Cited by 107Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchCerebrospinal fluid and hydrocephalus

The DOI matches its Crossref record.

Elevated Levels of the Endosomal‐Lysosomal Proteinase Cathepsin D in Cerebrospinal Fluid in Alzheimer Disease

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

Open this paper in CoChat — free account

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

Crossref · 10.1046/j.1471-4159.1995.64010443.x

Cites

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Still being checked.

Sorted by citations

Cathepsin D--many functions of one aspartic protease
Benes, P., Vetvicka, V., & Fusek, M. (2008) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2008.02.008 · Cited by 572
Altered lysosomal proteins in neural-derived plasma exosomes in preclinical Alzheimer disease
Goetzl, E. J., Boxer, A., Schwartz, J. B., Abner, E. L., Petersen, R. C., Miller, B. L., & Kapogiannis, D. (2015) · Neurology · doi:10.1212/wnl.0000000000001702 · Cited by 446
The Endosomal-Lysosomal System of Neurons in Alzheimer's Disease Pathogenesis: A Review
Nixon, R. A., Cataldo, A. M., & Mathews, P. M. (2000) · Neurochemical Research · doi:10.1023/a:1007675508413 · Cited by 320
Self-citation
Presenilin-1, Nicastrin, Amyloid Precursor Protein, and γ-Secretase Activity Are Co-localized in the Lysosomal Membrane
Pasternak, 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 326
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
Autophagy in neurons: a review.
Larsen, K. E., & Sulzer, D. (2002) · PubMed · doi:10.14670/hh-17.897 · Cited by 245
Degradation of Alzheimer's ß-Amyloid Protein by Human and Rat Brain Peptidases: Involvement of Insulin-Degrading Enzyme
MCDERMOTT, J. R., & GIBSON, A. M. (1997) · Neurochemical Research · doi:10.1023/a:1027325304203 · Cited by 184
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 181
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
Self-citation
Subcellular 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
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
Dysfunction of autophagy and endosomal-lysosomal pathways: Roles in pathogenesis of Down syndrome and Alzheimer’s Disease
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
Self-citation
Proteome 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 161
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
The role of the endosomal/ lysosomal system in amyloid-beta production and the pathophysiology of Alzheimer's disease: Reexamining the spatial paradox from a lysosomal perspective
Pasternak, S., Callahan, J. W., & Mahuran, D. J. (2003) · Journal of Alzheimer s Disease · doi:10.3233/jad-2004-6107 · Cited by 127
Genome-scale metabolic network reconstruction of model animals as a platform for translational research
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 126
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 113
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 114
Self-citation
Reconsider 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 109
Alzheimer's Disease-related Overexpression of the Cation-dependent Mannose 6-Phosphate Receptor Increases Aβ Secretion
Mathews, P. M., Guerra, C. B., Jiang, Y., Grbovic, O. M., Kao, B. H., Schmidt, S. D., Dinakar, R., Mercken, M., Hille-Rehfeld, A., Rohrer, J., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108161200 · Cited by 86
Self-citation
Amyloidogenic Processing of Human Amyloid Precursor Protein in Hippocampal Neurons Devoid of Cathepsin D
Säftig, 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
Identification of post‐mortem cerebrospinal fluid proteins as potential biomarkers of ischemia and neurodegeneration
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
Microarray expression analysis and identification of serum biomarkers for Niemann–Pick disease, type C1
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
The role of lysosomal cathepsins in neurodegeneration: Mechanistic insights, diagnostic potential and therapeutic approaches
Drobny, A., Huarcaya, S. P., Dobert, J. P., Kluge, A., Bunk, J., Schlothauer, T., & Zunke, F. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119243 · Cited by 94
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
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 87
Exosome Production Is Key to Neuronal Endosomal Pathway Integrity in Neurodegenerative Diseases
Mathews, P. M., & Levy, E. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01347 · Cited by 81
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
Emerging blood exosome-based biomarkers for preclinical and clinical Alzheimer’s disease: a meta-analysis and systematic review
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 76
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
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
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 66
Aberrant sphingomyelin/ceramide metabolic-induced neuronal endosomal/lysosomal dysfunction: potential pathological consequences in age-related neurodegeneration
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
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
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 62
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 61
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
Lysosomal Protease Inhibitors Induce Meganeurites and Tangle-like Structures in Entorhinohippocampal Regions Vulnerable to Alzheimer's Disease
Bi, X., Zhou, J., & LYNCH, G. S. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7087 · Cited by 57
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 58
Differential protein expression in diverse brain areas of Parkinson’s and Alzheimer’s disease patients
Esteves, A. R., & Cardoso, S. M. (2020) · Scientific Reports · doi:10.1038/s41598-020-70174-z · Cited by 55
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 51
A paramagnetic chemical exchange-based MRI probe metabolized by cathepsin D: design, synthesis and cellular uptake studies
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
Predominant Release of Lysosomal Enzymes by Newborn Rat Microglia After LPS Treatment Revealed by Proteomic Studies
Liu, J., Hong, Z., Ding, J., Liu, J., Zhang, J., & Chen, S. (2008) · Journal of Proteome Research · doi:10.1021/pr7007779 · Cited by 41
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
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
Proteolytic degradation of hemoglobin by endogenous lysosomal proteases gives rise to bioactive peptides: hemorphins
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
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
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
Self-citation
Lysosomes and Brain Aging in Mammals
LYNCH, G. S., & Bi, X. (2003) · Neurochemical Research · doi:10.1023/a:1026069223763 · Cited by 36
Proteomic Analysis of Alzheimers Disease Cerebrospinal Fluid from Neuropathologically Diagnosed Subjects
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 33
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 36
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
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 31
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
Elevated Levels of Tau in Cerebrospinal Fluid: Implications for the Antemortem Diagnosis of Alzheimer's Disease
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 29
Significance of cytosolic cathepsin D in Alzheimer's disease pathology: Protective cellular effects of PLGA nanoparticles against β‐amyloid‐toxicity
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 29
Resveratrol Attenuates CSF Markers of Neurodegeneration and Neuroinflammation in Individuals with Alzheimer’s Disease
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
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 29
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
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 28
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 28
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
Focusing on cellular biomarkers: The endo-lysosomal pathway in Down syndrome
Botté, A., & Potier, M. (2019) · Progress in brain research · doi:10.1016/bs.pbr.2019.10.002 · Cited by 22
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
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
Antenatal betamethasone exposure is associated with lower ANG-(1–7) and increased ACE in the CSF of adult sheep
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
Neuropeptide Y ( NPY ) in cerebrospinal fluid from patients with Huntington's Disease: increased NPY levels and differential degradation of the NPY 1–30fragment
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
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
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
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
Haplodeficiency of Cathepsin D does not affect cerebral amyloidosis and autophagy in APP / PS 1 transgenic mice
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
Expression and characterization of human β-secretase candidates metalloendopeptidase MP78 and cathepsin D in βAPP-overexpressing cells
Thompson, A., Grueninger‐Leitch, F., Huber, G., & Malherbe, P. (1997) · Molecular Brain Research · doi:10.1016/s0169-328x(97)00091-0 · Cited by 15
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
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
Prolonged In Vivo Retention of a Cathepsin D Targeted Optical Contrast Agent in a Mouse Model of Alzheimer’s Disease
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 13
Neurodegenerative biomarkers and inflammation in patients with propionic and methylmalonic acidemias: effect of L-carnitine treatment
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
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
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
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
Correlative cryo-soft X-ray tomography and cryo-structured illumination microscopy reveal changes to lysosomes in amyloid-β-treated neurons
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
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
Limited proteolytic processing of the mature form of cathepsin D in human and mouse brain: Postmortem stability of enzyme structure and activity
Compaine, A. (1995) · Neurochemistry International · doi:10.1016/0197-0186(95)00020-9 · Cited by 8
Differential patterns of lysosomal dysfunction are seen in the clinicopathological forms of primary progressive aphasia
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
Mild Cognitive Impairment
Kluger, A., Golomb, J. B., & Ferris, S. H. (2003) · Wiley eBooks · doi:10.1002/9780470752340.ch25 · Cited by 6
New preclinical biomarkers for prion diseases in the cerebrospinal fluid proteome revealed by mass spectrometry
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
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
Aktuelle klinisch-neurochemische Diagnostik der Alzheimer-Krankheit/Current Clinical Neurochemical Diagnosis of Alzheimer’s Disease
Rösler, N., Wichart, I., & Jellinger, K. A. (2002) · Journal of Laboratory Medicine · doi:10.1046/j.1439-0477.2002.02031.x · Cited by 5
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
Quantitative proteomic analysis of down syndrome biomarkers in maternal serum using isobaric tags for relative and absolute quantification (iTRAQ)
Zhao, S., Liu, X., Wu, S., Zheng, Y., & Zhang, W. (2019) · Gynecological Endocrinology · doi:10.1080/09513590.2019.1696302 · Cited by 2
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
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
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., Zhu, C., & Sasaki, H. (1996) · Nippon Ronen Igakkai Zasshi Japanese Journal of Geriatrics · doi:10.3143/geriatrics.33.669 · Cited by 2
Alterations in the Na+/H+ Exchanger NHE6 and Glutamate Transporters may Influence Purkinje Cell Fate in ARSACS
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
Bridging autophagy and endolysosomal dysfunction: Role of bridging integrator 1 in Alzheimer’s disease
Duckhorn, J. C., Kim, D. K., & Huang, Y. A. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-00243 · Cited by 2
Novel Cathepsin D Inhibitors Prevent the β-Secretase-Derived Intracellular Formation of a 12 kDa Potentially Amyloidogenic Product in Human Cells
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
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.
ORCID: Kowall, N. W.
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
DOI: 10.1046/j.1471-4159.1995.64010443.x
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
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 2883 d)
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: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Health Sciences › Medicine › Clinical Neurology › 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

Elevated Levels of the Endosomal‐Lysosomal Proteinase Cathepsin D in Cerebrospinal Fluid in Alzheimer Disease

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks