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维基百科

组织蛋白酶D

行進 27, 2023

组织蛋白酶D是一种在人体中由CTSD基因编码的蛋白质。[6][7]该基因编码一种溶酶体天冬氨酰蛋白酶，该蛋白酶由二硫键连接的重链和轻链的蛋白二聚体组成，两者均由单一蛋白质前体产生。组织蛋白酶D是一种天冬氨酸内切蛋白酶，广泛分布于溶酶体中。[8]组织蛋白酶D的主要功能是降解蛋白质并激活溶酶体前区室中生物活性蛋白的前体。[9]这种蛋白酶是肽酶A1家族的成员，具有与胃蛋白酶A相似但比胃蛋白酶A更窄的特异性。 CTSD基因的转录从几个位点开始，包括一个作为雌激素调节转录物起始位点的位点。该基因的突变与几种疾病的发病机制有关，包括乳腺癌和可能的阿尔茨海默病症。[7]CTSD基因的纯合缺失导致出生后阶段的早期致死性。[10]据报道，CTSD基因的缺陷是神经元蜡样脂褐质沉积症（NCL）的根本原因。[11]

组织蛋白酶D
已知的結構
PDB直系同源搜索: PDBe RCSB
識別號
别名CTSD；, CLN10, CPSD, HEL-S-130P, cathepsin D
外部IDOMIM：116840 MGI：88562 HomoloGene：55616 GeneCards：CTSD
相關疾病
neuronal ceroid lipofuscinosis 10、​神經元蠟樣脂褐質儲積症[1]
基因位置（人类）
染色体11號染色體[2]
基因座11p15.5起始1,752,752 bp[2]
终止1,764,573 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

1509

13033

Ensembl

ENSG00000117984

ENSMUSG00000007891

UniProt

P07339

P18242

mRNA​序列

NM_001909

NM_009983

蛋白序列

NP_001900

NP_034113

基因位置​（UCSC）Chr 11: 1.75 – 1.76 MbChr 7: 141.93 – 141.94 Mb
PubMed​查找[4][5]
維基數據
檢視/編輯人類檢視/編輯小鼠

结构

基因

CTSD基因位于11号染色体。

蛋白质

组织蛋白酶D的催化位点包括位于14kDa和34kDa链上的两个关键天冬氨酸残基（氨基酸33和231）。[12]成熟组织蛋白酶D的最终形式由337个氨基酸残基、196个重链氨基酸残基和141个轻链氨基酸残基组成。这两条链通过疏水效应连接起来。[13]

功能

在体外，组织蛋白酶D的最适pH值为4.5至5.0。[14]组织蛋白酶D是一种天冬氨酸蛋白酶，它严重依赖于其活性位点Asp残基的质子化。与Asp质子化一起，较低的pH 值也会导致组织蛋白酶D的构象转换：随着pH值的下降，蛋白酶的N端片段会移出活性位点。[15][16][17]与其他天冬氨酸蛋白酶类似，组织蛋白酶D在活性位点的结合裂隙中容纳多达8个氨基酸残基。组织蛋白酶D的主要生理功能包括细胞内蛋白质的代谢降解、多肽激素和生长因子的活化和降解、酶前体的活化、酶激活剂和抑制剂的加工、脑抗原加工和细胞程序性死亡的调节。[18][19][20][21]组织蛋白酶D也可以在细胞外空间中找到，[21]它是少数在中性pH条件下显示出一些活性的组织蛋白酶之一。[22]它能够激活生长因子VEGF-C和VEGF-D，这可能部分解释了它与肿瘤进展的相关性。[23]

临床意义

NCL表现为视觉功能的进行性丧失和神经发育衰退、癫痫发作、肌阵挛性抽搐和过早死亡。 CTSD基因是已确定的八个基因之一，其缺陷是导致NCL的原因。[11]据报告，外显子6中的纯合单核苷酸重复可以改变阅读框并导致255位的过早终止密码子。组织蛋白酶 D 的过表达刺激致瘤性和转移以及肿瘤细胞凋亡的开始。这种蛋白酶被认为是乳腺癌预后不良的独立标志物，与临床转移的发生率相关。[24][25]CTSD基因敲除会导致肠坏死和出血，胸腺凋亡增加，表明某些上皮细胞需要组织蛋白酶D进行组织重塑和更新。[10]另据报告，CTSD基因型可能对男性阿尔茨海默病风险有强烈影响。[26]组织蛋白酶D的酶活性诱导含有载脂蛋白B-100 的脂蛋白（包括 LDL）的水解修饰，这意味着它也可能与动脉粥样硬化有关。[19][27]

相互作用

参考文献

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更多阅读

  • Chao J, Miao RQ, Chen V, Chen LM, Chao L. Novel roles of kallistatin, a specific tissue kallikrein inhibitor, in vascular remodeling. Biological Chemistry. January 2001, 382 (1): 15–21. PMID 11258665. S2CID 33204682. doi:10.1515/BC.2001.003. 
  • Leto G, Tumminello FM, Crescimanno M, Flandina C, Gebbia N. Cathepsin D expression levels in nongynecological solid tumors: clinical and therapeutic implications. Clinical & Experimental Metastasis. 2004, 21 (2): 91–106. PMID 15168727. S2CID 3476324. doi:10.1023/B:CLIN.0000024740.44602.b7. 
  • Liaudet-Coopman E, Beaujouin M, Derocq D, Garcia M, Glondu-Lassis M, Laurent-Matha V, Prébois C, Rochefort H, Vignon F. Cathepsin D: newly discovered functions of a long-standing aspartic protease in cancer and apoptosis. Cancer Letters. June 2006, 237 (2): 167–79 [2022-09-18]. PMID 16046058. doi:10.1016/j.canlet.2005.06.007. （原始内容于2022-09-21）. 
  • Knight CG, Barrett AJ. Interaction of human cathepsin D with the inhibitor pepstatin. The Biochemical Journal. April 1976, 155 (1): 117–25. PMC 1172808  . PMID 938470. doi:10.1042/bj1550117. 
  • Gulnik S, Baldwin ET, Tarasova N, Erickson J. Human liver cathepsin D. Purification, crystallization and preliminary X-ray diffraction analysis of a lysosomal enzyme. Journal of Molecular Biology. September 1992, 227 (1): 265–70 [2022-09-18]. PMID 1522590. doi:10.1016/0022-2836(92)90696-H. （原始内容于2022-09-22）. 
  • Conner GE, Richo G. Isolation and characterization of a stable activation intermediate of the lysosomal aspartyl protease cathepsin D. Biochemistry. February 1992, 31 (4): 1142–7. PMID 1734961. doi:10.1021/bi00119a024. 
  • Fujita H, Tanaka Y, Noguchi Y, Kono A, Himeno M, Kato K. Isolation and sequencing of a cDNA clone encoding rat liver lysosomal cathepsin D and the structure of three forms of mature enzymes. Biochemical and Biophysical Research Communications. August 1991, 179 (1): 190–6. PMID 1883350. doi:10.1016/0006-291X(91)91353-E. 
  • Dunn AD, Crutchfield HE, Dunn JT. Thyroglobulin processing by thyroidal proteases. Major sites of cleavage by cathepsins B, D, and L. The Journal of Biological Chemistry. October 1991, 266 (30): 20198–204. PMID 1939080. doi:10.1016/S0021-9258(18)54909-7  . 
  • Lenarcic B, Krasovec M, Ritonja A, Olafsson I, Turk V. Inactivation of human cystatin C and kininogen by human cathepsin D. FEBS Letters. March 1991, 280 (2): 211–5. PMID 2013314. S2CID 23798502. doi:10.1016/0014-5793(91)80295-E. 
  • Redecker B, Heckendorf B, Grosch HW, Mersmann G, Hasilik A. Molecular organization of the human cathepsin D gene. DNA and Cell Biology. 1991, 10 (6): 423–31. PMID 2069717. doi:10.1089/dna.1991.10.423. 
  • Conner GE, Udey JA. Expression and refolding of recombinant human fibroblast procathepsin D. DNA and Cell Biology. 1990, 9 (1): 1–9. PMID 2180427. doi:10.1089/dna.1990.9.1. 
  • Capony F, Rougeot C, Montcourrier P, Cavailles V, Salazar G, Rochefort H. Increased secretion, altered processing, and glycosylation of pro-cathepsin D in human mammary cancer cells. Cancer Research. July 1989, 49 (14): 3904–9. PMID 2736531. 
  • Lenarcic B, Kos J, Dolenc I, Lucovnik P, Krizaj I, Turk V. Cathepsin D inactivates cysteine proteinase inhibitors, cystatins. Biochemical and Biophysical Research Communications. July 1988, 154 (2): 765–72. PMID 3261170. doi:10.1016/0006-291X(88)90206-9. 
  • Westley BR, May FE. Oestrogen regulates cathepsin D mRNA levels in oestrogen responsive human breast cancer cells. Nucleic Acids Research. May 1987, 15 (9): 3773–86. PMC 340781  . PMID 3588310. doi:10.1093/nar/15.9.3773. 
  • Terayama H, Fukuzumi R. Ubiquitous presence of calciferin-like and cathepsin D-like activities in the sera (vertebrates) and humoral fluids (invertebrates). Comparative Biochemistry and Physiology. B, Comparative Biochemistry. 1987, 87 (4): 675–9. PMID 3665421. doi:10.1016/0305-0491(87)90373-7. 
  • Sekiguchi K, Siri A, Zardi L, Hakomori S. Differences in domain structure between human fibronectins isolated from plasma and from culture supernatants of normal and transformed fibroblasts. Studies with domain-specific antibodies. The Journal of Biological Chemistry. April 1985, 260 (8): 5105–14. PMID 3988746. doi:10.1016/S0021-9258(18)89185-2  . 
  • Lemansky P, Gieselmann V, Hasilik A, von Figura K. Cathepsin D and beta-hexosaminidase synthesized in the presence of 1-deoxynojirimycin accumulate in the endoplasmic reticulum. The Journal of Biological Chemistry. August 1984, 259 (16): 10129–35. PMID 6236213. doi:10.1016/S0021-9258(18)90939-7  . 
  • Dreyer RN, Bausch KM, Fracasso P, Hammond LJ, Wunderlich D, Wirak DO, Davis G, Brini CM, Buckholz TM, König G. Processing of the pre-beta-amyloid protein by cathepsin D is enhanced by a familial Alzheimer's disease mutation. European Journal of Biochemistry. September 1994, 224 (2): 265–71. PMID 7523115. doi:10.1111/j.1432-1033.1994.00265.x  . 
  • Atkins KB, Troen BR. Regulation of cathepsin D gene expression in HL-60 cells by retinoic acid and calcitriol. Cell Growth & Differentiation. July 1995, 6 (7): 871–7. PMID 7547509. 

外部链接

  • The MEROPS online database for peptidases and their inhibitors: A01.009 （页面存档备份，存于互联网档案馆）
  • GeneReviews/NIH/NCBI/UW entry on Neuronal Ceroid-Lipofuscinoses （页面存档备份，存于互联网档案馆）
  • PDBe-KB （页面存档备份，存于互联网档案馆） provides an overview of all the structure information available in the PDB for Human Cathepsin D

行進 27, 2023
组织蛋白酶d, 是一种在人体中由ctsd基因编码的蛋白质, 该基因编码一种溶酶体天冬氨酰蛋白酶, 该蛋白酶由二硫键连接的重链和轻链的蛋白二聚体组成, 两者均由单一蛋白质前体产生, 是一种天冬氨酸内切蛋白酶, 广泛分布于溶酶体中, 的主要功能是降解蛋白质并激活溶酶体前区室中生物活性蛋白的前体, 这种蛋白酶是肽酶a1家族的成员, 具有与胃蛋白酶a相似但比胃蛋白酶a更窄的特异性, ctsd基因的转录从几个位点开始, 包括一个作为雌激素调节转录物起始位点的位点, 该基因的突变与几种疾病的发病机制有关, 包括乳腺癌和可能的阿. 组织蛋白酶D是一种在人体中由CTSD基因编码的蛋白质 6 7 该基因编码一种溶酶体天冬氨酰蛋白酶 该蛋白酶由二硫键连接的重链和轻链的蛋白二聚体组成 两者均由单一蛋白质前体产生 组织蛋白酶D是一种天冬氨酸内切蛋白酶 广泛分布于溶酶体中 8 组织蛋白酶D的主要功能是降解蛋白质并激活溶酶体前区室中生物活性蛋白的前体 9 这种蛋白酶是肽酶A1家族的成员 具有与胃蛋白酶A相似但比胃蛋白酶A更窄的特异性 CTSD基因的转录从几个位点开始 包括一个作为雌激素调节转录物起始位点的位点 该基因的突变与几种疾病的发病机制有关 包括乳腺癌和可能的阿尔茨海默病症 7 CTSD基因的纯合缺失导致出生后阶段的早期致死性 10 据报道 CTSD基因的缺陷是神经元蜡样脂褐质沉积症 NCL 的根本原因 11 组织蛋白酶D已知的結構PDB直系同源搜索 PDBe RCSBPDBID列表1LYA 1LYB 1LYW 4OBZ 4OC6 4OD9識別號别名CTSD CLN10 CPSD HEL S 130P cathepsin D外部IDOMIM 116840 MGI 88562 HomoloGene 55616 GeneCards CTSD相關疾病neuronal ceroid lipofuscinosis 10 神經元蠟樣脂褐質儲積症 1 基因位置 人类 染色体11號染色體 2 基因座11p15 5起始1 752 752 bp 2 终止1 764 573 bp 2 基因位置 小鼠 染色体小鼠7号染色体 3 基因座7 7 F5起始141 929 648 bp 3 终止141 941 775 bp 3 RNA表达模式查阅更多表达数据基因本體分子功能 肽酶活性 水解酶活性 血浆蛋白结合 serine type endopeptidase activity cysteine type endopeptidase activity aspartic type endopeptidase activity aspartic type peptidase activity細胞組分 lysosomal lumen 外排體 脂筏模型 细胞外间质 溶酶体 黑色素体 細胞外空間 specific granule lumen tertiary granule lumen ficolin 1 rich granule lumen 細胞外區域 collagen containing extracellular matrix lysosomal membrane endosome membrane生物學過程 protein catabolic process 自噬 collagen catabolic process antigen processing and presentation of exogenous peptide antigen via MHC class II 蛋白酶解 neutrophil degranulation lipoprotein catabolic process positive regulation of apoptotic process positive regulation of cysteine type endopeptidase activity involved in apoptotic process regulation of establishment of protein localizationSources Amigo QuickGO直系同源物種人類小鼠Entrez150913033EnsemblENSG00000117984ENSMUSG00000007891UniProtP07339P18242mRNA 序列NM 001909NM 009983蛋白序列NP 001900NP 034113基因位置 UCSC Chr 11 1 75 1 76 MbChr 7 141 93 141 94 MbPubMed 查找 4 5 維基數據檢視 編輯人類檢視 編輯小鼠 目录 1 结构 1 1 基因 1 2 蛋白质 2 功能 3 临床意义 4 相互作用 5 参考文献 6 更多阅读 7 外部链接结构 编辑基因 编辑 CTSD基因位于11号染色体 蛋白质 编辑 组织蛋白酶D的催化位点包括位于14kDa和34kDa链上的两个关键天冬氨酸残基 氨基酸33和231 12 成熟组织蛋白酶D的最终形式由337个氨基酸残基 196个重链氨基酸残基和141个轻链氨基酸残基组成 这两条链通过疏水效应连接起来 13 功能 编辑在体外 组织蛋白酶D的最适pH值为4 5至5 0 14 组织蛋白酶D是一种天冬氨酸蛋白酶 它严重依赖于其活性位点Asp残基的质子化 与Asp质子化一起 较低的pH 值也会导致组织蛋白酶D的构象转换 随着pH值的下降 蛋白酶的N端片段会移出活性位点 15 16 17 与其他天冬氨酸蛋白酶类似 组织蛋白酶D在活性位点的结合裂隙中容纳多达8个氨基酸残基 组织蛋白酶D的主要生理功能包括细胞内蛋白质的代谢降解 多肽激素和生长因子的活化和降解 酶前体的活化 酶激活剂和抑制剂的加工 脑抗原加工和细胞程序性死亡的调节 18 19 20 21 组织蛋白酶D也可以在细胞外空间中找到 21 它是少数在中性pH条件下显示出一些活性的组织蛋白酶之一 22 它能够激活生长因子VEGF C和VEGF D 这可能部分解释了它与肿瘤进展的相关性 23 临床意义 编辑NCL表现为视觉功能的进行性丧失和神经发育衰退 癫痫发作 肌阵挛性抽搐和过早死亡 CTSD基因是已确定的八个基因之一 其缺陷是导致NCL的原因 11 据报告 外显子6中的纯合单核苷酸重复可以改变阅读框并导致255位的过早终止密码子 组织蛋白酶 D 的过表达刺激致瘤性和转移以及肿瘤细胞凋亡的开始 这种蛋白酶被认为是乳腺癌预后不良的独立标志物 与临床转移的发生率相关 24 25 CTSD基因敲除会导致肠坏死和出血 胸腺凋亡增加 表明某些上皮细胞需要组织蛋白酶D进行组织重塑和更新 10 另据报告 CTSD基因型可能对男性阿尔茨海默病风险有强烈影响 26 组织蛋白酶D的酶活性诱导含有载脂蛋白B 100 的脂蛋白 包括 LDL 的水解修饰 这意味着它也可能与动脉粥样硬化有关 19 27 相互作用 编辑胃酶抑素 28 转谷氨酰胺酶2 29 血红素结合蛋白1 HEBP1 30 a 2 巨球蛋白 A2M 31 神经酰胺 32 参考文献 编辑 與组织蛋白酶D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 ENSG00000117984 Ensembl May 2017 3 0 3 1 3 2 GRCm38 Ensembl release 89 ENSMUSG00000007891 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 Faust PL Kornfeld S Chirgwin JM Cloning and sequence analysis of cDNA for human cathepsin D Proceedings of the National Academy of Sciences of the United States of America August 1985 82 15 4910 4 Bibcode 1985PNAS 82 4910F PMC 390467 PMID 3927292 doi 10 1073 pnas 82 15 4910 7 0 7 1 Entrez Gene CTSD cathepsin D 2022 09 18 原始内容存档于2010 04 12 Barrett AJ Cathepsin D Purification of isoenzymes from human and chicken liver The Biochemical Journal April 1970 117 3 601 7 PMC 1178965 PMID 5419752 doi 10 1042 bj1170601 Diment S Martin KJ Stahl PD Cleavage of parathyroid hormone in macrophage endosomes illustrates a novel pathway for 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Polish Histochemical and Cytochemical Society 2008 46 1 23 38 PMID 18296260 doi 10 2478 v10042 008 0003 x Briozzo P Morisset M Capony F Rougeot C Rochefort H In vitro degradation of extracellular matrix with Mr 52 000 cathepsin D secreted by breast cancer cells Cancer Research July 1988 48 13 3688 92 PMID 3378211 Authier F Metioui M Fabrega S Kouach M Briand G Endosomal proteolysis of internalized insulin at the C terminal region of the B chain by cathepsin D The Journal of Biological Chemistry March 2002 277 11 9437 46 PMID 11779865 doi 10 1074 jbc M110188200 Lee AY Gulnik SV Erickson JW Conformational switching in an aspartic proteinase Nature Structural Biology October 1998 5 10 866 71 2022 09 18 PMID 9783744 S2CID 5685201 doi 10 1038 2306 原始内容存档于2022 09 22 Petsko G Ringe D Protein Structure and Function Oxford England Sunderland MA New York Oxford University Press 2004 ISBN 978 1 4051 1922 1 Baechle D Flad T Cansier A Steffen H Schittek B Tolson J et al Cathepsin D is present in human eccrine sweat and involved in the postsecretory processing of the antimicrobial peptide DCD 1L The Journal of Biological Chemistry March 2006 281 9 5406 15 PMID 16354654 doi 10 1074 jbc M504670200 19 0 19 1 Hakala JK Oksjoki R Laine P Du H Grabowski GA Kovanen PT Pentikainen MO Lysosomal enzymes are released from cultured human macrophages hydrolyze LDL in vitro and are present extracellularly in human atherosclerotic lesions Arteriosclerosis Thrombosis and Vascular Biology August 2003 23 8 1430 6 PMID 12750117 doi 10 1161 01 ATV 0000077207 49221 06 Bankowska A Gacko M Chyczewska E Worowska A Biological and diagnostic role of cathepsin D Roczniki Akademii Medycznej W Bialymstoku 1997 42 Suppl 1 79 85 PMID 9337526 21 0 21 1 Benes P Vetvicka V Fusek M Cathepsin D many functions of one aspartic protease Critical Reviews in Oncology Hematology October 2008 68 1 12 28 PMC 2635020 PMID 18396408 doi 10 1016 j critrevonc 2008 02 008 Lkhider M Castino R Bouguyon E Isidoro C Ollivier Bousquet M Cathepsin D released by lactating rat mammary epithelial cells is involved in prolactin cleavage under physiological conditions Journal of Cell Science October 2004 117 Pt 21 5155 64 PMID 15456852 doi 10 1242 jcs 01396 Jha Sawan Kumar Rauniyar Khushbu Chronowska Ewa Mattonet Kenny Maina Eunice Wairimu Koistinen Hannu Stenman Ulf Hakan Alitalo Kari Jeltsch Michael KLK3 PSA and cathepsin D activate VEGF C and VEGF D eLife 2019 05 17 8 44478 ISSN 2050 084X PMC 6588350 PMID 31099754 doi 10 7554 eLife 44478 Traynor JP Oun HA McKenzie P Shilliday IR McKay IG Dunlop A Geddes CC Mactier RA Assessing the utility of the stop dialysate flow method in patients receiving haemodiafiltration Nephrology Dialysis Transplantation November 2005 20 11 2479 84 PMID 16046508 doi 10 1093 ndt gfi021 Wolf M Clark Lewis I Buri C Langen H Lis M Mazzucchelli L Cathepsin D specifically cleaves the chemokines macrophage inflammatory protein 1 alpha macrophage inflammatory protein 1 beta and SLC that are expressed in human breast cancer The American Journal of Pathology April 2003 162 4 1183 90 PMC 1851240 PMID 12651610 doi 10 1016 S0002 9440 10 63914 4 Menzer G Muller Thomsen T Meins W Alberici A Binetti G Hock C Nitsch RM Stoppe G Reiss J Finckh U Non replication of association between cathepsin D genotype and late onset Alzheimer disease American Journal of Medical Genetics March 2001 105 2 179 82 PMID 11304834 doi 10 1002 ajmg 1204 Haidar B Kiss RS Sarov Blat L Brunet R Harder C McPherson R Marcel YL Cathepsin D a lysosomal protease regulates ABCA1 mediated lipid efflux The Journal of Biological Chemistry December 2006 281 52 39971 81 PMID 17032648 doi 10 1074 jbc M605095200 Umezawa H Aoyagi T Morishima H Matsuzaki M Hamada M Pepstatin a new pepsin inhibitor produced by Actinomycetes The Journal of Antibiotics May 1970 23 5 259 62 PMID 4912600 doi 10 7164 antibiotics 23 259 Kim SJ Kim KH Ahn ER Yoo BC Kim SY Depletion of cathepsin D by transglutaminase 2 through protein cross linking promotes cell survival Amino Acids January 2013 44 1 73 80 PMID 21960143 S2CID 17149825 doi 10 1007 s00726 011 1089 6 Devosse T Dutoit R Migeotte I De Nadai P Imbault V Communi D Salmon I Parmentier M Processing of HEBP1 by cathepsin D gives rise to F2L the agonist of formyl peptide receptor 3 Journal of Immunology August 2011 187 3 1475 85 PMID 21709160 doi 10 4049 jimmunol 1003545 Mariani E Seripa D Ingegni T Nocentini G Mangialasche F Ercolani S Cherubini A Metastasio A Pilotto A Senin U Mecocci P Interaction of CTSD and A2M polymorphisms in the risk for Alzheimer s disease Journal of the Neurological Sciences September 2006 247 2 187 91 PMID 16784755 S2CID 34224448 doi 10 1016 j jns 2006 05 043 Heinrich M Wickel M Schneider Brachert W Sandberg C Gahr J Schwandner R Weber T Saftig P Peters C Brunner J Kronke M Schutze S Cathepsin D targeted by acid sphingomyelinase derived ceramide The EMBO Journal October 1999 18 19 5252 63 PMC 1171596 PMID 10508159 doi 10 1093 emboj 18 19 5252 更多阅读 编辑Chao J Miao RQ Chen V Chen LM Chao L Novel roles of kallistatin a specific tissue kallikrein inhibitor in vascular remodeling Biological Chemistry January 2001 382 1 15 21 PMID 11258665 S2CID 33204682 doi 10 1515 BC 2001 003 Leto G Tumminello FM Crescimanno M Flandina C Gebbia N Cathepsin D expression levels in nongynecological solid tumors clinical and therapeutic implications Clinical amp Experimental Metastasis 2004 21 2 91 106 PMID 15168727 S2CID 3476324 doi 10 1023 B CLIN 0000024740 44602 b7 Liaudet Coopman E Beaujouin M Derocq D Garcia M Glondu Lassis M Laurent Matha V Prebois C Rochefort H Vignon F Cathepsin D newly discovered functions of a long standing aspartic protease in cancer and apoptosis Cancer Letters June 2006 237 2 167 79 2022 09 18 PMID 16046058 doi 10 1016 j canlet 2005 06 007 原始内容存档于2022 09 21 Knight CG Barrett AJ Interaction of human cathepsin D with the inhibitor pepstatin The Biochemical Journal April 1976 155 1 117 25 PMC 1172808 PMID 938470 doi 10 1042 bj1550117 Gulnik S Baldwin ET Tarasova N Erickson J Human liver cathepsin D Purification crystallization and preliminary X ray diffraction analysis of a lysosomal enzyme Journal of Molecular Biology September 1992 227 1 265 70 2022 09 18 PMID 1522590 doi 10 1016 0022 2836 92 90696 H 原始内容存档于2022 09 22 Conner GE Richo G Isolation and characterization of a stable activation intermediate of the lysosomal aspartyl protease cathepsin D Biochemistry February 1992 31 4 1142 7 PMID 1734961 doi 10 1021 bi00119a024 Fujita H Tanaka Y Noguchi Y Kono A Himeno M Kato K Isolation and sequencing of a cDNA clone encoding rat liver lysosomal cathepsin D and the structure of three forms of mature enzymes Biochemical and Biophysical Research Communications August 1991 179 1 190 6 PMID 1883350 doi 10 1016 0006 291X 91 91353 E Dunn AD Crutchfield HE Dunn JT Thyroglobulin processing by thyroidal proteases Major sites of cleavage by cathepsins B D and L The Journal of Biological Chemistry October 1991 266 30 20198 204 PMID 1939080 doi 10 1016 S0021 9258 18 54909 7 Lenarcic B Krasovec M Ritonja A Olafsson I Turk V Inactivation of human cystatin C and kininogen by human cathepsin D FEBS Letters March 1991 280 2 211 5 PMID 2013314 S2CID 23798502 doi 10 1016 0014 5793 91 80295 E Redecker B Heckendorf B Grosch HW Mersmann G Hasilik A Molecular organization of the human cathepsin D gene DNA and Cell Biology 1991 10 6 423 31 PMID 2069717 doi 10 1089 dna 1991 10 423 Conner GE Udey JA Expression and refolding of recombinant human fibroblast procathepsin D DNA and Cell Biology 1990 9 1 1 9 PMID 2180427 doi 10 1089 dna 1990 9 1 Capony F Rougeot C Montcourrier P Cavailles V Salazar G Rochefort H Increased secretion altered processing and glycosylation of pro cathepsin D in human mammary cancer cells Cancer Research July 1989 49 14 3904 9 PMID 2736531 Lenarcic B Kos J Dolenc I Lucovnik P Krizaj I Turk V Cathepsin D inactivates cysteine proteinase inhibitors cystatins Biochemical and Biophysical Research Communications July 1988 154 2 765 72 PMID 3261170 doi 10 1016 0006 291X 88 90206 9 Westley BR May FE Oestrogen regulates cathepsin D mRNA levels in oestrogen responsive human breast cancer cells Nucleic Acids Research May 1987 15 9 3773 86 PMC 340781 PMID 3588310 doi 10 1093 nar 15 9 3773 Terayama H Fukuzumi R Ubiquitous presence of calciferin like and cathepsin D like activities in the sera vertebrates and humoral fluids invertebrates Comparative Biochemistry and Physiology B Comparative Biochemistry 1987 87 4 675 9 PMID 3665421 doi 10 1016 0305 0491 87 90373 7 Sekiguchi K Siri A Zardi L Hakomori S Differences in domain structure between human fibronectins isolated from plasma and from culture supernatants of normal and transformed fibroblasts Studies with domain specific antibodies The Journal of Biological Chemistry April 1985 260 8 5105 14 PMID 3988746 doi 10 1016 S0021 9258 18 89185 2 Lemansky P Gieselmann V Hasilik A von Figura K Cathepsin D and beta hexosaminidase synthesized in the presence of 1 deoxynojirimycin accumulate in the endoplasmic reticulum The Journal of Biological Chemistry August 1984 259 16 10129 35 PMID 6236213 doi 10 1016 S0021 9258 18 90939 7 Dreyer RN Bausch KM Fracasso P Hammond LJ Wunderlich D Wirak DO Davis G Brini CM Buckholz TM Konig G Processing of the pre beta amyloid protein by cathepsin D is enhanced by a familial Alzheimer s disease mutation European Journal of Biochemistry September 1994 224 2 265 71 PMID 7523115 doi 10 1111 j 1432 1033 1994 00265 x Atkins KB Troen BR Regulation of cathepsin D gene expression in HL 60 cells by retinoic acid and calcitriol Cell Growth amp Differentiation July 1995 6 7 871 7 PMID 7547509 外部链接 编辑The MEROPS online database for peptidases and their inhibitors A01 009 页面存档备份 存于互联网档案馆 GeneReviews NIH NCBI UW entry on Neuronal Ceroid Lipofuscinoses 页面存档备份 存于互联网档案馆 PDBe KB 页面存档备份 存于互联网档案馆 provides an overview of all the structure information available in the PDB for Human Cathepsin D 取自 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