Cited by 379Alzheimer's disease research and treatmentsProtease and Inhibitor MechanismsDementia and Cognitive Impairment Research

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Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: Evidence for early up-regulation of the endosomal-lysosomal system

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Cataldo, Anne M, Barnett, Jody L, Berman, Stephen A, Li, Jinhe, Quarless, Shelley, Bursztajn, Sherry, Lippa, Carol, Nixon, Ralph A·1995·Neuron

DOI 10.1016/0896-6273(95)90324-0

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Abstract

In Alzheimer's disease brains, more than 90% of pyramidal neurons in lamina V and 70% in lamina III displayed 2- to 5-fold elevated levels of cathepsin D (Cat D) mRNA by in situ hybridization compared with neurologically normal controls. Most of these cells appeared histologically normal. The less vulnerable nonpyramidal neuron population in lamina IV had relatively normal message levels. Neuronal populations expressing more Cat D mRNA also displayed quantitatively increased Cat D immunoreactive protein. Cat D mRNA expression was only moderately increased in astrocytes. Degenerating neurons exhibited intense immunoreactivity but lowered Cat D mRNA levels. The upregulation of Cat D synthesis and accumulation of hydrolase-laden lysosomes indicate an early activation of the endosomal-lysosomal system in vulnerable neuronal populations, possibly reflecting early regenerative or repair processes. These abnormalities also represent a basis for altered regulation of amyloid precursor protein processing.

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Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589
Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures.
Hsu, S. M., Raine, L., & Fanger, H. (1981) · Journal of Histochemistry & Cytochemistry · doi:10.1177/29.4.6166661 · Cited by 14,075
Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families
Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429
The Consortium to Establish a Registry for Alzheimer's Disease (CERAD): Part II. Standardization of the neuropathologic assessment of Alzheimer's disease
Mirra, S. S., Heyman, A., McKeel, D., Sumi, S. M., Crain, B. J., Brownlee, L. M., Vogel, F. S., Hughes, J. P., Belle, G. V., Berg, L., et al. (1991) · Neurology · doi:10.1212/wnl.41.4.479 · Cited by 4,961
Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659
Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue
Duve, C. D., Pressman, B. C., Gianetto, R., Wattiaux, R., & Appelmans, F. (1955) · Biochemical Journal · doi:10.1042/bj0600604 · Cited by 4,176
Apolipoprotein E: Cholesterol Transport Protein with Expanding Role in Cell Biology
Mahley, R. W. (1988) · Science · doi:10.1126/science.3283935 · Cited by 4,028
Functions of Lysosomes
de Duve, C., & Wattiaux, R. (1966) · Annual Review of Physiology · doi:10.1146/annurev.ph.28.030166.002251 · Cited by 3,033
Detection of mRNAs in sea urchin embryos by in situ hybridization using asymmetric RNA probes
Cox, K. H., DeLeon, D. V., Angerer, L. M., & Angerer, R. C. (1984) · Developmental Biology · doi:10.1016/0012-1606(84)90162-3 · Cited by 1,610
The Biogenesis of Lysosomes
Kornfeld, S. A., & Mellman, I. (1989) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.05.110189.002411 · Cited by 1,593

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Oyama, F., Murakami, N., & Ihara, Y. (1998) · Neuroscience Research · doi:10.1016/s0168-0102(98)00020-0 · Cited by 47
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Sadik, G., Kaji, H., Takeda, K., Yamagata, F., Kameoka, Y., Hashimoto, K., Miyanaga, K., & Shinoda, T. (1999) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(99)00053-9 · Cited by 47
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Thal, D. R., Gawor, K., & Moonen, S. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02722-0 · Cited by 50
Involvement of cystatin C in pathophysiology of CNS diseases
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Viña, J., Lloret, A., Vallés, S. L., Borrás, C., Badía, M.-C., Pallardó, F. V., Sastre, J., & Alonso, M.-D. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-11205 · Cited by 44
Mutation of potential N-linked glycosylation sites in the Alzheimer's disease amyloid precursor protein (APP)
Yazaki, M., Tagawa, K., Maruyama, K., Sorimachi, H., Tsuchiya, T., Ishiura, S., & Suzuki, K. (1996) · Neuroscience Letters · doi:10.1016/s0304-3940(96)13285-7 · Cited by 43
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Caspase‐cleaved actin (fractin) immunolabelling of Hirano bodies
Rossiter, J. P., Anderson, L. L., Yang, F., & Cole, G. M. (2000) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2000.00252.x · Cited by 42
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
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Neuronal gene expression profiling: uncovering the molecular biology of neurodegenerative disease
Mufson, E. J., Counts, S., Che, S., & Ginsberg, S. D. (2006) · Progress in brain research · doi:10.1016/s0079-6123(06)58010-0 · Cited by 40
Kinetic properties of cathepsin D and BACE 1 indicate the need to search for additional β-secretase candidate(s)
Schechter, I., & Ziv, E. (2008) · Biological Chemistry · doi:10.1515/bc.2008.025 · Cited by 40
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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
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DeKroon, R. M., & Armati, P. J. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0362 · Cited by 38
Roles of cathepsins in reperfusion-induced apoptosis in cultured astrocytes
Takuma, K., Kiriu, M., Mori, K., Lee, E., Enomoto, R., Baba, A., & Matsuda, T. (2002) · Neurochemistry International · doi:10.1016/s0197-0186(02)00077-3 · Cited by 37
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Shafei, M. A., Harris, M., & Conway, M. E. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00173 · Cited by 38
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Burrinha, T., Cunha, C., Hall, M. J., Lopes‐da‐Silva, M., Seabra, M. C., & Guimas Almeida, C. (2023) · Traffic · doi:10.1111/tra.12889 · Cited by 35
Processing of β-Amyloid Precursor Protein by Cathepsin D
Higaki, J. N., Catalano, R., Guzzetta, A. W., Quon, D. H., Navé, J.-F., Tarnus, C., d'Orchymont, H., & Cordell, B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.50.31885 · Cited by 35
From sentencing to execution – the processes of apoptosis
Moffitt, K. L., Martin, L., & Walker, B. (2010) · Journal of Pharmacy and Pharmacology · doi:10.1211/jpp.62.05.0001 · Cited by 35
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Watanabe, Y., Hirao, Y., Kasuga, K., Tokutake, T., Semizu, Y., Kitamura, K., Ikeuchi, T., Nakamura, K., & Yamamoto, T. (2019) · Dementia and Geriatric Cognitive Disorders Extra · doi:10.1159/000496100 · Cited by 35
Impaired lysosomal processing of β2-microglobulin by infiltrating macrophages in dialysis amyloidosis
Garcia-Garcia, M., Argilés, À., Gouin, A., Durfort, M., García‐Valero, J., & Mourad, G. (1999) · Kidney International · doi:10.1046/j.1523-1755.1999.055003899.x · Cited by 33
Genetic and biochemical markers for Alzheimer's disease: recent developments
Mulder, C., Scheltens, P., Visser, J. J., van Kamp, G. J., & Schutgens, R. B. H. (2000) · Annals of Clinical Biochemistry International Journal of Laboratory Medicine · doi:10.1258/0004563001899898 · Cited by 32

Authors: Cataldo, A. M., Barnett, J. L., Berman, S. A., Li, J., Quarless, S., Bursztajn, S., Lippa, C., & Nixon, R. A.
Affiliations: Harvard University (US)
University of Massachusetts Chan Medical School (US)
ORCID: Li, Jinhe
Lippa, Carol
Nixon, Ralph A
Venue: Neuron
Publisher: Elsevier BV
Published: 1995-03
Volume: 14
Issue: 3
Pages: 671-680
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/0896-6273(95)90324-0
OpenAlex: W1988022242
Cited by: 379
References: 88
Citations by year: 2026: 5 · 2025: 10 · 2024: 11 · 2023: 11 · 2022: 5 · 2021: 9 · 2020: 17 · 2019: 18 · 2018: 14 · 2017: 10 · 2016: 18 · 2015: 16 · 2014: 17 · 2013: 12 · 2012: 16
FWCI: 8.86
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 6713 d)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r35ag010916-08, 5r01ag008278-11)
National Institute on Aging (AG 08278, AG 10916, P50AG005134, AG 05134)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: cathepsin D, Alzheimer's disease, endosomal-lysosomal system, lysosomes, pyramidal neurons, lamina V, lamina III, lamina IV, non-pyramidal neurons, astrocytes, neurodegeneration, APP processing, gene expression
MeSH terms: Aged, Alzheimer Disease, Cathepsin D, Humans, Hydrolases, Lysosomes, Middle Aged, Nerve Degeneration, Neurons, Protein Processing, Post-Translational, Endosomes, Reference Values, RNA, Messenger, Blotting, Northern, Gene Expression, Gene Expression Regulation, Enzymologic, Prefrontal Cortex, In Situ Hybridization

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Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: Evidence for early up-regulation of the endosomal-lysosomal system

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