Elevated Levels of the Endosomal‐Lysosomal Proteinase Cathepsin D in Cerebrospinal Fluid in Alzheimer Disease
Abstract
Lysosomal hydrolases are normally intracellular enzymes but are abundant extracellularly within senile plaques in Alzheimer disease and in other conditions where beta-amyloid accumulates. To examine whether acid hydrolases released from abnormal hydrolase-laden neurons are detectable in CSF, we measured levels of the major aspartic proteinase of lysosomes, cathepsin D (Cat D), in ventricular CSF collected after death from 30 patients with Alzheimer disease, 14 patients with Huntington disease, and seven patients with other neurodegenerative diseases. The levels of Cat D-immunoreactive protein, expressed as micrograms per milliliter of protein, determined by western blot immunoassay using a polyclonal antiserum against human brain Cat D, were more than fourfold higher in the Alzheimer patients than in the other patient groups (p < 0.0005). Cat D activity, assayed separately against [14C]methemoglobin at pH 3.2, was also significantly elevated but less than Cat D content. The lower specific activity of Cat D in Alzheimer CSF therefore indicated that the abnormally accumulated Cat D included a high proportion of inactive enzyme. These results indicate that abnormal Cat D release from affected neurons into the extracellular space is an active, ongoing process in Alzheimer brain. In addition, the levels of this enzyme and possibly other lysosomal hydrolases in CSF may prove to be useful biological markers of Alzheimer disease.
Integrity signals
Registry
Cites
Statistics
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?
Ventricular CSF obtained postmortem from AD patients has substantially elevated levels of CTSD with markedly lowered specific activity compared with CSF from individuals with Huntington's disease or from non-neurologic disease controls.
“we previously reported that ventricular CSF obtained postmortem from AD patients has substantially elevated levels of CTSD with markedly lowered specific activity compared with CSF from individuals with Huntington's disease or from non-neurologic disease controls (Schwagerl et al., 1995).”
From Lysosomal Dysfunction in Down Syndrome Is APP-Dependent and Mediated by APP-βCTF (C99) (2019) · cites this paper as Schwagerl et al., 1995
Cites
Still being checked.
Cited by
Sorted by citations
Cathepsin D—Many functions of one aspartic protease
Beneš, P., Větvička, V., & Fusek, M. (2008) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2008.02.008 · Cited by 640 · see citing works
Altered lysosomal proteins in neural-derived plasma exosomes in preclinical Alzheimer disease
Goetzl, E. J., Boxer, A. L., Schwartz, J. B., Abner, E. L., Petersen, R. C., Miller, B. L., & Kapogiannis, D. (2015) · Neurology · doi:10.1212/wnl.0000000000001702 · Cited by 466 · see citing works
The Endosomal-Lysosomal System of Neurons in Alzheimer's Disease Pathogenesis: A Review
Nixon, R., Cataldo, A., & Mathews, P. (2000) · Neurochemical Research · doi:10.1023/a:1007675508413 · Cited by 332 · see citing works
Self-citationPasternak, S., Bagshaw, R. D., Guiral, M., Zhang, S., Ackerley, C. A., Pak, B. J., Callahan, J. W., & Mahuran, D. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304009200 · Cited by 314 · see citing works
Tau in cerebrospinal fluid: A potential diagnostic marker in Alzheimer's disease
Arai, H., Terajima, M., Miura, M., Higuchi, S., Muramatsu, T., Machida, N., Seiki, H., Takase, S., Clark, C., Lee, V. M., et al. (1995) · Annals of Neurology · doi:10.1002/ana.410380414 · Cited by 314 · see citing works
Autophagy in neurons: a review.
Larsen, K. E., & Sulzer, D. L. (2002) · PubMed · doi:10.14670/hh-17.897 · Cited by 242 · see citing works
MCDERMOTT, J. R., & GIBSON, A. M. (1997) · Neurochemical Research · doi:10.1023/a:1027325304203 · Cited by 184 · see citing works
Lysosomal Dysfunction and α‐Synuclein Aggregation in Parkinson's Disease: Diagnostic Links
Moors, T. E., Paciotti, S., Chiasserini, D., Calabresi, P., Parnetti, L., Beccari, T., & van de Berg, W. D. J. (2016) · Movement Disorders · doi:10.1002/mds.26562 · Cited by 175 · see citing works
Lysosomal Dysfunction in Down Syndrome Is APP-Dependent and Mediated by APP-βCTF (C99)
Jiang, Y., Sato, Y., Im, E., Berg, M., Bordi, M., Darji, S., Kumar, A., Mohan, P. S., Bandyopadhyay, U., Diaz, A., et al. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.0578-19.2019 · Cited by 166 · see citing works
Self-citationSubcellular Topography of Neuronal Aβ Peptide in APPxPS1 Transgenic Mice
Langui, D., Girardot, N., El Hachimi, K. H., Allinquant, B., Blanchard, V., Pradier, L., & Duyckaerts, C. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63405-0 · Cited by 165 · see citing works
The Role of Cathepsin D in the Pathogenesis of Human Neurodegenerative Disorders
Vidoni, C., Follo, C., Savino, M., Melone, M. A. B., & Isidoro, C. (2016) · Medicinal Research Reviews · doi:10.1002/med.21394 · Cited by 164 · see citing works
Colacurcio, D. J., Pensalfini, A., Jiang, Y., & Nixon, R. A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.10.001 · Cited by 167 · see citing works
Self-citationProteome profiling of cerebrospinal fluid reveals biomarker candidates for Parkinson’s disease
Karayel, Ö., Winter, S. V., Padmanabhan, S., Kuras, Y. I., Vu, D. T., Tuncali, I., Merchant, K., Wills, A.-M. A., Scherzer, C. R., & Mann, M. (2022) · Cell Reports Medicine · doi:10.1016/j.xcrm.2022.100661 · Cited by 158 · see citing works
Endo‐lysosomal and autophagic dysfunction: a driving factor in Alzheimer's disease?
Whyte, L. S., Lau, A. A., Hemsley, K. M., Hopwood, J. J., & Sargeant, T. J. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.13935 · Cited by 150 · see citing works
Pasternak, S., Callahan, J., & Mahuran, D. (2003) · Journal of Alzheimer's Disease · doi:10.3233/jad-2004-6107 · Cited by 129 · see citing works
Wang, H., Robinson, J. L., Kocabaş, P., Gustafsson, J., Anton, M., Cholley, P., Huang, S., Gobom, J., Svensson, T., Uhlén, M., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2102344118 · Cited by 113 · see citing works
Lysosomal Network Proteins as Potential Novel CSF Biomarkers for Alzheimer’s Disease
Armstrong, A., Mattsson, N., Appelqvist, H., Janefjord, C., Sandin, L., Agholme, L., Olsson, B., Svensson, S., Blennow, K., Zetterberg, H., et al. (2013) · NeuroMolecular Medicine · doi:10.1007/s12017-013-8269-3 · Cited by 111 · see citing works
The neuronal endosomal-lysosomal system in Alzheimer's disease
Nixon, R. A., Mathews, P. M., & Cataldo, A. M. (2001) · Journal of Alzheimer s Disease · doi:10.3233/jad-2001-3114 · Cited by 111 · see citing works
Self-citationReconsider Alzheimer's disease by the ‘calpain–cathepsin hypothesis’—A perspective review
Yamashima, T. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.02.004 · Cited by 107 · see citing works
Mathews, P. M., Guerra, C. B., Jiang, Y., Grbovic, O. M., Kao, B. H., Schmidt, S. D., Dinakar, R., Mercken, M. H., Hille‐Rehfeld, A., Rohrer, J., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108161200 · Cited by 103 · see citing works
Self-citationSäftig, P., Peters, C., FIGURA, K. V., Craessaerts, K., LEUVEN, F. V., & Strooper, B. D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27241 · Cited by 95 · see citing works
Lescuyer, P., Allard, L., Zimmermann‐Ivol, C. G., Burgess, J., Frutiger, S., Burkhard, P. R., Sanchez, J., & Hochstrasser, D. F. (2004) · PROTEOMICS · doi:10.1002/pmic.200300822 · Cited by 96 · see citing works
Cluzeau, C. V. M., Watkins‐Chow, D. E., Fu, R., Borate, B. R., Yanjanin, N. M., Dail, M. K., Davidson, C. D., Walkley, S. U., Ory, D. S., Wassif, C. A., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds193 · Cited by 93 · see citing works
Drobny, A., Huarcaya, S. P., Dobert, J., Kluge, A., Bunk, J., Schlothauer, T., & Zunke, F. (2022) · Biochimica et biophysica acta. Molecular cell research · doi:10.1016/j.bbamcr.2022.119243 · Cited by 86 · see citing works
Preserving Lysosomal Function in the Aging Brain: Insights from Neurodegeneration
Peng, W., Minakaki, G., Nguyen, M., & Krainc, D. (2019) · Neurotherapeutics · doi:10.1007/s13311-019-00742-3 · Cited by 79 · see citing works
The role of Alzheimer's disease risk genes in endolysosomal pathways
Szabo, M. P., Mishra, S., Knupp, A., & Young, J. E. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105576 · Cited by 81 · see citing works
Exosome Production Is Key to Neuronal Endosomal Pathway Integrity in Neurodegenerative Diseases
Mathews, P., & Levy, E. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01347 · Cited by 73 · see citing works
Cathepsin D displays in vitro β-secretase-like specificity
Chevallier, N., Vizzavona, J., Marambaud, P., Baur, C.-P., Spillantini, M. G., Fulcrand, P., Martínez, J., Goedert, M., Vincent, J., & Checler, F. (1997) · Brain Research · doi:10.1016/s0006-8993(96)01330-3 · Cited by 78 · see citing works
Chen, L., Liu, W., Lin, H., Lin, M., Yu, Y., Liu, H., Dai, Y., Chen, L.-W., Jia, W., He, X., et al. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.335832 · Cited by 74 · see citing works
The possible place of cathepsins and cystatins in the puzzle of Alzheimer disease
Bernstein, H., Kirschke, H., Wiederanders, B., Kh, P., Zipress, A., & Rinne, A. (1996) · Molecular and Chemical Neuropathology · doi:10.1007/bf02815106 · Cited by 70 · see citing works
Autophagy Modulation as a Treatment of Amyloid Diseases
Mputhia, Z., Hone, E., Tripathi, T., Sargeant, T. J., Martins, R. N., & Bharadwaj, P. (2019) · Molecules · doi:10.3390/molecules24183372 · Cited by 69 · see citing works
Cathepsin D expression is decreased in Alzheimer's disease fibroblasts
Urbanelli, L., Emiliani, C., Massini, C., Persichetti, E., Orlacchio, A., Pelicci, G., Sorbi, S., Hasilík, A., Bernardi, G., & Orlacchio, A. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.09.005 · Cited by 64 · see citing works
Soreghan, B. A., Thomas, S. N., & Yang, A. J. (2003) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2003.07.007 · Cited by 62 · see citing works
Differential expression of cathepsin X in aging and pathological central nervous system of mice
Wendt, W., Zhu, X., Lübbert, H., & Stichel, C. C. (2007) · Experimental Neurology · doi:10.1016/j.expneurol.2007.01.007 · Cited by 62 · see citing works
Protective properties of lysozyme on β-amyloid pathology: implications for Alzheimer disease
Helmfors, L., Boman, A., Civitelli, L., Nath, S., Sandin, L., Janefjord, C., McCann, H., Zetterberg, H., Blennow, K., Halliday, G. M., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.08.024 · Cited by 61 · see citing works
Cathepsin D gene and the risk of Alzheimer's disease: A population-based study and meta-analysis
Schuur, M., Ikram, M. A., Swieten, J. C. V., Isaacs, A. J., Vergeer, J. M., Albert Hofman, D., Oostra, B. A., Breteler, M. M. B., & van Duijn, C. M. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.10.011 · Cited by 60 · see citing works
Hippocampal Endosomal, Lysosomal, and Autophagic Dysregulation in Mild Cognitive Impairment
Perez, S. E., He, B., Nadeem, M., Wuu, J., Ginsberg, S. D., Ikonomović, M. D., & Mufson, E. J. (2015) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000179 · Cited by 57 · see citing works
Bi, X., Zhou, J., & LYNCH, G. S. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7087 · Cited by 57 · see citing works
Potential neurotoxic activity of diverse molecules released by microglia
Lindhout, I. A., Murray, T. E., Richards, C. M., & Klegeris, A. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105117 · Cited by 56 · see citing works
Esteves, A. R., & Cardoso, S. M. (2020) · Scientific Reports · doi:10.1038/s41598-020-70174-z · Cited by 55 · see citing works
Relevance of Autophagy and Mitophagy Dynamics and Markers in Neurodegenerative Diseases
Giorgi, C., Bouhamida, E., Danese, A., Previati, M., Pinton, P., & Patergnani, S. (2021) · Biomedicines · doi:10.3390/biomedicines9020149 · Cited by 50 · see citing works
Suchý, M., Ta, R. M., Li, A. X., Wojciechowski, F., Pasternak, S., Bartha, R., & Hudson, R. H. E. (2010) · Organic & Biomolecular Chemistry · doi:10.1039/b926639a · Cited by 47 · see citing works
Liu, J., Hong, Z., Ding, J., Liu, J., Zhang, J., & Chen, S. (2008) · Journal of Proteome Research · doi:10.1021/pr7007779 · Cited by 41 · see citing works
Bridging the Gap Between Fluid Biomarkers for Alzheimer’s Disease, Model Systems, and Patients
Bjorkli, C., Sandvig, A., & Sandvig, I. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00272 · Cited by 41 · see citing works
Identification of Cathepsin D as a Plasma Biomarker for Alzheimer’s Disease
Kim, J.-W., Jung, S.-Y., Kim, Y., Heo, H., Hong, C., Seo, S.-W., Choi, S.-H., Son, S., Lee, S., & Chang, J. (2021) · Cells · doi:10.3390/cells10010138 · Cited by 40 · see citing works
Fruitier‐Arnaudin, I., Garreau-Balandier, I., Lacroix, A., Cupo, A., & Piot, J. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00271-9 · Cited by 40 · see citing works
Proteome analysis of cerebrospinal fluid in Guillain–Barré syndrome (GBS)
Lehmensiek, V., Süßmuth, S. D., Brettschneider, J., Tauscher, G., Felk, S., Gillardon, F., & Tumani, H. (2007) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2007.01.022 · Cited by 38 · see citing works
Abnormalities of the Endosomal-Lysomal System in Alzheimer’s disease
Cataldo, A. M., Hamilton, D. J., Barnett, J. L., Paskevich, P. A., & Nixon, R. A. (1996) · Advances in experimental medicine and biology · doi:10.1007/978-1-4613-0335-0_34 · Cited by 37 · see citing works
Self-citationLysosomes and Brain Aging in Mammals
LYNCH, G. S., & Bi, X. (2003) · Neurochemical Research · doi:10.1023/a:1026069223763 · Cited by 36 · see citing works
Maarouf, C. L., Andacht, T. M., Kokjohn, T. A., Castaño, E. M., Sue, L. I., Beach, T. G., & Roher, A. E. (2009) · Current Alzheimer Research · doi:10.2174/156720509788929318 · Cited by 34 · see citing works
The Role of Oxidized Cholesterol in Diabetes-Induced Lysosomal Dysfunction in the Brain
Sims‐Robinson, C., Bakeman, A., Rosko, A. J., Glasser, R., & Feldman, E. L. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9207-1 · Cited by 33 · see citing works
Enhanced GM1 ganglioside catabolism in cultured fibroblasts from Alzheimer patients
Pitto, M., Raimondo, F., Zoia, C., Brighina, L., Ferrarese, C., & Masserini, M. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.07.006 · Cited by 31 · see citing works
The Cathepsin D rs17571 polymorphism: effects on CSF tau concentrations in Alzheimer disease
Riemenschneider, M. J., Blennow, K., Wagenpfeil, S., Andreasen, N., Prince, J. A., Laws, S. M., Förstl, H., & Kurz, A. (2006) · Human Mutation · doi:10.1002/humu.20326 · Cited by 30 · see citing works
Trojanowski, J. Q., Clark, C. M., Arai, H., & Lee, V. M. ‐. (1999) · Journal of Alzheimer s Disease · doi:10.3233/jad-1999-14-510 · Cited by 30 · see citing works
Wang, Y., Wu, Q., Anand, B. G., Karthivashan, G., Phukan, G., Yang, J., Thinakaran, G., Westaway, D. A., & Kar, S. (2020) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12647 · Cited by 28 · see citing works
Liu, X., Baxley, S., Hebron, M. L., Turner, R. S., & Moussa, C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26115044 · Cited by 29 · see citing works
Lysosomal peptidases—intriguing roles in cancer progression and neurodegeneration
Kos, J., Mitrović, A., Nanut, M. P., & Pišlar, A. H. (2022) · FEBS Open Bio · doi:10.1002/2211-5463.13372 · Cited by 28 · see citing works
Gene Expression of Proteases and Protease Inhibitors in the Human Ciliary Epithelium and ODM-2 Cells
Ortego, J., Escribano, J., & Coca‐Prados, M. (1997) · Experimental Eye Research · doi:10.1006/exer.1997.0333 · Cited by 28 · see citing works
The Alzheimer's Disease Gene SORL1 Regulates Lysosome Function in Human Microglia
Mishra, S., Morshed, N., Sidhu, S. B., Kinoshita, C., Stevens, B., Jayadev, S., & Young, J. E. (2025) · Glia · doi:10.1002/glia.70009 · Cited by 29 · see citing works
Factors Influencing the Measurement of Lysosomal Enzymes Activity in Human Cerebrospinal Fluid
Persichetti, E., Chiasserini, D., Parnetti, L., Eusebi, P., Paciotti, S., Carlo, C. D., Codini, M., Tambasco, N., Rossi, A., El‐Agnaf, O. M. A., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101453 · Cited by 27 · see citing works
Pleiotropic Effects of Cathepsin D
Vashishta, A., Ohri, S. S., & Větvička, V. (2009) · Endocrine Metabolic & Immune Disorders - Drug Targets · doi:10.2174/187153009789839174 · Cited by 25 · see citing works
β-Amyloid increases cathepsin D levels in hippocampus
Hoffman, K. B., Bi, X., Pham, J. T., & LYNCH, G. S. (1998) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00364-4 · Cited by 25 · see citing works
Focusing on cellular biomarkers: The endo-lysosomal pathway in Down syndrome.
Botté, A., & Potier, M. (2020) · Progress in Brain Research · doi:10.1016/bs.pbr.2019.10.002 · Cited by 20 · see citing works
Non-replication of association between cathepsin D genotype and late onset Alzheimer disease
Menzer, G., Müller‐Thomsen, T., Meins, W., Alberici, A., Binetti, G. G., Höck, C., Nitsch, R. M., Stoppe, G., Reiss, J., & Finckh, U. (2001) · American Journal of Medical Genetics · doi:10.1002/ajmg.1204 · Cited by 24 · see citing works
Lysosomal enzyme activities as possible CSF biomarkers of synucleinopathies
Paciotti, S., Gatticchi, L., Beccari, T., & Parnetti, L. (2019) · Clinica Chimica Acta · doi:10.1016/j.cca.2019.03.1627 · Cited by 23 · see citing works
Marshall, A. C., Shaltout, H. A., Pirro, N. T., Rose, J. C., Diz, D. I., & Chappell, M. C. (2013) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00321.2013 · Cited by 22 · see citing works
Wagner, L., Björkqvist, M., Lundh, S. H., Wolf, R., Börgel, A., Schlenzig, D., Ludwig, H., Rahfeld, J., Leavitt, B. R., Demuth, H., et al. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13624 · Cited by 21 · see citing works
Link between neurodegeneration and trabecular meshwork injury in glaucomatous patients
Zhang, Y., Yang, Q., Guo, F., Chen, X., & Xie, L. (2017) · BMC Ophthalmology · doi:10.1186/s12886-017-0623-z · Cited by 20 · see citing works
A dual magnetic resonance imaging/fluorescent contrast agent for Cathepsin‐D detection
Ta, R. M., Suchý, M., Tam, J. H. K., Li, A. X., Martínez‐Santiesteban, F., Scholl, T. J., Hudson, R. H. E., Bartha, R., & Pasternak, S. (2012) · Contrast Media & Molecular Imaging · doi:10.1002/cmmi.1502 · Cited by 17 · see citing works
Lysosomal Dysfunction Reduces Brain-Derived Neurotrophic Factor Expression
Bednarski, E., Lauterborn, J. C., Gall, C. M., & LYNCH, G. S. (1998) · Experimental Neurology · doi:10.1006/exnr.1997.6747 · Cited by 16 · see citing works
Cheng, S., Wani, W. Y., Hottman, D. A., Jeong, A., Cao, D., LeBlanc, K. J., Säftig, P., Zhang, J., & Li, L. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14048 · Cited by 15 · see citing works
Thompson, A., Grueninger‐Leitch, F., Huber, G., & Malherbe, P. (1997) · Molecular Brain Research · doi:10.1016/s0169-328x(97)00091-0 · Cited by 15 · see citing works
Isoform- and cell-state-specific APOE homeostasis and function
Lindner, K., & Gavin, A.-C. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01470 · Cited by 13 · see citing works
Targeted proteolytic products of τ and α-synuclein in neurodegeneration
Xia, Y., Lloyd, G. M., & Giasson, B. I. (2021) · Essays in Biochemistry · doi:10.1042/ebc20210028 · Cited by 13 · see citing works
Snir, J. A., Suchý, M., Lawrence, K. S., Hudson, R. H. E., Pasternak, S., & Bartha, R. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150123 · Cited by 12 · see citing works
dos Reis, B. G., Becker, G. S., Marchetti, D. P., Coelho, D. D. M., Sitta, Â., Wajner, M., & Vargas, C. R. (2024) · Metabolic Brain Disease · doi:10.1007/s11011-024-01475-9 · Cited by 11 · see citing works
An Aspartyl Cathepsin Targeted PET Agent: Application in an Alzheimer’s Disease Mouse Model
Snir, J. A., Suchý, M., Bindseil, G. A., Kovacs, M. S., Chronik, B. A., Hudson, R. H. E., Pasternak, S., & Bartha, R. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170115 · Cited by 10 · see citing works
Some Remarks on Biological Markers of Alzheimer’s Disease
Robles, A. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00011-6 · Cited by 9 · see citing works
Serum Cathepsin D Is a Potential Biomarker for Alzheimer’s Disease Dementia and Cognitive Decline
Chai, Y. L., Liang, N. H. P., Chong, J. R., Venketasubramanian, N., Tan, B. Y., Hilal, S., Chen, C., & Lai, M. K. P. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220852 · Cited by 9 · see citing works
Marshall, K. E., Mengham, K., Spink, M. C., Vania, L., Pollard, H. J., Darrow, M. C., Duke, E., Harkiolaki, M., & Serpell, L. C. (2024) · Structure · doi:10.1016/j.str.2024.02.010 · Cited by 8 · see citing works
Origin of α-mannosidase activity in CSF
Tasegian, A., Paciotti, S., Ceccarini, M. R., Codini, M., Moors, T. E., Chiasserini, D., Albi, E., WINCHESTER, B. G., van de Berg, W. D. J., Parnetti, L., et al. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.03.016 · Cited by 8 · see citing works
Compaine, A. (1995) · Neurochemistry International · doi:10.1016/0197-0186(95)00020-9 · Cited by 8 · see citing works
Swift, I. J., Sjödin, S., Gobom, J., Brinkmalm, A., Blennow, K., Zetterberg, H., Rohrer, J. D., & Sogorb‐Esteve, A. (2023) · Journal of Neurology · doi:10.1007/s00415-023-12063-9 · Cited by 6 · see citing works
Kluger, A., Golomb, J. B., & Ferris, S. H. (2003) · doi:10.1002/9780470752340.ch25 · Cited by 6 · see citing works
Lázaro, S. P., Barrio, T., Bravo, S. B., Sevilla, E., Otero, A., Chantada‐Vázquez, M. D. P., Martín‐Burriel, I., Requena, J. R., Badiola, J. J., & Bolea, R. (2024) · Veterinary Quarterly · doi:10.1080/01652176.2024.2424837 · Cited by 4 · see citing works
Single-Column Purification of Syncephapepsin—An Aspartic Proteinase fromSyncephalastrum racemosum
Ho, H.-C., Shiau, P., & Wu, S. (1998) · Protein Expression and Purification · doi:10.1006/prep.1997.0842 · Cited by 4 · see citing works
Rösler, N., Wichart, I., & Jellinger, K. A. (2002) · Journal of Laboratory Medicine · doi:10.1515/labmed.2002.019 · Cited by 3 · see citing works
Peripheral Markers of Alzheimer’s
Percy, M. E., Andrews, D. F., & Potter, H. (2000) · Humana Press eBooks · doi:10.1007/978-1-59259-005-6_9 · Cited by 3 · see citing works
Zhao, S., Liu, X., Wu, S., Zheng, Y., & Zhang, W. (2019) · Gynecological Endocrinology · doi:10.1080/09513590.2019.1696302 · Cited by 2 · see citing works
Immunohistochemical study of microscopic globular bodies of normal human brain
Odagiri, S., Mori, F., Tanji, K., Kuroda, N., & Wakabayashi, K. (2011) · Biomedical Research · doi:10.2220/biomedres.32.337 · Cited by 2 · see citing works
Neuronal degenerative mechanisms as clues to pathogenesis and treatment of Alzheimer's disease
Nixon, R. A. (1994) · Neurobiology of Aging · doi:10.1016/0197-4580(94)90172-4 · Cited by 2 · see citing works
Self-citation[Tau protein in cerebrospinal fluid--a potential marker of Alzheimer's disease].
Arai, H., Satoh, K., Terajima, M., Nakagawa, T., Higuchi, M., Kosaka, Y.-I., Zhu, C.-Q., & Sasaki, H. (1996) · Nihon Ronen Igakkai zasshi. Japanese journal of geriatrics · doi:10.3143/geriatrics.33.669 · Cited by 2 · see citing works
Masson, L.-C., Kanagasabai, A. S., Toscano‐Márquez, B., Tourbina-Kolomiets, J., Charron, F. M., Watt, A. J., & McKinney, R. A. (2025) · The Cerebellum · doi:10.1007/s12311-025-01850-x · Cited by 1 · see citing works
Duckhorn, J. C., Kim, D. K., & Huang, Y. A. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-00243 · Cited by 2 · see citing works
Chevallier, N., Marambaud, P., Vincent, J., Checler, F., Vizzavona, J., Fulcrand, P., Martínez, J., Baur, C.-P., Spillantini, M. G., & Goedert, M. (1997) · Birkhäuser Boston eBooks · doi:10.1007/978-1-4612-4116-4_11 · Cited by 1 · see citing works
Genetic Determinants of Cognitive Function and Age-Related Brain Changes
Schuur, M. (2010) · RePub (Erasmus University Rotterdam)
Rational design and synthesis of conformationally constrained inhibitors of human cathepsin D
Majer, P., Collins, J., Pan, W., Gulnik, S., Lee, A. Y., Gustchina, E., & Erickson, J. W. (2005) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-46862-x_293
Review Autophagy in neurons: a review
Larsen, K. E., & Sulzer, D. L. (2002)
Cathepsin D Deficiency : Molecular and Cellular Mechanisms of Neurodegeneration
Partanen, S. (2006) · Työväentutkimus Vuosikirja
CELLULAR MECHANISMS OF NEURODEGENERATION
Partanen, S. (2006)
- Authors
- Schwagerl, A. L., Mohan, P. S., Cataldo, A. M., Vonsattel, J. P., Kowall, N. W., & Nixon, R. A.
- Affiliations
- Georgetown University (US)
- McLean Hospital (US)
- Harvard University (US)
- United States Department of Veterans Affairs (US)
- Corresponding author
- Nixon, R. A.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 1995-01
- Volume
- 64
- Issue
- 1
- Pages
- 443-446
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W1974250737
- Cited by
- 107
- References
- 0
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 4 · 2023: 1 · 2022: 6 · 2021: 6 · 2020: 3 · 2019: 7 · 2018: 1 · 2017: 4 · 2016: 5 · 2015: 5 · 2014: 1 · 2013: 4 · 2012: 3
- FWCI
- 3.32
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r35ag010916-08, 5r01mh031862-24)
- National Institute on Aging (AG 10916)
- National Institute of Mental Health (MH31862)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Cerebrospinal fluid and hydrocephalus
- Keywords
- cathepsin D, Alzheimer's disease, cerebrospinal fluid, lysosomal enzymes, aspartic protease, amyloid plaques, amyloid-beta, Huntington's disease, neurodegenerative diseases, enzyme activity, biomarkers
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Cathepsins, Female, Humans, Huntington Disease, Lysosomes, Male, Middle Aged, Endosomes, Blotting, Western
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