The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Cathepsin D--many functions of one aspartic protease
Abstract
For years, it has been held that cathepsin D (CD) is involved in rather non-specific protein degradation in a strongly acidic milieu of lysosomes. Studies with CD knock-out mice revealed that CD is not necessary for embryonal development, but it is indispensable for postnatal tissue homeostasis. Mutation that abolishes CD enzymatic activity causes neuronal ceroid lipofuscinosis (NCL) characterized by severe neurodegeneration, developmental regression, visual loss and epilepsy in both animals and humans. In the last decade, however, an increasing number of studies demonstrated that enzymatic function of CD is not restricted solely to acidic milieu of lysosomes with important consequences in regulation of apoptosis. In addition to CD enzymatic activity, it has been shown that apoptosis is also regulated by catalytically inactive mutants of CD which suggests that CD interacts with other important molecules and influences cell signaling. Moreover, procathepsin D (pCD), secreted from cancer cells, acts as a mitogen on both cancer and stromal cells and stimulates their pro-invasive and pro-metastatic properties. Numerous studies found that pCD/CD level represents an independent prognostic factor in a variety of cancers and is therefore considered to be a potential target of anti-cancer therapy. Studies dealing with functions of cathepsin D are complicated by the fact that there are several simultaneous forms of CD in a cell-pCD, intermediate enzymatically active CD and mature heavy…
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
An increase in pro-CTSD is a reliable indicator of impaired retromer-dependent trafficking and ultimately lysosomal dysfunction.
“Thus, an increase in pro-CTSD is considered a reliable indicator of impaired retromer-dependent trafficking (Benes et al., 2008; Rojas et al., 2008; Han et al., 2021), and ultimately lysosomal dysfunction.”
From The neuronal retromer can regulate both neuronal and microglial phenotypes of Alzheimer's disease (2022) · cites this paper as Benes et al., 2008
Citations
Cites
Systematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database
Bertram, L., McQueen, M. B., Mullin, K., Blacker, D., & Tanzi, R. E. (2007) · Nature Genetics · doi:10.1038/ng1934 · Cited by 1,857
Bidère, N., Lorenzo, H. K., Carmona, S., Laforge, M., Harper, F., Dumont, C., & Senik, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301911200 · Cited by 435
Boya, P., Gonzalez-Polo, R.-A., Poncet, D., Andreau, K., Vieira, H. L., Roumier, T., Perfettini, J.-L., & Kroemer, G. (2003) · Oncogene · doi:10.1038/sj.onc.1206622 · Cited by 385
Cataldo, A. M., Barnett, J. L., Berman, S. A., Li, J., Quarless, S., Bursztajn, S., Lippa, C., & Nixon, R. A. (1995) · Neuron · doi:10.1016/0896-6273(95)90324-0 · Cited by 379
Koike, M., Shibata, M., Waguri, S., Yoshimura, K., Tanida, I., Kominami, E., Gotow, T., Peters, C., von Figura, K., Mizushima, N., et al. (2005) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)61253-9 · Cited by 330
Tyynelä, J., Sohar, I., Sleat, D. E., Gin, R. M., Donnelly, R. J., Baumann, M., Haltia, M., & Lobel, P. (2000) · The EMBO Journal · doi:10.1093/emboj/19.12.2786 · Cited by 245
Prevention of oxidant-induced cell death by lysosomotropic iron chelators
Persson, H. L., Yu, Z., Tirosh, O., Eaton, J. W., & Brunk, U. T. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00106-0 · Cited by 185
Schwagerl, A. L., Mohan, P. S., Cataldo, A. M., Vonsattel, J. P., Kowall, N. W., & Nixon, R. A. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64010443.x · Cited by 107
Flagged first, then by citations
Research works printed but not linked: 212
- Hasilik, 1980, Biosynthesis of lysosomal enzymes in fibroblasts. Synthesis as precursors of higher molecular weight, J Biol Chem, 255, 4937, 10.1016/S0021-9258(19)85585-0 · DOI
- Kornfeld, 1990, Lysosomal enzyme targeting, Biochem Soc Trans, 18, 367, 10.1042/bst0180367 · DOI
- Hasilik, 1980, Biosynthesis of lysosomal enzymes in fibroblasts. Phosphorylation of mannose residues, J Biol Chem, 255, 4946, 10.1016/S0021-9258(19)85586-2 · DOI · Paper page
- Fortenberry, 1995, Role of glycosylation in the expression of human procathepsin D, J Cell Sci, 108, 2001, 10.1242/jcs.108.5.2001 · DOI
- von Figura, 1986, Lysosomal enzymes and their receptors, Annu Rev Biochem, 55, 167, 10.1146/annurev.bi.55.070186.001123 · DOI
- Rijnboutt, 1991, Mannose 6-phosphate-independent targeting of cathepsin D to lysosomes in HepG2 cells, J Biol Chem, 266, 23586, 10.1016/S0021-9258(18)54323-4 · DOI
- Zhu, 1994, Intermolecular association of lysosomal protein precursors during biosynthesis, J Biol Chem, 269, 3846, 10.1016/S0021-9258(17)41937-5 · DOI
- Capony, 1994, Specific mannose-6-phosphate receptor-independent sorting of pro-cathepsin D in breast cancer cells, Exp Cell Res, 215, 154, 10.1006/excr.1994.1327 · DOI
- Dittmer, 1999, Alternative mechanisms for trafficking of lysosomal enzymes in mannose 6-phosphate receptor-deficient mice are cell type-specific, J Cell Sci, 112, 1591, 10.1242/jcs.112.10.1591 · DOI
- Gopalakrishnan, 2004, Purified recombinant human prosaposin forms oligomers that bind procathepsin D and affect its autoactivation, Biochem J, 383, 507, 10.1042/BJ20040175 · DOI
- Erickson, 1981, Biosynthesis of a lysosomal enzyme. Partial structure of two transient and functionally distinct NH2-terminal sequences in cathepsin D, J Biol Chem, 256, 11224, 10.1016/S0021-9258(19)68581-9 · DOI
- Conner, 1992, Isolation and characterization of a stable activation intermediate of the lysosomal aspartyl protease cathepsin D, Biochemistry, 31, 1142, 10.1021/bi00119a024 · DOI
- Gieselmann, 1985, Processing of human cathepsin D in lysosomes in vitro, J Biol Chem, 260, 3215, 10.1016/S0021-9258(18)89493-5 · DOI
- Hentze, 1984, Enhanced degradation of cathepsin D synthesized in the presence of the threonine analog beta-hydroxynorvaline, Arch Biochem Biophys, 230, 375, 10.1016/0003-9861(84)90120-6 · DOI
- Samarel, 1989, Effects of cysteine protease inhibitors on rabbit cathepsin D maturation, Am J Physiol, 257, 1069, 10.1152/ajpcell.1989.257.6.C1069 · DOI
- Richo, 1991, Proteolytic activation of human procathepsin D, Adv Exp Med Biol, 306, 289, 10.1007/978-1-4684-6012-4_35 · DOI
- Wittlin, 1999, Mechanisms and kinetics of procathepsin D activation, Eur J Biochem, 265, 384, 10.1046/j.1432-1327.1999.00747.x · DOI
- Heinrich, 1999, Cathepsin D targeted by acid sphingomyelinase-derived ceramide, EMBO J, 18, 5252, 10.1093/emboj/18.19.5252 · DOI
- Eder, 2007, Aspartic proteases in drug discovery, Curr Pharm Des, 13, 271, 10.2174/138161207779313560 · DOI
- Vetvicka, 1993, Human breast milk contains procathepsin D-detection by specific antibodies, Biochem Mol Biol Int, 30, 921
- Larsen, 1995, Identification of five molecular forms of cathepsin D in bovine milk, Adv Exp Med Biol, 362, 279, 10.1007/978-1-4615-1871-6_32 · DOI
- Benes, 2002, Detection of procathepsin D in rat milk, Comp Biochem Physiol B Biochem Mol Biol, 133, 113, 10.1016/S1096-4959(02)00112-4 · DOI
- Zühlsdorf, 1983, Molecular forms of beta-hexosaminidase and cathepsin D in serum and urine of healthy subjects and patients with elevated activity of lysosomal enzymes, Biochem J, 213, 733, 10.1042/bj2130733 · DOI
- Baechle, 2006, Cathepsin D is present in human eccrine sweat and involved in the postsecretory processing of the antimicrobial peptide DCD-1L, J Biol Chem, 281, 5406, 10.1074/jbc.M504670200 · DOI
- Leto, 2004, Cathepsin D expression levels in nongynecological solid tumors: clinical and therapeutic implications, Clin Exp Metastasis, 21, 91, 10.1023/B:CLIN.0000024740.44602.b7 · DOI
- Laurent-Matha, 1998, Endocytosis of pro-cathepsin D into breast cancer cells is mostly independent of mannose-6-phosphate receptors, J Cell Sci, 111, 2539, 10.1242/jcs.111.17.2539 · DOI
- Laurent-Matha, 2005, Catalytically inactive human cathepsin D triggers fibroblast invasive growth, J Cell Biol, 168, 489, 10.1083/jcb.200403078 · DOI
- Poole, 1974, Cathepsin D in cartilage: the immunohistochemical demonstration of extracellular enzyme in normal and pathological conditions, J Cell Sci, 14, 139, 10.1242/jcs.14.1.139 · DOI
- Poole, 1976, Secretion and localization of cathepsin D in synovial tissues removed from rheumatoid and traumatized joints. An immunohistochemical study, Arthritis Rheum, 19, 1295, 10.1002/art.1780190610 · DOI
- Bjelle, 1976, Cathepsin D activity in bovine articular cartilage, synovial membrane and fluid: degradation of cartilage proteoglycans from same joint, J Rheumatol, 3, 400
- Vittorio, 1986, Histologic assessment of cathepsin D in osteoarthritic cartilage, Clin Exp Rheumatol, 4, 221
- Hakala, 2003, Lysosomal enzymes are released from cultured human macrophages, hydrolyze LDL in vitro, and are present extracellularly in human atherosclerotic lesions, Arterioscler Thromb Vasc Biol, 23, 1430, 10.1161/01.ATV.0000077207.49221.06 · DOI
- Vashishta, 2007, Procathepsin D secreted by HaCaT keratinocyte cells—a novel regulator of keratinocyte growth, Eur J Cell Biol, 86, 303, 10.1016/j.ejcb.2007.03.008 · DOI
- Dunn, 1995, Comparison of the active site specificity of the aspartic proteinases based on a systematic series of peptide substrates, Adv Exp Med Biol, 362, 1, 10.1007/978-1-4615-1871-6_1 · DOI
- Dunn, 2000, The two sides of enzyme-substrate specificity: lessons from the aspartic proteinases, Biochim Biophys Acta, 1477, 231, 10.1016/S0167-4838(99)00275-7 · DOI
- Bankowska, 1997, Biological and diagnostic role of cathepsin D, Rocz Akad Med Bialymst, 42, 79
- Takei, 1997, Mitogenic activity toward human breast cancer cell line MCF-7 of two bFGFs purified from sera of breast cancer patients: co-operative role of cathepsin D, Breast Cancer Res Treat, 43, 53, 10.1023/A:1005749925296 · DOI
- Morikawa, 2000, Angiostatin generation by cathepsin D secreted by human prostate carcinoma cells, J Biol Chem, 275, 38912, 10.1074/jbc.M005402200 · DOI
- Piwnica, 2004, Cathepsin D processes human prolactin into multiple 16K-like N-terminal fragments: study of their antiangiogenic properties and physiological relevance, Mol Endocrinol, 18, 2522, 10.1210/me.2004-0200 · DOI
- Lkhider, 2004, Cathepsin D released by lactating rat mammary epithelial cells is involved in prolactin cleavage under physiological conditions, J Cell Sci, 117, 5155, 10.1242/jcs.01396 · DOI
- Ferreras, 2000, Generation and degradation of human endostatin proteins by various proteinases, FEBS Lett, 486, 247, 10.1016/S0014-5793(00)02249-3 · DOI
- Baumgrass, 1997, 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, 12, 447, 10.1359/jbmr.1997.12.3.447 · DOI
- Dunn, 1991, Thyroglobulin processing by thyroidal proteases. Major sites of cleavage by cathepsins B, D, and L, J Biol Chem, 266, 20198, 10.1016/S0021-9258(18)54909-7 · DOI
- Woessner, 1971, Purification and properties of cathepsin D from bovine utrus, J Biol Chem, 246, 1951, 10.1016/S0021-9258(19)77174-9 · DOI
- Authier, 1995, Proteolysis of glucagon within hepatic endosomes by membrane-associated cathepsins B and D, J Biol Chem, 270, 15798, 10.1074/jbc.270.26.15798 · DOI
- Kudo, 1999, Proteases involved in the metabolic degradation of human interleukin-1beta by rat kidney lysosomes, J Interferon Cytokine Res, 19, 361, 10.1089/107999099314063 · DOI
- Nunn, 1997, Acid-activated insulin-like growth factor binding protein protease activity of cathepsin D in normal and malignant prostatic epithelial cells and seminal plasma, J Cell Physiol, 171, 196, 10.1002/(SICI)1097-4652(199705)171:2<196::AID-JCP10>3.0.CO;2-C · DOI
- Mordente, 1998, Hydrolysis of androgen receptor by cathepsin D: its biological significance in human prostate cancer, Br J Urol, 82, 431, 10.1046/j.1464-410X.1998.00760.x · DOI
- Diment, 1989, Cleavage of parathyroid hormone in macrophage endosomes illustrates a novel pathway for intracellular processing of proteins, J Biol Chem, 264, 13403, 10.1016/S0021-9258(18)80010-2 · DOI
- Wolf, 2003, 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, Am J Pathol, 162, 1183, 10.1016/S0002-9440(10)63914-4 · DOI
- Nishimura, 1988, Identification of latent procathepsins B and L in microsomal lumen: characterization of enzymatic activation and proteolytic processing in vitro, Arch Biochem Biophys, 261, 64, 10.1016/0003-9861(88)90104-X · DOI
- van der Stappen, 1996, Activation of cathepsin B, secreted by a colorectal cancer cell line requires low pH and is mediated by cathepsin D, Int J Cancer, 67, 547, 10.1002/(SICI)1097-0215(19960807)67:4<547::AID-IJC14>3.0.CO;2-4 · DOI
- Nishimura, 1989, Evidence that aspartic proteinase is involved in the proteolytic processing event of procathepsin L in lysosomes, Arch Biochem Biophys, 271, 400, 10.1016/0003-9861(89)90289-0 · DOI
- Egberts, 2004, Cathepsin D is involved in the regulation of transglutaminase 1 and epidermal differentiation, J Cell Sci, 117, 2295, 10.1242/jcs.01075 · DOI
- Sadik, 1999, In vitro processing of amyloid precursor protein by cathepsin D, Int J Biochem Cell Biol, 31, 1327, 10.1016/S1357-2725(99)00053-9 · DOI
- Ladror, 1994, Cleavage at the amino and carboxyl termini of Alzheimer's amyloid-beta by cathepsin D, J Biol Chem, 269, 18422, 10.1016/S0021-9258(17)32325-6 · DOI
- Kenessey, 1997, Degradation of tau by lysosomal enzyme cathepsin D: implication for Alzheimer neurofibrillary degeneration, J Neurochem, 69, 2026, 10.1046/j.1471-4159.1997.69052026.x · DOI
- Banay-Schwartz, 1983, Developmental changes in the breakdown of brain tubulin by cerebral cathepsin D, Neurochem Res, 8, 51, 10.1007/BF00965653 · DOI
- Benuck, 1975, Metabolic instability of myelin proteins. Breakdown of basic protein induced by brain cathepsin D, Eur J Biochem, 52, 615, 10.1111/j.1432-1033.1975.tb04033.x · DOI
- Kim, 2006, Lysosomal proteases are involved in generation of N-terminal huntingtin fragments, Neurobiol Dis, 22, 346, 10.1016/j.nbd.2005.11.012 · DOI
- Zhou, 2006, Cathepsin D-mediated proteolysis of apolipoprotein E: possible role in Alzheimer's disease, Neuroscience, 143, 689, 10.1016/j.neuroscience.2006.08.019 · DOI
- Takahashi, 2007, Oxidative stress-induced phosphorylation, degradation and aggregation of alpha-synuclein are linked to upregulated CK2 and cathepsin D, Eur J Neurosci, 26, 863, 10.1111/j.1460-9568.2007.05736.x · DOI
- Banay-Schwartz, 1987, The breakdown of the individual neurofilament proteins by cathepsin D, Neurochem Res, 12, 361, 10.1007/BF00993246 · DOI
- Bird, 1977, Degradation of myofibrillar proteins by cathepsins B and D, Acta Biol Med Ger, 36, 1587
- Jones, 1983, Susceptibilities of cardiac myofibrillar proteins to cathepsin D-catalyzed degradation, Am J Physiol, 245, 294
- Okitani, 1981, Purification of cathepsin D from rabbit skeletal muscle and its action towards myofibrils, Biochim Biophys Acta, 662, 202, 10.1016/0005-2744(81)90031-0 · DOI
- Simon, 1994, The fibrin(ogen)olytic properties of cathepsin D, Biochemistry, 33, 6555, 10.1021/bi00187a024 · DOI
- Loscalzo, 1996, The macrophage and fibrinolysis, Semin Thromb Hemost, 22, 503, 10.1055/s-2007-999051 · DOI
- Heinrich, 2004, Cathepsin D links TNF-induced acid sphingomyelinase to Bid-mediated caspase-9 and -3 activation, Cell Death Differ, 11, 550, 10.1038/sj.cdd.4401382 · DOI
- Haendeler, 2005, Cathepsin D and H2O2 stimulate degradation of thioredoxin-1: implication for endothelial cell apoptosis, J Biol Chem, 280, 42945, 10.1074/jbc.M506985200 · DOI
- Hiraiwa, 1997, Lysosomal proteolysis of prosaposin, the precursor of saposins (sphingolipid activator proteins): its mechanism and inhibition by ganglioside, Arch Biochem Biophys, 341, 17, 10.1006/abbi.1997.9958 · DOI
- Pimenta, 2000, Alpha1-antichymotrypsin and kallistatin hydrolysis by human cathepsin D, J Protein Chem, 19, 411, 10.1023/A:1026432402259 · DOI
- Lenarcic, 1991, Inactivation of human cystatin C and kininogen by human cathepsin D, FEBS Lett, 280, 211, 10.1016/0014-5793(91)80295-E · DOI
- van der Westhuyzen, 1980, Cathepsin-D-dependent initiation of the hydrolysis by lysosomal enzymes of apoprotein B from low-density lipoproteins, Eur J Biochem, 112, 153, 10.1111/j.1432-1033.1980.tb04996.x · DOI
- Roughley, 1977, The degradation of cartilage proteoglycans by tissue proteinases. Proteoglycan heterogeneity and the pathway of proteolytic degradation, Biochem J, 167, 639, 10.1042/bj1670639 · DOI
- Handley, 2001, Cathepsin D cleaves aggrecan at unique sites within the interglobular domain and chondroitin sulfate attachment regions that are also cleaved when cartilage is maintained at acid pH, Matrix Biol, 20, 543, 10.1016/S0945-053X(01)00168-8 · DOI
- Scott, 1978, Cathepsin D: cleavage of soluble collagen and crosslinked peptides, FEBS Lett, 88, 41, 10.1016/0014-5793(78)80602-4 · DOI
- Scott, 1981, Cathepsin D: specificity of peptide-bond cleavage in type-I collagen and effects on type-III collagen and procollagen, Eur J Biochem, 114, 59, 10.1111/j.1432-1033.1981.tb06172.x · DOI
- Tressel, 1988, Human placental fibronectin: demonstration of structural differences between the A and B chains in the extra domain-A region, Arch Biochem Biophys, 266, 639, 10.1016/0003-9861(88)90297-4 · DOI
- Hultquist, 1989, Cathepsin D in erythroid cells, Prog Clin Biol Res, 319, 93
- Kim, 1995, Cleavage of connectin by calpain and cathepsin D, Biosci Biotechnol Biochem, 59, 896, 10.1271/bbb.59.896 · DOI
- Saftig, 1995, Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells, EMBO J, 14, 3599, 10.1002/j.1460-2075.1995.tb00029.x · DOI
- Guicciardi, 2004, Lysosomes in cell death, Oncogene, 23, 2881, 10.1038/sj.onc.1207512 · DOI
- Koike, 2003, Involvement of two different cell death pathways in retinal atrophy of cathepsin D-deficient mice, Mol Cell Neurosci, 22, 146, 10.1016/S1044-7431(03)00035-6 · DOI
- Myllykangas, 2005, Cathepsin D-deficient Drosophila recapitulate the key features of neuronal ceroid lipofuscinoses, Neurobiol Dis, 19, 194, 10.1016/j.nbd.2004.12.019 · DOI
- Tyynelä, 2001, Congenital ovine neuronal ceroid lipofuscinosis—a cathepsin D deficiency with increased levels of the inactive enzyme, Eur J Paediatr Neurol, 5, 43, 10.1053/ejpn.2000.0433 · DOI
- Awano, 2006, A mutation in the cathepsin D gene (CTSD) in American Bulldogs with neuronal ceroid lipofuscinosis, Mol Genet Metab, 87, 341, 10.1016/j.ymgme.2005.11.005 · DOI
- Steinfeld, 2006, Cathepsin D deficiency is associated with a human neurodegenerative disorder, Am J Hum Genet, 78, 988, 10.1086/504159 · DOI
- Siintola, 2006, Cathepsin D deficiency underlies congenital human neuronal ceroid-lipofuscinosis, Brain, 129, 1438, 10.1093/brain/awl107 · DOI
- Partanen, 2003, A replacement of the active-site aspartic acid residue 293 in mouse cathepsin D affects its intracellular stability, processing and transport in HEK-293 cells, Biochem J, 369, 55, 10.1042/bj20021226 · DOI
- Koike, 2000, Cathepsin D deficiency induces lysosomal storage with ceroid lipofuscin in mouse CNS neurons, J Neurosci, 20, 6898, 10.1523/JNEUROSCI.20-18-06898.2000 · DOI
- Walls, 2007, Altered regulation of phosphatidylinositol 3-kinase signaling in cathepsin D-deficient brain, Autophagy, 3, 222, 10.4161/auto.3822 · DOI
- Shacka, 2007, Cathepsin D deficiency induces persistent neurodegeneration in the absence of Bax-dependent apoptosis, J Neurosci, 27, 2081, 10.1523/JNEUROSCI.5577-06.2007 · DOI
- Zhang, 2005, Correlation between inactive cathepsin D expression and retinal changes in mcd2/mcd2 transgenic mice, Invest Ophthalmol Vis Sci, 46, 3031, 10.1167/iovs.04-1510 · DOI · Paper page
- Chen, 2000, Response of keratinocytes from normal and psoriatic epidermis to interferon-gamma differs in the expression of zinc-alpha(2)-glycoprotein and cathepsin D, FASEB J, 14, 565, 10.1096/fasebj.14.3.565 · DOI
- Kawada, 1997, Processing of cathepsins L, B and D in psoriatic epidermis, Arch Dermatol Res, 289, 87, 10.1007/s004030050160 · DOI
- Kim, 1995, Expression of transglutaminase 1 in human epidermis, J Invest Dermatol, 104, 211, 10.1111/1523-1747.ep12612769 · DOI
- Negi, 1981, Mechanism of regulation of human epidermal transglutaminase, J Invest Dermatol, 77, 389, 10.1111/1523-1747.ep12494561 · DOI
- Negi, 1990, Alteration of human epidermal transglutaminase during its activation, J Dermatol Sci, 1, 167, 10.1016/0923-1811(90)90128-Z · DOI
- Steinert, 1996, Inactive zymogen and highly active proteolytically processed membrane-bound forms of the transglutaminase 1 enzyme in human epidermal keratinocytes, Biochem Biophys Res Commun, 221, 101, 10.1006/bbrc.1996.0552 · DOI
- Kim, 1998, Calpain inhibitors reduce the cornified cell envelope formation by inhibiting proteolytic processing of transglutaminase 1, Exp Mol Med, 30, 257, 10.1038/emm.1998.38 · DOI
- Bröker, 2005, Cell death independent of caspases: a review, Clin Cancer Res, 11, 3155, 10.1158/1078-0432.CCR-04-2223 · DOI
- Li, 2000, Induction of cell death by the lysosomotropic detergent MSDH, FEBS Lett, 470, 35, 10.1016/S0014-5793(00)01286-2 · DOI
- Boya, 2003, Lysosomal membrane permeabilization induces cell death in a mitochondrion-dependent fashion, J Exp Med, 197, 1323, 10.1084/jem.20021952 · DOI · Paper page
- Roberg, 1998, Oxidative stress causes relocation of the lysosomal enzyme cathepsin D with ensuing apoptosis in neonatal rat cardiomyocytes, Am J Pathol, 152, 1151
- Castino, 2007, Cathepsin D-Bax death pathway in oxidative stressed neuroblastoma cells, Free Radic Biol Med, 42, 1305, 10.1016/j.freeradbiomed.2006.12.030 · DOI
- Kagedal, 2005, Lysosomal membrane permeabilization during apoptosis-involvement of Bax?, Int J Exp Pathol, 86, 309, 10.1111/j.0959-9673.2005.00442.x · DOI
- Kagedal, 2001, Sphingosine-induced apoptosis is dependent on lysosomal proteases, Biochem J, 359, 335, 10.1042/bj3590335 · DOI
- Zhao, 2003, Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis, Eur J Biochem, 270, 3778, 10.1046/j.1432-1033.2003.03765.x · DOI
- Kolesnick, 1999, Ceramide and apoptosis, Trends Biochem Sci, 24, 224, 10.1016/S0968-0004(99)01408-5 · DOI
- Hannun, 2000, Ceramide in the eukaryotic stress response, Trends Cell Biol, 10, 73, 10.1016/S0962-8924(99)01694-3 · DOI
- De Stefanis, 2002, Increase in ceramide level alters the lysosomal targeting of cathepsin D prior to onset of apoptosis in HT-29 colon cancer cells, Biol Chem, 383, 989, 10.1515/BC.2002.106 · DOI
- Deiss, 1996, Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha, EMBO J, 15, 3861, 10.1002/j.1460-2075.1996.tb00760.x · DOI
- Roberg, 2002, Microinjection of cathepsin d induces caspase-dependent apoptosis in fibroblasts, Am J Pathol, 161, 89, 10.1016/S0002-9440(10)64160-0 · DOI
- Schestkowa, 2007, The catalytically inactive precursor of cathepsin D induces apoptosis in human fibroblasts and HeLa cells, J Cell Biochem, 101, 1558, 10.1002/jcb.21269 · DOI
- Emert-Sedlak, 2005, Involvement of cathepsin D in chemotherapy-induced cytochrome c release, caspase activation, and cell death, Mol Cancer Ther, 4, 733, 10.1158/1535-7163.MCT-04-0301 · DOI
- Wu, 1998, Potential role for cathepsin D in p53-dependent tumor suppression and chemosensitivity, Oncogene, 16, 2177, 10.1038/sj.onc.1201755 · DOI
- Trincheri, 2007, Resveratrol induces cell death in colorectal cancer cells by a novel pathway involving lysosomal cathepsin D, Carcinogenesis, 28, 922, 10.1093/carcin/bgl223 · DOI · Paper page
- Beaujouin, 2006, Overexpression of both catalytically-active and -inactive cathepsin D by cancer cells enhances apoptosis-dependent chemo-sensitivity, Oncogene, 25, 1967, 10.1038/sj.onc.1209221 · DOI
- Shibata, 1998, Participation of cathepsins B and D in apoptosis of PC12 cells following serum deprivation, Biochem Biophys Res Commun, 251, 199, 10.1006/bbrc.1998.9422 · DOI
- Roberg, 1999, Lysosomal release of cathepsin D precedes relocation of cytochrome c and loss of mitochondrial transmembrane potential during apoptosis induced by oxidative stress, Free Radic Biol Med, 27, 1228, 10.1016/S0891-5849(99)00146-X · DOI
- Kagedal, 2001, The lysosomal protease cathepsin D mediates apoptosis induced by oxidative stress, FASEB J, 15, 1592, 10.1096/fj.00-0708fje · DOI
- Tardy, 2003, Stress-induced apoptosis is impaired in cells with a lysosomal targeting defect but is not affected in cells synthesizing a catalytically inactive cathepsin D, Cell Death Differ, 10, 1090, 10.1038/sj.cdd.4401272 · DOI
- Reiners, 2002, Release of cytochrome c and activation of pro-caspase-9 following lysosomal photodamage involves Bid cleavage, Cell Death Differ, 9, 934, 10.1038/sj.cdd.4401048 · DOI
- Berchem, 2002, Cathepsin-D affects multiple tumor progression steps in vivo: proliferation, angiogenesis and apoptosis, Oncogene, 21, 5951, 10.1038/sj.onc.1205745 · DOI
- Zaidi, 2007, A novel cell penetrating aspartic protease inhibitor blocks processing and presentation of tetanus toxoid more efficiently than pepstatin A, Biochem Biophys Res Commun, 364, 243, 10.1016/j.bbrc.2007.09.114 · DOI
- Bessodes, 1999, Inhibition of cathepsin D by tripeptides containing statine analogs, Biochem Pharmacol, 58329
- Yoshida, 2006, Pepstatin A, an aspartic proteinase inhibitor, suppresses RANKL-induced osteoclast differentiation, J Biochem, 139, 583, 10.1093/jb/mvj066 · DOI
- Schotte, 1999, Non-specific effects of methyl ketone peptide inhibitors of caspases, FEBS Lett, 442, 117, 10.1016/S0014-5793(98)01640-8 · DOI
- Dash, 2003, Aspartic peptidase inhibitors: implications in drug development, Crit Rev Biochem Mol Biol, 38, 89, 10.1080/713609213 · DOI
- Selkoe, 2001, Alzheimer's disease: genes, proteins, and therapy, Physiol Rev, 81, 741, 10.1152/physrev.2001.81.2.741 · DOI · Paper page
- Cataldo, 1991, Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer disease, Proc Natl Acad Sci USA, 88, 10998, 10.1073/pnas.88.24.10998 · DOI
- Cataldo, 1990, Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain, Proc Natl Acad Sci USA, 87, 3861, 10.1073/pnas.87.10.3861 · DOI · Paper page
- Ginsberg, 2000, Expression profile of transcripts in Alzheimer's disease tangle-bearing CA1 neurons, Ann Neurol, 48, 77, 10.1002/1531-8249(200007)48:1<77::AID-ANA12>3.0.CO;2-A · DOI
- Spires, 2005, Transgenic models of Alzheimer's disease: learning from animals, NeuroRx, 2, 423, 10.1602/neurorx.2.3.423 · DOI
- Saftig, 1996, Amyloidogenic processing of human amyloid precursor protein in hippocampal neurons devoid of cathepsin D, J Biol Chem, 271, 27241, 10.1074/jbc.271.44.27241 · DOI
- Touitou, 1994, Missense polymorphism (C/T224) in the human cathepsin D pro-fragment determined by polymerase chain reaction-single strand conformational polymorphism analysis and possible consequences in cancer cells, Eur J Cancer, 30A, 390, 10.1016/0959-8049(94)90261-5 · DOI
- Masa, 2006, Cathepsin d propeptide: mechanism and regulation of its interaction with the catalytic core, Biochemistry, 45, 15474, 10.1021/bi0614986 · DOI
- Mariani, 2006, Interaction of CTSD and A2M polymorphisms in the risk for Alzheimer's disease, J Neurol Sci, 247, 187, 10.1016/j.jns.2006.05.043 · DOI
- Heun, 2004, Contribution of apolipoprotein E and cathepsin D genotypes to the familial aggregation of Alzheimer's disease, Dement Geriatr Cogn Disord, 18, 151, 10.1159/000079195 · DOI
- Papassotiropoulos, 2000, A genetic variation of cathepsin D is a major risk factor for Alzheimer's disease, Ann Neurol, 47, 399, 10.1002/1531-8249(200003)47:3<399::AID-ANA22>3.0.CO;2-5 · DOI
- Papassotiropoulos, 2002, Cerebrospinal fluid levels of beta-amyloid(42) in patients with Alzheimer's disease are related to the exon 2 polymorphism of the cathepsin D gene, Neuroreport, 13, 1291, 10.1097/00001756-200207190-00015 · DOI
- Riemenschneider, 2006, The cathepsin D rs17571 polymorphism: effects on CSF tau concentrations in Alzheimer disease, Hum Mutat, 27, 532, 10.1002/humu.20326 · DOI
- Davidson, 2006, Genetic associations between cathepsin D exon 2 C→T polymorphism and Alzheimer's disease, and pathological correlations with genotype, J Neurol Neurosurg Psychiatry, 77, 515, 10.1136/jnnp.2005.063917 · DOI · Paper page
- Ntais, 2004, Meta-analysis of the association of the cathepsin D Ala224Val gene polymorphism with the risk of Alzheimer's disease: a HuGE gene-disease association review, Am J Epidemiol, 159, 527, 10.1093/aje/kwh069 · DOI
- Lusis, 2000, Atherosclerosis, Nature, 407, 233, 10.1038/35025203 · DOI
- Duran, 2007, Atorvastatin modulates the profile of proteins released by human atherosclerotic plaques, Eur J Pharmacol, 562, 119, 10.1016/j.ejphar.2007.01.077 · DOI
- Leake, 1997, Does an acidic pH explain why low density lipoprotein is oxidised in atherosclerotic lesions?, Atherosclerosis, 129, 149, 10.1016/S0021-9150(96)06035-2 · DOI
- Tapper, 1992, Cytosolic pH regulation in mouse macrophages. Proton extrusion by plasma-membrane-localized H(+)-ATPase, Biochem J, 281, 245, 10.1042/bj2810245 · DOI
- Chen, 1991, Differences in local conformation in human apolipoprotein B-100 of plasma low density and very low density lipoproteins as identified by cathepsin D, J Biol Chem, 266, 12581, 10.1016/S0021-9258(18)98938-6 · DOI
- Chen, 1994, Conformational differences in human apolipoprotein B-100 among subspecies of low density lipoproteins (LDL). Association of altered proteolytic accessibility with decreased receptor binding of LDL subspecies from hypertriglyceridemic subjects, J Biol Chem, 269, 29121, 10.1016/S0021-9258(19)62020-X · DOI
- Björkerud, 1996, Apoptosis is abundant in human atherosclerotic lesions, especially in inflammatory cells (macrophages and T cells), and may contribute to the accumulation of gruel and plaque instability, Am J Pathol, 149, 367
- Yuan, 1997, The toxicity to macrophages of oxidized low-density lipoprotein is mediated through lysosomal damage, Atherosclerosis, 133, 153, 10.1016/S0021-9150(97)00094-4 · DOI
- Hardwick, 1996, Apoptosis in human monocyte-macrophages exposed to oxidized low density lipoprotein, J Pathol, 179, 294, 10.1002/(SICI)1096-9896(199607)179:3<294::AID-PATH590>3.0.CO;2-X · DOI
- Mitchinson, 1990, Ceroid, macrophages and atherosclerosis, Biochem Soc Trans, 18, 1066, 10.1042/bst0181066 · DOI
- Li, 1998, OxLDL-induced macrophage cytotoxicity is mediated by lysosomal rupture and modified by intralysosomal redox-active iron, Free Radic Res, 29, 389, 10.1080/10715769800300431 · DOI
- Li, 2004, Increased expression and translocation of lysosomal cathepsins contribute to macrophage apoptosis in atherogenesis, Ann N Y Acad Sci, 1030, 427, 10.1196/annals.1329.053 · DOI
- Haidar, 2006, Cathepsin D, a lysosomal protease, regulates ABCA1-mediated lipid efflux, J Biol Chem, 281, 39971, 10.1074/jbc.M605095200 · DOI
- Reid, 1986, Immunolocalization of cathepsin D in normal and neoplastic human tissues, J Clin Pathol, 39, 1323, 10.1136/jcp.39.12.1323 · DOI
- Thorpe, 1989, Association between high concentrations of Mr 52,000 cathepsin D and poor prognosis in primary human breast cancer, Cancer Res, 49, 6008
- Spyratos, 1989, Cathepsin D: an independent prognostic factor for metastasis of breast cancer, Lancet, 2, 1115, 10.1016/S0140-6736(89)91487-6 · DOI
- Ioachin, 2005, Immunohistochemical tumour markers in endometrial carcinoma, Eur J Gynaecol Oncol, 26, 363
- Cunat, 2004, Estrogens and epithelial ovarian cancer, Gynecol Oncol, 94, 25, 10.1016/j.ygyno.2004.03.026 · DOI
- Rochefort, 1999, Cathepsin D in cancer metastasis: a protease and a ligand, APMIS, 107, 86, 10.1111/j.1699-0463.1999.tb01530.x · DOI
- Mirza, 2002, Prognostic factors in node-negative breast cancer: a review of studies with sample size more than 200 and follow-up more than 5 years, Ann Surg, 235, 10, 10.1097/00000658-200201000-00003 · DOI
- Ferrandina, 1997, Relationship between cathepsin-D content and disease-free survival in node-negative breast cancer patients: a meta-analysis, Br J Cancer, 76, 661, 10.1038/bjc.1997.442 · DOI
- Foekens, 1999, Cathepsin-D in primary breast cancer: prognostic evaluation involving 2810 patients, Br J Cancer, 79, 300, 10.1038/sj.bjc.6690048 · DOI
- Billgren, 2000, The role of cathepsin D and PAI-1 in primary invasive breast cancer as prognosticators and predictors of treatment benefit with adjuvant tamoxifen, Eur J Cancer, 36, 1374, 10.1016/S0959-8049(00)00114-3 · DOI
- Rodríguez, 2005, Clinical significance of cathepsin D concentration in tumor cytosol of primary breast cancer, Int J Biol Markers, 20, 103, 10.1177/172460080502000204 · DOI
- Harris, 2007, American Society of Clinical Oncology 2007 update of recommendations for the use of tumor markers in breast cancer, J Clin Oncol, 25, 5287, 10.1200/JCO.2007.14.2364 · DOI
- Vignon, 1986, Autocrine growth stimulation of the MCF 7 breast cancer cells by the estrogen-regulated 52K protein, Endocrinology, 118, 1537, 10.1210/endo-118-4-1537 · DOI
- Fusek, 1994, Mitogenic function of human procathepsin D: the role of the propeptide, Biochem J, 303, 775, 10.1042/bj3030775 · DOI
- Vetvicka, 1994, Effect of human procathepsin D on proliferation of human cell lines, Cancer Lett, 79, 131, 10.1016/0304-3835(94)90251-8 · DOI
- Vetvicka, 1998, Effect of procathepsin D and its activation peptide on prostate cancer cells, Cancer Lett, 129, 55, 10.1016/S0304-3835(98)00091-3 · DOI
- Vetvicka, 2000, Role of procathepsin D activation peptide in prostate cancer growth, Prostate, 44, 1, 10.1002/1097-0045(20000615)44:1<1::AID-PROS1>3.0.CO;2-4 · DOI
- Bazzett, 1999, Modulation of proliferation and chemosensitivity by procathepsin D and its peptides in ovarian cancer, Gynecol Oncol, 74, 181, 10.1006/gyno.1999.5426 · DOI
- Vetvicka, 2004, Role of enzymatically inactive procathepsin D in lung cancer, Anticancer Res, 24, 2739
- Vashishta, 2006, Role of activation peptide of procathepsin D in proliferation and invasion of lung cancer cells, Anticancer Res, 26, 4163
- Glondu, 2002, Down-regulation of cathepsin-D expression by antisense gene transfer inhibits tumor growth and experimental lung metastasis of human breast cancer cells, Oncogene, 21, 5127, 10.1038/sj.onc.1205657 · DOI
- Ohri, 2007, Depletion of procathepsin D gene expression by RNA interference: a potential therapeutic target for breast cancer, Cancer Biol Ther, 6, 1081, 10.4161/cbt.6.7.4325 · DOI
- Vashishta, 2007, Ribozyme-targeting procathepsin D and its effect on invasion and growth of breast cancer cells: an implication in breast cancer therapy, Int J Oncol, 30, 1223
- Vetvicka, 1997, Analysis of the interaction of procathepsin D activation peptide with breast cancer cells, Int J Cancer, 73, 403, 10.1002/(SICI)1097-0215(19971104)73:3<403::AID-IJC15>3.0.CO;2-D · DOI
- Vetvicka, 1999, Anti-human procathepsin D activation peptide antibodies inhibit breast cancer development, Breast Cancer Res Treat, 57, 261, 10.1023/A:1006238003772 · DOI
- Gerweck, 1996, Cellular pH gradient in tumor versus normal tissue: potential exploitation for the treatment of cancer, Cancer Res, 56, 1194
- Montcourrier, 1997, Breast cancer cells have a high capacity to acidify extracellular milieu by a dual mechanism, Clin Exp Metastasis, 15, 382, 10.1023/A:1018446104071 · DOI
- Glondu, 2001, A mutated cathepsin-D devoid of its catalytic activity stimulates the growth of cancer cells, Oncogene, 20, 6920, 10.1038/sj.onc.1204843 · DOI
- Capony, 1989, Increased secretion, altered processing, and glycosylation of pro-cathepsin D in human mammary cancer cells, Cancer Res, 49, 3904
- Maguchi, 1988, Elevated activity and increased mannose-6-phosphate in the carbohydrate moiety of cathepsin D from human hepatoma, Cancer Res, 48, 362
- Mathieu, 1990, Interactions of cathepsin-D and insulin-like growth factor-II (IGF-II) on the IGF-II/mannose-6-phosphate receptor in human breast cancer cells and possible consequences on mitogenic activity of IGF-II, Mol Endocrinol, 4, 1327, 10.1210/mend-4-9-1327 · DOI
- Vignon, 1992, Interactions of pro-cathepsin D and IGF-II on the mannose-6-phosphate/IGF-II receptor, Breast Cancer Res Treat, 22, 47, 10.1007/BF01833333 · DOI
- Vetvicka, 2002, Procathepsin D in breast cancer: what do we know? Effects of ribozymes and other inhibitors, Cancer Gene Ther, 9, 854, 10.1038/sj.cgt.7700508 · DOI
- Ohri, 2008, The propeptide of cathepsin D increases proliferation, invasion and metastasis of breast cancer cells, Int J Oncol, 32, 491
- Baldwin, 1993, Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design, Proc Natl Acad Sci USA, 90, 6796, 10.1073/pnas.90.14.6796 · DOI
- Metcalf, 1993, Two crystal structures for cathepsin D: the lysosomal targeting signal and active site, EMBO J, 12, 1293, 10.1002/j.1460-2075.1993.tb05774.x · DOI
- Koelsch, 1995, Human procathepsin D: three-dimensional model and isolation, Adv Exp Med Biol, 362, 273, 10.1007/978-1-4615-1871-6_31 · DOI
- Garcia, 1990, Overexpression of transfected cathepsin D in transformed cells increases their malignant phenotype and metastatic potency, Oncogene, 5, 1809
- Tedone, 1997, Release of the aspartyl protease cathepsin D is associated with and facilitates human breast cancer cell invasion, FASEB J, 11, 785, 10.1096/fasebj.11.10.9271363 · DOI
- Sivaparvathi, 1996, Expression of cathepsin D during the progression of human gliomas, Neurosci Lett, 208, 171, 10.1016/0304-3940(96)12584-2 · DOI
- Lösch, 2004, Cathepsin D in ovarian cancer: prognostic value and correlation with p53 expression and microvessel density, Gynecol Oncol, 92, 545, 10.1016/j.ygyno.2003.11.016 · DOI
- González-Vela, 1999, Cathepsin D in host stromal cells is associated with more highly vascular and aggressive invasive breast carcinoma, Histopathology, 34, 35, 10.1046/j.1365-2559.1999.00548.x · DOI
200 of 212 shown
Cited by
Sorted by citations
Roca, F. J., Whitworth, L. J., Redmond, S., Jones, A. A., & Ramakrishnan, L. (2019) · Cell · doi:10.1016/j.cell.2019.08.004 · Cited by 233
Degradation of engulfed mitochondria is rate-limiting in Optineurin-mediated mitophagy in neurons
Evans, C. S., & Holzbaur, E. L. (2020) · eLife · doi:10.7554/elife.50260 · Cited by 137
Di Domenico, F., Barone, E., Perluigi, M., & Butterfield, D. A. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6759 · Cited by 114
The propeptide of yeast cathepsin D inhibits programmed necrosis
Carmona-Gutiérrez, D., Bauer, M. A., Ring, J., Knauer, H., Eisenberg, T., Büttner, S., Ruckenstuhl, C., Reisenbichler, A., Magnes, C., Rechberger, G. N., et al. (2011) · Cell Death & Disease · doi:10.1038/cddis.2011.43 · Cited by 69
Cathepsin D in Podocytes Is Important in the Pathogenesis of Proteinuria and CKD
Yamamoto-Nonaka, K., Koike, M., Asanuma, K., Takagi, M., Oliva Trejo, J. A., Seki, T., Hidaka, T., Ichimura, K., Sakai, T., Tada, N., et al. (2016) · Journal of the American Society of Nephrology · doi:10.1681/asn.2015040366 · Cited by 59
Di Domenico, F., Head, E., Butterfield, D. A., & Perluigi, M. (2014) · Advances in Geriatrics · doi:10.1155/2014/527518 · Cited by 50
The neuronal retromer can regulate both neuronal and microglial phenotypes of Alzheimer's disease
Qureshi, Y. H., Berman, D. E., Marsh, S. E., Klein, R. L., Patel, V. M., Simoes, S., Kannan, S., Petsko, G. A., Stevens, B., & Small, S. A. (2022) · Cell Reports · doi:10.1016/j.celrep.2021.110262 · Cited by 31
The extracellular matrix phenome across species
Statzer, C., & Ewald, C. Y. (2020) · Matrix Biology Plus · doi:10.1016/j.mbplus.2020.100039 · Cited by 21
Loss of melanoregulin (MREG) enhances cathepsin-D secretion by the retinal pigment epithelium
FROST, L. S., LOPES, V. S., STEFANO, F. P., BRAGIN, A., WILLIAMS, D. S., MITCHELL, C. H., & BOESZE-BATTAGLIA, K. (2013) · Visual Neuroscience · doi:10.1017/s0952523813000096 · Cited by 9
Metadata
- Authors
- Benes, P., Vetvicka, V., & Fusek, M.
- Venue
- Critical Reviews in Oncology/Hematology
- Publisher
- Elsevier BV
- Published
- 2008-10
- Volume
- 68
- Issue
- 1
- Pages
- 12-28
- ISSN
- 1040-8428
- Cited by
- 572
- References
- 8
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review