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维基百科

组织蛋白酶L1

行進 29, 2023

组织蛋白酶L1（英语：Cathepsin L1）是人类体内由CTSL1基因编码的蛋白质。[3][4][5]该蛋白质是木瓜样蛋白酶（英语：Papain-like protease），是一种溶酶体半胱氨酸蛋白酶，在细胞内蛋白质分解代谢中起着主要的作用。[6][7][8][9]

组织蛋白酶L1
已知的結構
PDB人类UniProt搜索: PDBe RCSB
識別號
别名CTSL；, CATL, CTSL1, MEP, cathepsin L
外部IDOMIM：116880 HomoloGene：129366 GeneCards：CTSL
基因位置（人类）
染色体9號染色體[1]
基因座9q21.33起始87,724,051 bp[1]
终止87,731,469 bp[1]
RNA表达模式
查阅更多表达数据
直系同源
物種人類小鼠
Entrez

1514

无数据

Ensembl

ENSG00000135047

无数据

UniProt

P07711
Q9HBQ7

无数据

mRNA​序列

无数据

蛋白序列

无数据

基因位置​（UCSC）Chr 9: 87.72 – 87.73 Mb无数据
PubMed​查找[2]无数据
維基數據
檢視/編輯人類

作用

组织蛋白酶L1是肽酶C1（组织蛋白酶）MEROPS家族的成员。组织蛋白酶L1在包括正常溶酶体介导的蛋白质周转、抗原、前蛋白加工以及细胞凋亡在内的多种过程中发挥重要的作用。[10]其底物包括胶原蛋白、弹性蛋白和SERPINA1（英语：Alpha-1 antitrypsin），这是中性粒细胞弹性蛋白酶（英语：Neutrophil elastase）活性的主要控制元素。组织蛋白酶L1与多种病理过程有关，包括肌病（英语：Myopathy）、冠状动脉疾病中的肌原纤维（英语：Myofibril）坏死以及肾小管对蛋白尿的反应。它是由二硫键连接的重链和轻链组成的二聚体，均由单一蛋白质前体产生。已发现该基因至少有两种编码相同蛋白质的转录变体。[5]

病毒进入

病毒进入细胞需要2型新冠病毒S2刺突蛋白的裂解。此过程可以通过位于细胞膜上的蛋白酶——跨膜丝氨酸蛋白酶2或内溶酶体中的组织蛋白酶（主要是组织蛋白酶L1）来完成。[11]羟氯喹可以抑制内溶酶体中组织蛋白酶L1的作用，但由于与跨膜丝氨酸蛋白酶2裂解相比，组织蛋白酶L1的裂解较小，因此羟氯喹对2型新冠病毒感染的抑制作用很小。[11]

炎症

虽然组织蛋白酶L1通常被表征为溶酶体蛋白酶，但它可以被分泌，导致病理性炎症。[12]组织蛋白酶L1和其他木瓜样蛋白酶在引起病理性炎症时往往由巨噬细胞和其他侵入组织的免疫细胞分泌而出。[13]

交互作用

组织蛋白酶L1已被证明与胱抑素A有相互作用。[14][15]

分布

组织蛋白酶L1已在许多生物体中发现，包括鱼类[16]、鸟类、哺乳动物和海绵。[17]

参见

参考文献

  1. ^ 1.0 1.1 1.2 GRCh38: Ensembl release 89: ENSG00000135047 - Ensembl, May 2017
  2. ^ Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine. 
  3. ^ Chauhan SS, Popescu NC, Ray D, Fleischmann R, Gottesman MM, Troen BR. Cloning, genomic organization, and chromosomal localization of human cathepsin L. J Biol Chem. Feb 1993, 268 (2): 1039–45. PMID 8419312. doi:10.1016/S0021-9258(18)54038-2  . 
  4. ^ Joseph LJ, Chang LC, Stamenkovich D, Sukhatme VP. Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts. J Clin Invest. Jun 1988, 81 (5): 1621–9. PMC 442598  . PMID 2835398. doi:10.1172/JCI113497. 
  5. ^ 5.0 5.1 Entrez Gene: CTSL1 cathepsin L1. 
  6. ^ Barrett AJ, Kirschke H. Cathepsin B, Cathepsin H, and cathepsin L. Methods in Enzymology. 1981,. 80 Pt C: 535–561. PMID 7043200. doi:10.1016/s0076-6879(81)80043-2. 
  7. ^ Barrett AJ, Buttle DJ, Mason RW. Lysosomal cysteine proteinases. ISI Atlas of Science. Biochemistry. 1988, 1: 256–260. 
  8. ^ Joseph LJ, Chang LC, Stamenkovich D, Sukhatme VP. Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts. The Journal of Clinical Investigation. May 1988, 81 (5): 1621–1629. PMC 442598  . PMID 2835398. doi:10.1172/JCI113497. 
  9. ^ Kirschke H, Wikstrom P, Shaw E. Active center differences between cathepsins L and B: the S1 binding region. FEBS Letters. February 1988, 228 (1): 128–130. PMID 3342870. doi:10.1016/0014-5793(88)80600-8  . 
  10. ^ Dickinson DP. Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and Disease. Critical Reviews in Oral Biology and Medicine. 2002, 13 (3): 238–75. PMID 12090464. doi:10.1177/154411130201300304. 
  11. ^ 11.0 11.1 Jackson CB, Farzan M, Chen B, Choe H. Mechanisms of SARS-CoV-2 entry into cells. Nature Reviews. Molecular Cell Biology. January 2022, 23 (1): 3–20. PMC 8491763  . PMID 34611326. doi:10.1038/s41580-021-00418-x. 
  12. ^ Gomes CP, Fernandes DE, Casimiro F, da Mata GF, Passos MT, Varela P, et al. Cathepsin L in COVID-19: From Pharmacological Evidences to Genetics. Frontiers in Cellular and Infection Microbiology. 2022, 10: 589505. PMC 7753008  . PMID 33364201. doi:10.3389/fcimb.2020.589505  . 
  13. ^ Berdowska I, Matusiewicz M. Cathepsin L, transmembrane peptidase/serine subfamily member 2/4, and other host proteases in COVID-19 pathogenesis - with impact on gastrointestinal tract. World Journal of Gastroenterology. October 2021, 27 (39): 6590–6600. PMC 8554394  . PMID 34754154. doi:10.3748/wjg.v27.i39.6590. 
  14. ^ Majerle, Andreja; Jerala Roman. Protein inhibitors form complexes with procathepsin L and augment cleavage of the propeptide. Arch. Biochem. Biophys. Sep 2003, 417 (1): 53–8. ISSN 0003-9861. PMID 12921779. doi:10.1016/S0003-9861(03)00319-9. 
  15. ^ Estrada, S; Nycander M; Hill N J; Craven C J; Waltho J P; Björk I. The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin L. Biochemistry. May 1998, 37 (20): 7551–60. ISSN 0006-2960. PMID 9585570. doi:10.1021/bi980026r. 
  16. ^ Venkatesh K, Prasanth B, Rajesh P, Annie JG, Mukesh P, Jesu A. A murrel cysteine protease, cathepsin L: bioinformatics characterization, gene expression and proteolytic activity. Biologia. 2014, 39 (3): 395–406. doi:10.2478/s11756-013-0326-8  . 
  17. ^ Sevenich L, Pennacchio LA, Peters C, Reinheckel T. Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice. Biological Chemistry. July 2006, 387 (7): 885–91 [2022-10-31]. PMID 16913838. S2CID 27739485. doi:10.1515/BC.2006.112. （原始内容于2022-10-31）. 

拓展阅读

  • Smith CG, Smith MT, Besch NF, et al. Effect of delta 9-tetrahydrocannabinol (THC) on female reproductive function.. Advances in the Biosciences. 1980, 22–23: 449–67. ISBN 9780080237596. PMID 116880. doi:10.1016/b978-0-08-023759-6.50040-8. 
  • Goretzki L, Schmitt M, Mann K, et al. Effective activation of the proenzyme form of the urokinase-type plasminogen activator (pro-uPA) by the cysteine protease cathepsin L.. FEBS Lett. 1992, 297 (1–2): 112–8. PMID 1551416. S2CID 45421148. doi:10.1016/0014-5793(92)80339-I. 
  • Dunn AD, Crutchfield HE, Dunn JT. Thyroglobulin processing by thyroidal proteases. Major sites of cleavage by cathepsins B, D, and L.. J. Biol. Chem. 1991, 266 (30): 20198–204. PMID 1939080. doi:10.1016/S0021-9258(18)54909-7  . 
  • Stearns NA, Dong JM, Pan JX, et al. Comparison of cathepsin L synthesized by normal and transformed cells at the gene, message, protein, and oligosaccharide levels.. Arch. Biochem. Biophys. 1991, 283 (2): 447–57. PMID 2275556. doi:10.1016/0003-9861(90)90666-M. 
  • Ritonja A, Popović T, Kotnik M, et al. Amino acid sequences of the human kidney cathepsins H and L.. FEBS Lett. 1988, 228 (2): 341–5. PMID 3342889. S2CID 45768546. doi:10.1016/0014-5793(88)80028-0  . 
  • Gal S, Gottesman MM. Isolation and sequence of a cDNA for human pro-(cathepsin L).. Biochem. J. 1988, 253 (1): 303–6. PMC 1149292  . PMID 3421948. doi:10.1042/bj2530303. 
  • Johnson DA, Barrett AJ, Mason RW. Cathepsin L inactivates alpha 1-proteinase inhibitor by cleavage in the reactive site region.. J. Biol. Chem. 1986, 261 (31): 14748–51. PMID 3490478. doi:10.1016/S0021-9258(18)66935-2  . 
  • Mason RW, Walker JE, Northrop FD. The N-terminal amino acid sequences of the heavy and light chains of human cathepsin L. Relationship to a cDNA clone for a major cysteine proteinase from a mouse macrophage cell line.. Biochem. J. 1987, 240 (2): 373–7. PMC 1147428  . PMID 3545185. doi:10.1042/bj2400373. 
  • Joseph L, Lapid S, Sukhatme V. The major ras induced protein in NIH3T3 cells is cathepsin L.. Nucleic Acids Res. 1987, 15 (7): 3186. PMC 340927  . PMID 3550705. doi:10.1093/nar/15.7.3186. 
  • Kärgel HJ, Dettmer R, Etzold G, et al. Action of rat liver cathepsin L on glucagon.. Acta Biol. Med. Ger. 1982, 40 (9): 1139–43. PMID 7340337. 
  • Bevec T, Stoka V, Pungercic G, et al. Major histocompatibility complex class II-associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L.. J. Exp. Med. 1996, 183 (4): 1331–8. PMC 2192513  . PMID 8666891. doi:10.1084/jem.183.4.1331. 
  • Coulombe R, Grochulski P, Sivaraman J, et al. Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment.. EMBO J. 1996, 15 (20): 5492–503. PMC 452294  . PMID 8896443. doi:10.1002/j.1460-2075.1996.tb00934.x. 
  • Baumgrass R, Williamson MK, Price PA. Identification of peptide fragments generated by digestion of bovine and human osteocalcin with the lysosomal proteinases cathepsin B, D, L, H, and S.. J. Bone Miner. Res. 1997, 12 (3): 447–55. PMID 9076588. S2CID 20815411. doi:10.1359/jbmr.1997.12.3.447  . 
  • Fujishima A, Imai Y, Nomura T, et al. The crystal structure of human cathepsin L complexed with E-64.. FEBS Lett. 1997, 407 (1): 47–50. PMID 9141479. S2CID 46288832. doi:10.1016/S0014-5793(97)00216-0  . 
  • Ménard R, Carmona E, Takebe S, et al. Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro.. J. Biol. Chem. 1998, 273 (8): 4478–84. PMID 9468501. doi:10.1074/jbc.273.8.4478  . 
  • Schick C, Pemberton PA, Shi GP, et al. Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: a kinetic analysis.. Biochemistry. 1998, 37 (15): 5258–66. PMID 9548757. doi:10.1021/bi972521d. 
  • Estrada S, Nycander M, Hill NJ, et al. The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin L.. Biochemistry. 1998, 37 (20): 7551–60. PMID 9585570. doi:10.1021/bi980026r. 
  • Halfon S, Ford J, Foster J, et al. Leukocystatin, a new Class II cystatin expressed selectively by hematopoietic cells.. J. Biol. Chem. 1998, 273 (26): 16400–8. PMID 9632704. doi:10.1074/jbc.273.26.16400  . 

外部链接

行進 29, 2023
组织蛋白酶l1, 英语, cathepsin, 是人类体内由ctsl1基因编码的蛋白质, 该蛋白质是木瓜样蛋白酶, 英语, papain, like, protease, 是一种溶酶体半胱氨酸蛋白酶, 在细胞内蛋白质分解代谢中起着主要的作用, 已知的結構pdb人类uniprot搜索, pdbe, rcsbpdbid列表1cjl, 1cs8, 1icf, 1mhw, 2nqd, 2vhs, 2xu1, 2xu3, 2xu4, 2xu5, 2yj2, 2yj8, 2yj9, 2yjb, 2yjc, 3bc3, 3h89. 组织蛋白酶L1 英语 Cathepsin L1 是人类体内由CTSL1基因编码的蛋白质 3 4 5 该蛋白质是木瓜样蛋白酶 英语 Papain like protease 是一种溶酶体半胱氨酸蛋白酶 在细胞内蛋白质分解代谢中起着主要的作用 6 7 8 9 组织蛋白酶L1已知的結構PDB人类UniProt搜索 PDBe RCSBPDBID列表1CJL 1CS8 1ICF 1MHW 2NQD 2VHS 2XU1 2XU3 2XU4 2XU5 2YJ2 2YJ8 2YJ9 2YJB 2YJC 3BC3 3H89 3H8B 3H8C 3HHA 3HWN 3IV2 3K24 3KSE 3OF8 3OF9 4AXL 4AXM 5F02 5I4H識別號别名CTSL CATL CTSL1 MEP cathepsin L外部IDOMIM 116880 HomoloGene 129366 GeneCards CTSL基因位置 人类 染色体9號染色體 1 基因座9q21 33起始87 724 051 bp 1 终止87 731 469 bp 1 RNA表达模式查阅更多表达数据基因本體分子功能 fibronectin binding 半胱氨酸型肽酶活性 collagen binding histone binding serpin family protein binding 肽酶活性 血浆蛋白结合 cysteine type endopeptidase activity 水解酶活性 proteoglycan binding serine type endopeptidase activity細胞組分 細胞外區域 endolysosome lumen lysosomal lumen 溶酶体 外排體 细胞核 細胞外空間 collagen containing extracellular matrix 多囊泡体 细胞膜生物學過程 macrophage apoptotic process antigen processing and presentation adaptive immune response antigen processing and presentation of exogenous peptide antigen via MHC class II extracellular matrix disassembly 蛋白酶解 toll like receptor signaling pathway cellular response to thyroid hormone stimulus collagen catabolic process proteolysis involved in cellular protein catabolic process regulation of keratinocyte differentiationSources Amigo QuickGO直系同源物種人類小鼠Entrez1514无数据EnsemblENSG00000135047无数据UniProtP07711Q9HBQ7无数据mRNA 序列NM 001257971 NM 001257972 NM 001257973 NM 001912 NM 145918 NM 001382757 NM 001382758 NM 001382766 NM 001382767 NM 001382768无数据蛋白序列NP 001244900 NP 001244901 NP 001244902 NP 001903 NP 666023 NP 001369686 NP 001369687 NP 001369695 NP 001369696 NP 001369697NP 001244902 1无数据基因位置 UCSC Chr 9 87 72 87 73 Mb无数据PubMed 查找 2 无数据維基數據檢視 編輯人類 目录 1 作用 1 1 病毒进入 1 2 炎症 2 交互作用 3 分布 4 参见 5 参考文献 6 拓展阅读 7 外部链接作用 编辑组织蛋白酶L1是肽酶C1 组织蛋白酶 MEROPS家族的成员 组织蛋白酶L1在包括正常溶酶体介导的蛋白质周转 抗原 前蛋白加工以及细胞凋亡在内的多种过程中发挥重要的作用 10 其底物包括胶原蛋白 弹性蛋白和SERPINA1 英语 Alpha 1 antitrypsin 这是中性粒细胞弹性蛋白酶 英语 Neutrophil elastase 活性的主要控制元素 组织蛋白酶L1与多种病理过程有关 包括肌病 英语 Myopathy 冠状动脉疾病中的肌原纤维 英语 Myofibril 坏死以及肾小管对蛋白尿的反应 它是由二硫键连接的重链和轻链组成的二聚体 均由单一蛋白质前体产生 已发现该基因至少有两种编码相同蛋白质的转录变体 5 病毒进入 编辑 病毒进入细胞需要2型新冠病毒S2刺突蛋白的裂解 此过程可以通过位于细胞膜上的蛋白酶 跨膜丝氨酸蛋白酶2或内溶酶体中的组织蛋白酶 主要是组织蛋白酶L1 来完成 11 羟氯喹可以抑制内溶酶体中组织蛋白酶L1的作用 但由于与跨膜丝氨酸蛋白酶2裂解相比 组织蛋白酶L1的裂解较小 因此羟氯喹对2型新冠病毒感染的抑制作用很小 11 炎症 编辑 虽然组织蛋白酶L1通常被表征为溶酶体蛋白酶 但它可以被分泌 导致病理性炎症 12 组织蛋白酶L1和其他木瓜样蛋白酶在引起病理性炎症时往往由巨噬细胞和其他侵入组织的免疫细胞分泌而出 13 交互作用 编辑组织蛋白酶L1已被证明与胱抑素A有相互作用 14 15 分布 编辑组织蛋白酶L1已在许多生物体中发现 包括鱼类 16 鸟类 哺乳动物和海绵 17 参见 编辑组织蛋白酶V 或称为组织蛋白酶L2或组织蛋白酶U 组织蛋白酶参考文献 编辑 1 0 1 1 1 2 GRCh38 Ensembl release 89 ENSG00000135047 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Chauhan SS Popescu NC Ray D Fleischmann R Gottesman MM Troen BR Cloning genomic organization and chromosomal localization of human cathepsin L J Biol Chem Feb 1993 268 2 1039 45 PMID 8419312 doi 10 1016 S0021 9258 18 54038 2 Joseph LJ Chang LC Stamenkovich D Sukhatme VP Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L An abundant transcript induced by transformation of fibroblasts J Clin Invest Jun 1988 81 5 1621 9 PMC 442598 PMID 2835398 doi 10 1172 JCI113497 5 0 5 1 Entrez Gene CTSL1 cathepsin L1 Barrett AJ Kirschke H Cathepsin B Cathepsin H and cathepsin L Methods in Enzymology 1981 80 Pt C 535 561 PMID 7043200 doi 10 1016 s0076 6879 81 80043 2 Barrett AJ Buttle DJ Mason RW Lysosomal cysteine proteinases ISI Atlas of Science Biochemistry 1988 1 256 260 Joseph LJ Chang LC Stamenkovich D Sukhatme VP Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L An abundant transcript induced by transformation of fibroblasts The Journal of Clinical Investigation May 1988 81 5 1621 1629 PMC 442598 PMID 2835398 doi 10 1172 JCI113497 Kirschke H Wikstrom P Shaw E Active center differences between cathepsins L and B the S1 binding region FEBS Letters February 1988 228 1 128 130 PMID 3342870 doi 10 1016 0014 5793 88 80600 8 Dickinson DP Cysteine Peptidases of Mammals Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and Disease Critical Reviews in Oral Biology and Medicine 2002 13 3 238 75 PMID 12090464 doi 10 1177 154411130201300304 11 0 11 1 Jackson CB Farzan M Chen B Choe H Mechanisms of SARS CoV 2 entry into cells Nature Reviews Molecular Cell Biology January 2022 23 1 3 20 PMC 8491763 PMID 34611326 doi 10 1038 s41580 021 00418 x Gomes CP Fernandes DE Casimiro F da Mata GF Passos MT Varela P et al Cathepsin L in COVID 19 From Pharmacological Evidences to Genetics Frontiers in Cellular and Infection Microbiology 2022 10 589505 PMC 7753008 PMID 33364201 doi 10 3389 fcimb 2020 589505 Berdowska I Matusiewicz M Cathepsin L transmembrane peptidase serine subfamily member 2 4 and other host proteases in COVID 19 pathogenesis with impact on gastrointestinal tract World Journal of Gastroenterology October 2021 27 39 6590 6600 PMC 8554394 PMID 34754154 doi 10 3748 wjg v27 i39 6590 Majerle Andreja Jerala Roman Protein inhibitors form complexes with procathepsin L and augment cleavage of the propeptide Arch Biochem Biophys Sep 2003 417 1 53 8 ISSN 0003 9861 PMID 12921779 doi 10 1016 S0003 9861 03 00319 9 Estrada S Nycander M Hill N J Craven C J Waltho J P Bjork I The role of Gly 4 of human cystatin A stefin A in the binding of target proteinases Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly 4 mutants with papain cathepsin B and cathepsin L Biochemistry May 1998 37 20 7551 60 ISSN 0006 2960 PMID 9585570 doi 10 1021 bi980026r Venkatesh K Prasanth B Rajesh P Annie JG Mukesh P Jesu A A murrel cysteine protease cathepsin L bioinformatics characterization gene expression and proteolytic activity Biologia 2014 39 3 395 406 doi 10 2478 s11756 013 0326 8 Sevenich L Pennacchio LA Peters C Reinheckel T Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B L double deficient mice Biological Chemistry July 2006 387 7 885 91 2022 10 31 PMID 16913838 S2CID 27739485 doi 10 1515 BC 2006 112 原始内容存档于2022 10 31 拓展阅读 编辑Smith CG Smith MT Besch NF et al Effect of delta 9 tetrahydrocannabinol THC on female reproductive function Advances in the Biosciences 1980 22 23 449 67 ISBN 9780080237596 PMID 116880 doi 10 1016 b978 0 08 023759 6 50040 8 Goretzki L Schmitt M Mann K et al Effective activation of the proenzyme form of the urokinase type plasminogen activator pro uPA by the cysteine protease cathepsin L FEBS Lett 1992 297 1 2 112 8 PMID 1551416 S2CID 45421148 doi 10 1016 0014 5793 92 80339 I Dunn AD Crutchfield HE Dunn JT Thyroglobulin processing by thyroidal proteases Major sites of cleavage by cathepsins B D and L J Biol Chem 1991 266 30 20198 204 PMID 1939080 doi 10 1016 S0021 9258 18 54909 7 Stearns NA Dong JM Pan JX et al Comparison of cathepsin L synthesized by normal and transformed cells at the gene message protein and oligosaccharide levels Arch Biochem Biophys 1991 283 2 447 57 PMID 2275556 doi 10 1016 0003 9861 90 90666 M Ritonja A Popovic T Kotnik M et al Amino acid sequences of the human kidney cathepsins H and L FEBS Lett 1988 228 2 341 5 PMID 3342889 S2CID 45768546 doi 10 1016 0014 5793 88 80028 0 Gal S Gottesman MM Isolation and sequence of a cDNA for human pro cathepsin L Biochem J 1988 253 1 303 6 PMC 1149292 PMID 3421948 doi 10 1042 bj2530303 Johnson DA Barrett AJ Mason RW Cathepsin L inactivates alpha 1 proteinase inhibitor by cleavage in the reactive site region J Biol Chem 1986 261 31 14748 51 PMID 3490478 doi 10 1016 S0021 9258 18 66935 2 Mason RW Walker JE Northrop FD The N terminal amino acid sequences of the heavy and light chains of human cathepsin L Relationship to a cDNA clone for a major cysteine proteinase from a mouse macrophage cell line Biochem J 1987 240 2 373 7 PMC 1147428 PMID 3545185 doi 10 1042 bj2400373 Joseph L Lapid S Sukhatme V The major ras induced protein in NIH3T3 cells is cathepsin L Nucleic Acids Res 1987 15 7 3186 PMC 340927 PMID 3550705 doi 10 1093 nar 15 7 3186 Kargel HJ Dettmer R Etzold G et al Action of rat liver cathepsin L on glucagon Acta Biol Med Ger 1982 40 9 1139 43 PMID 7340337 Bevec T Stoka V Pungercic G et al Major histocompatibility complex class II associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L J Exp Med 1996 183 4 1331 8 PMC 2192513 PMID 8666891 doi 10 1084 jem 183 4 1331 Coulombe R Grochulski P Sivaraman J et al Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment EMBO J 1996 15 20 5492 503 PMC 452294 PMID 8896443 doi 10 1002 j 1460 2075 1996 tb00934 x Baumgrass R Williamson MK Price PA Identification of peptide fragments generated by digestion of bovine and human osteocalcin with the lysosomal proteinases cathepsin B D L H and S J Bone Miner Res 1997 12 3 447 55 PMID 9076588 S2CID 20815411 doi 10 1359 jbmr 1997 12 3 447 Fujishima A Imai Y Nomura T et al The crystal structure of human cathepsin L complexed with E 64 FEBS Lett 1997 407 1 47 50 PMID 9141479 S2CID 46288832 doi 10 1016 S0014 5793 97 00216 0 Menard R Carmona E Takebe S et al Autocatalytic processing of recombinant human procathepsin L Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro J Biol Chem 1998 273 8 4478 84 PMID 9468501 doi 10 1074 jbc 273 8 4478 Schick C Pemberton PA Shi GP et al Cross class inhibition of the cysteine proteinases cathepsins K L and S by the serpin squamous cell carcinoma antigen 1 a kinetic analysis Biochemistry 1998 37 15 5258 66 PMID 9548757 doi 10 1021 bi972521d Estrada S Nycander M Hill NJ et al The role of Gly 4 of human cystatin A stefin A in the binding of target proteinases Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly 4 mutants with papain cathepsin B and cathepsin L Biochemistry 1998 37 20 7551 60 PMID 9585570 doi 10 1021 bi980026r Halfon S Ford J Foster J et al Leukocystatin a new Class II cystatin expressed selectively by hematopoietic cells J Biol Chem 1998 273 26 16400 8 PMID 9632704 doi 10 1074 jbc 273 26 16400 外部链接 编辑The MEROPS online database for peptidases and their inhibitors C01 032 醫學主題詞表 MeSH Cathepsin L 生物学主题 取自 https zh wikipedia org w index php title 组织蛋白酶L1 amp oldid 75102779, 维基百科，wiki，书籍，书籍，图书馆，

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