therapeutic, diagnostic, and prognostic potential |journal=Biological Chemistry |volume=396 |issue=8 |pages=867–882 |doi=10.1515/hsz-2015-0114 |pmid=25872877 |s2cid=17582321}}</ref><ref>{{cite journal |vauthors=Liuzzo JP, Petanceska SS, Devi LA |date=May 1999 |title=Neurotrophic factors regulate cathepsin S in macrophages and microglia: A role in the degradation of myelin basic protein and amyloid beta peptide |journal=Molecular Medicine |volume=5 |issue=5 |pages=334–343 |doi=10.1007/BF03402069 |pmc=2230424 |pmid=10390549}}</ref><ref>{{cite journal |vauthors=Sena BF, Figueiredo JL, Aikawa E |date=2017 |title=Cathepsin S As an Inhibitor of Cardiovascular Inflammation and Calcification in Chronic Kidney Disease |journal=Frontiers in Cardiovascular Medicine |volume=4 |pages=88 |doi=10.3389/fcvm.2017.00088 |pmc=5770806 |pmid=29379789 |doi-access=free}}</ref>，但组织蛋白酶S是一个例外。该酶在中性pH值下保持[[催化|催化活性]]，并在pH值5.0和7.5之间具有最佳pH值。<ref>{{cite journal |display-authors=6 |vauthors=Kim NY, Ahn SJ, Lee AR, Seo JS, Kim MS, Kim JK, Chung JK, Lee HH |date=November 2010 |title=Cloning, expression analysis and enzymatic characterization of cathepsin S from olive flounder (Paralichthys olivaceus) |journal=Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology |volume=157 |issue=3 |pages=238–247 |doi=10.1016/j.cbpb.2010.06.008 |pmid=20601061}}</ref><ref>{{cite journal |display-authors=6 |vauthors=Brömme D, Bonneau PR, Lachance P, Wiederanders B, Kirschke H, Peters C, Thomas DY, Storer AC, Vernet T |date=March 1993 |title=Functional expression of human cathepsin S in Saccharomyces cerevisiae. Purification and characterization of the recombinant enzyme |journal=The Journal of Biological Chemistry |volume=268 |issue=7 |pages=4832–4838 |doi=10.1016/S0021-9258(18)53472-4 |pmid=8444861 |doi-access=free}}</ref>由于稳定性问题，许多溶酶体蛋白酶被困在溶酶体内。相反，组织蛋白酶S可以保持稳定并在溶酶体外具有生理作用。<ref>{{cite journal |vauthors=Karimkhanloo H, Keenan SN, Sun EW, Wattchow DA, Keating DJ, Montgomery MK, Watt MJ |date=February 2021 |title=Circulating cathepsin S improves glycaemic control in mice |journal=The Journal of Endocrinology |volume=248 |issue=2 |pages=167–179 |doi=10.1530/JOE-20-0408 |pmid=33289685 |s2cid=227951644}}</ref><ref>{{cite journal |display-authors=6 |vauthors=Bibli SI, Hu J, Sigala F, Wittig I, Heidler J, Zukunft S, Tsilimigras DI, Randriamboavonjy V, Wittig J, Kojonazarov B, Schürmann C, Siragusa M, Siuda D, Luck B, Abdel Malik R, Filis KA, Zografos G, Chen C, Wang DW, Pfeilschifter J, Brandes RP, Szabo C, Papapetropoulos A, Fleming I |date=January 2019 |title=Cystathionine γ Lyase Sulfhydrates the RNA Binding Protein Human Antigen R to Preserve Endothelial Cell Function and Delay Atherogenesis |journal=Circulation |volume=139 |issue=1 |pages=101–114 |doi=10.1161/CIRCULATIONAHA.118.034757 |pmid=29970364 |s2cid=49652298}}</ref>[[免疫細胞|免疫细胞]]，包括巨噬细胞和小胶质细胞，分泌组织蛋白酶S以响应[[炎症]]介质，包括[[脂多糖]]<ref>{{cite journal |display-authors=6 |vauthors=Janga H, Cassidy L, Wang F, Spengler D, Oestern-Fitschen S, Krause MF, Seekamp A, Tholey A, Fuchs S |date=February 2018 |title=Site-specific and endothelial-mediated dysfunction of the alveolar-capillary barrier in response to lipopolysaccharides |journal=Journal of Cellular and Molecular Medicine |volume=22 |issue=2 |pages=982–998 |doi=10.1111/jcmm.13421 |pmc=5783864 |pmid=29210175}}</ref>、促炎性细胞因子<ref>{{cite journal |display-authors=6 |vauthors=Ainscough JS, Macleod T, McGonagle D, Brakefield R, Baron JM, Alase A, Wittmann M, Stacey M |date=March 2017 |title=Cathepsin S is the major activator of the psoriasis-associated proinflammatory cytokine IL-36γ |journal=Proceedings of the National Academy of Sciences of the United States of America |volume=114 |issue=13 |pages=E2748–E2757 |bibcode=2017PNAS..114E2748A |doi=10.1073/pnas.1620954114 |pmc=5380102 |pmid=28289191 |doi-access=free}}</ref>和[[中性粒细胞]]。.<ref>{{cite journal |vauthors=Wang H, Jiang H, Cheng XW |date=2022 |title=Cathepsin S are involved in human carotid atherosclerotic disease progression, mainly by mediating phagosomes: bioinformatics and ''in vivo'' and ''vitro'' experiments |journal=PeerJ |volume=10 |pages=e12846 |doi=10.7717/peerj.12846 |pmc=8833225 |pmid=35186462}}</ref>在体外，组织蛋白酶S在 3M[[尿素]]存在下保留一些酶活性。<ref>{{cite journal |display-authors=6 |vauthors=Flynn CM, Garbers Y, Düsterhöft S, Wichert R, Lokau J, Lehmann CH, Dudziak D, Schröder B, Becker-Pauly C, Rose-John S, Aparicio-Siegmund S, Garbers C |date=December 2020 |title=Cathepsin S provokes interleukin-6 (IL-6) trans-signaling through cleavage of the IL-6 receptor in vitro |journal=Scientific Reports |volume=10 |issue=1 |pages=21612 |bibcode=2020NatSR..1021612F |doi=10.1038/s41598-020-77884-4 |pmc=7730449 |pmid=33303781}}</ref>组织蛋白酶S作为[[酶原]]产生并通过加工被激活。<ref>{{cite journal |vauthors=Wiederanders B |date=2000 |title=The function of propeptide domains of cysteine proteinases |journal=Advances in Experimental Medicine and Biology |volume=477 |pages=261–270 |doi=10.1007/0-306-46826-3_28 |isbn=0-306-46383-0 |pmid=10849753}}</ref>


组织蛋白酶S的活性受到其内源性抑制剂[[胱抑素C]]的严格调节，胱抑素C在抗原呈递中也有作用。<ref>{{cite journal |vauthors=Paraoan L, Gray D, Hiscott P, Garcia-Finana M, Lane B, Damato B, Grierson I |date=January 2009 |title=Cathepsin S and its inhibitor cystatin C: imbalance in uveal melanoma |journal=Frontiers in Bioscience |volume=14 |issue=7 |pages=2504–2513 |doi=10.2741/3393 |pmid=19273215}}</ref><ref>{{cite journal |display-authors=6 |vauthors=Zhang W, Zi M, Sun L, Wang F, Chen S, Zhao Y, Liang S, Hu J, Liu S, Liu L, Zhan Y, Lew AM, Xu Y |date=November 2019 |title=Cystatin C regulates major histocompatibility complex-II-peptide presentation and extracellular signal-regulated kinase-dependent polarizing cytokine production by bone marrow-derived dendritic cells |journal=Immunology and Cell Biology |volume=97 |issue=10 |pages=916–930 |doi=10.1111/imcb.12290 |pmid=31513306 |s2cid=213168319}}</ref>与胱抑素C相比，{{link-en|胱抑素A|Cystatin A}}和{{link-en|胱抑素B|Cystatin B}}的活性较低。<ref>{{cite journal |vauthors=Bangsuwan P, Hirunwidchayarat W, Jirawechwongsakul P, Talungchit S, Taebunpakul P |date=September 2021 |title=Expression of Cathepsin B and Cystatin A in Oral Lichen Planus |journal=Journal of International Society of Preventive & Community Dentistry |volume=11 |issue=5 |pages=566–573 |doi=10.4103/jispcd.JISPCD_97_21 |doi-broken-date=2022-10-07 |pmc=8533036 |pmid=34760802}}</ref>

组织蛋白酶S的活性切割位点 -(-Val-Val-Arg-)- 应该从每侧至少有两个[[氨基酸]]围绕它。<ref>{{cite journal |display-authors=6 |vauthors=Fu Q, Zhao S, Yang N, Tian M, Cai X, Zhang L, Hu J, Cao M, Xue T, Li C |date=July 2020 |title=Genome-wide identification, expression signature and immune functional analysis of two cathepsin S (CTSS) genes in turbot (Scophthalmus maximus L.) |journal=Fish & Shellfish Immunology |volume=102 |pages=243–256 |doi=10.1016/j.fsi.2020.04.028 |pmid=32315741 |s2cid=216074706}}</ref>

虽然溶酶体蛋白酶最终降解溶酶体中的蛋白质，但组织蛋白酶S具有其独特的生理作用。<ref>{{cite journal |display-authors=6 |vauthors=Sage J, Mallèvre F, Barbarin-Costes F, Samsonov SA, Gehrcke JP, Pisabarro MT, Perrier E, Schnebert S, Roget A, Livache T, Nizard C, Lalmanach G, Lecaille F |date=September 2013 |title=Binding of chondroitin 4-sulfate to cathepsin S regulates its enzymatic activity |journal=Biochemistry |volume=52 |issue=37 |pages=6487–6498 |doi=10.1021/bi400925g |pmid=23968158}}</ref>
== 参见 ==
== 参见 ==


2022年11月2日 (三) 15:15的版本

组织蛋白酶S
已知的結構
PDB直系同源搜索: PDBe RCSB
識別號
别名CTSS；, cathepsin S
外部IDOMIM：116845 MGI：107341 HomoloGene：20867 GeneCards：CTSS
為以下藥物的標靶
odanacatib[1]
基因位置（人类）
1號染色體
染色体1號染色體[2]
1號染色體
组织蛋白酶S的基因位置
组织蛋白酶S的基因位置
基因座1q21.3起始150,730,079 bp[2]
终止150,765,957 bp[2]
RNA表达模式


查阅更多表达数据
直系同源
物種人類小鼠
Entrez

1520

13040

Ensembl

ENSG00000163131

ENSMUSG00000038642

UniProt

P25774

O70370

mRNA​序列

NM_004079
​NM_001199739

NM_001267695
​NM_021281

蛋白序列

NP_001186668
​NP_004070

NP_001254624
​NP_067256

基因位置​（UCSC）Chr 1: 150.73 – 150.77 MbChr 3: 95.43 – 95.46 Mb
PubMed​查找[4][5]
維基數據
檢視/編輯人類檢視/編輯小鼠

组织蛋白酶S（学名：Cathepsin S）是人类体内由CTSS基因编码的蛋白质[6]该基因存在利用替代多腺苷酸化信号的转录变体。[6]

组织蛋白酶S是木瓜样蛋白酶（英语：Papain-like protease）肽酶C1家族的成员[7]，这是一种溶酶体半胱氨酸蛋白酶，可参与将抗原蛋白降解为肽以呈递给MHC II类分子。[8][9]组织蛋白酶S可以在肺泡巨噬细胞的广泛pH范围内作为弹性蛋白酶发挥作用。[10][11]

作用

虽然早已认识到在抗原呈递中的作用[12][13]，但现在已经了解组织蛋白酶S在瘙痒和疼痛或伤害感受中起作用。[14] 伤害性活性是由组织蛋白酶S通过激活G蛋白偶联受体家族的蛋白酶激活受体（英语：Protease-activated receptor）2和4成员作为信号分子而产生的。[15]

组织蛋白酶S由抗原呈递细胞表达，包括巨噬细胞、B细胞、树突状细胞和小胶质细胞。[16][17]组织蛋白酶S由一些上皮细胞表达。[18]在用γ-干扰素刺激后，其在人角质形成细胞中的表达显着增加，并且由于促炎性细胞因子的刺激，其在银屑病角质形成细胞中的表达升高。[19]相反，皮质胸腺上皮细胞（英语：Cortical thymic epithelial cells）不表达组织蛋白酶S。[20][21]

虽然许多溶酶体蛋白酶的最适pH值是酸性的[22][23][24]，但组织蛋白酶S是一个例外。该酶在中性pH值下保持催化活性，并在pH值5.0和7.5之间具有最佳pH值。[25][26]由于稳定性问题，许多溶酶体蛋白酶被困在溶酶体内。相反，组织蛋白酶S可以保持稳定并在溶酶体外具有生理作用。[27][28]免疫细胞，包括巨噬细胞和小胶质细胞，分泌组织蛋白酶S以响应炎症介质，包括脂多糖[29]、促炎性细胞因子[30]和中性粒细胞。.[31]在体外，组织蛋白酶S在 3M尿素存在下保留一些酶活性。[32]组织蛋白酶S作为酶原产生并通过加工被激活。[33]

组织蛋白酶S的活性受到其内源性抑制剂胱抑素C的严格调节，胱抑素C在抗原呈递中也有作用。[34][35]与胱抑素C相比，胱抑素A和胱抑素B的活性较低。[36]

组织蛋白酶S的活性切割位点 -(-Val-Val-Arg-)- 应该从每侧至少有两个氨基酸围绕它。[37]

虽然溶酶体蛋白酶最终降解溶酶体中的蛋白质，但组织蛋白酶S具有其独特的生理作用。[38]

参见

参考文献

  1. ^ 對Cathepsin S起作用的藥物；在維基數據上查看/編輯參考. 
  2. ^ 2.0 2.1 2.2 GRCh38: Ensembl release 89: ENSG00000163131 - Ensembl, May 2017
  3. ^ 3.0 3.1 3.2 GRCm38: Ensembl release 89: ENSMUSG00000038642 - 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. 
  6. ^ 6.0 6.1 Entrez Gene: CTSS cathepsin S. 
  7. ^ Wang GH, He SW, Du X, Xie B, Gu QQ, Zhang M, Hu YH. Characterization, expression, enzymatic activity, and functional identification of cathepsin S from black rockfish Sebastes schlegelii. Fish & Shellfish Immunology. October 2019, 93: 623–630. PMID 31400512. S2CID 199527780. doi:10.1016/j.fsi.2019.08.012. 
  8. ^ Cheng XW, Zhang J, Song H, Yang G, Qin XZ, Guan LK, et al. [Association between lysosomal cysteine protease cathepsin's activation and left ventricular function and remodeling in hypertensive heart failure rats]. Zhonghua Xin Xue Guan Bing Za Zhi. January 2008, 36 (1): 51–56. PMID 19099930. 
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外部链接

胱天蛋白酶
来自果实
钙蛋白酶
组织蛋白酶
其它
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
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动力学
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取自“https://zh.wikipedia.org/w/index.php?title=组织蛋白酶S&oldid=74367910”