Cited by 337Protease and Inhibitor MechanismsCalpain Protease Function and RegulationAutophagy in Disease and Therapy

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Neuronal loss and brain atrophy in mice lacking cathepsins B and L

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Felbor, Ute, Kessler, Benedikt, Mothes, Walther, Goebel, Hans H., Ploegh, Hidde L., Bronson, Roderick T., Olsen, Bjorn R.·2002·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.112632299PMC PMC122989

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Abstract

Cathepsins B and L are widely expressed cysteine proteases implicated in both intracellular proteolysis and extracellular matrix remodeling. However, specific roles remain to be validated in vivo . Here we show that combined deficiency of cathepsins B and L in mice is lethal during the second to fourth week of life. Cathepsin B −/− /L −/− mice reveal a degree of brain atrophy not previously seen in mice. This is because of massive apoptosis of select neurons in the cerebral cortex and the cerebellar Purkinje and granule cell layers. Neurodegeneration is accompanied by pronounced reactive astrocytosis and is preceded by an accumulation of ultrastructurally and biochemically unique lysosomal bodies in large cortical neurons and by axonal enlargements. Our data demonstrate a pivotal role for cathepsins B and L in maintenance of the central nervous system.

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Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation.
Gavrieli, Y., Sherman, Y., & Ben-Sasson, S. A. (1992) · The Journal of cell biology · doi:10.1083/jcb.119.3.493 · Cited by 9,444
Synaptic assembly of the brain in the absence of neurotransmitter secretion.
Verhage, M., Maia, A., Plomp, J., Brussaard, A., Heeroma, J., Vermeer, H., Toonen, R., Hammer, R., van den Berg, T. K., Missler, M., et al. (2000) · Science · doi:10.1126/science.287.5454.864 · Cited by 1,387
The Handbook of proteolytic enzymes
Barrett, A. J., Rawlings, N. D., & Woessner, J. F. (1998) · Cited by 1,119
Pycnodysostosis, a Lysosomal Disease Caused by Cathepsin K Deficiency
Gelb, B. D., Shi, G., Chapman, H. A., & Desnick, R. J. (1996) · Science · doi:10.1126/science.273.5279.1236 · Cited by 1,022
Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin-K-deficient mice
Säftig, P., Hunziker, E. B., Wehmeyer, O., Jones, S. J., BOYDE, A., Rommerskirch, W., Moritz, J. D., Schu, P. V., & FIGURA, K. V. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13453 · Cited by 909
Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis
Vesa, J., Hellsten, E., Verkruyse, L. A., Camp, L. A., Rapola, J., Santavuori, P., Hofmann, S. L., & Peltonen, L. (1995) · Nature · doi:10.1038/376584a0 · Cited by 736
Cathepsin B contributes to TNF-α–mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c
Guicciardi, M. E., Deussing, J. M., Miyoshi, H., Bronk, S. F., Svingen, P. A., Peters, C., Kaufmann, S. H., & Gores, G. J. (2000) · Journal of Clinical Investigation · doi:10.1172/jci9914 · Cited by 710
Cathepsin L: Critical Role in Ii Degradation and CD4 T Cell Selection in the Thymus
Nakagawa, T. Y., Roth, W., Wong, P., Nelson, A., Farr, A. G., Deussing, J. M., Villadangos, J. A., Ploegh, H. L., Peters, C., & Rudensky, A. Y. (1998) · Science · doi:10.1126/science.280.5362.450 · Cited by 675
Self-citation
Cathepsin B Acts as a Dominant Execution Protease in Tumor Cell Apoptosis Induced by Tumor Necrosis Factor
Foghsgaard, L., Wissing, D., Mauch, D., Lademann, U. A., Bastholm, L., Boes, M. L., Elling, F., Leist, M., & Jäättelä, M. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.5.999 · Cited by 629
Association of Mutations in a Lysosomal Protein with Classical Late-Infantile Neuronal Ceroid Lipofuscinosis
Sleat, D. E., DONNELLY, R. J., Lackland, H., Liu, C., Sohár, I., Pullarkat, R. K., & Lobel, P. (1997) · Science · doi:10.1126/science.277.5333.1802 · Cited by 581

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H Kirschke Handbook of Proteolytic Enzymes, eds A J Barrett, N D Rawlings, J F Woessner (Academic, San Diego), pp. 617–621 (1998).

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Kudo, L. C., Karsten, S. L., Chen, J., Levitt, P. R., & Geschwind, D. H. (2006) · Cerebral Cortex · doi:10.1093/cercor/bhl118 · Cited by 31
Three-dimensional cultures modeling premalignant progression of human breast epithelial cells: role of cysteine cathepsins
Mullins, S., Sameni, M., Blum, G., Bogyo, M. S., Sloane, B. F., & Moin, K. (2012) · Biological Chemistry · doi:10.1515/hsz-2012-0252 · Cited by 30
Olomoucine inhibits cathepsin L nuclear translocation, activates autophagy and attenuates toxicity of 6-hydroxydopamine
Fei, X., Qin, Z., Xiang, B., Li, L., Han, F., Fukunaga, K., & Liang, Z. (2009) · Brain Research · doi:10.1016/j.brainres.2009.01.057 · Cited by 30
Predominance of Interferon-Related Responses in the Brain during Murine Malaria, as Identified by Microarray Analysis
Miu, J., Hunt, N. H., & Ball, H. J. (2008) · Infection and Immunity · doi:10.1128/iai.01650-07 · Cited by 30
Compensational role between cathepsins
Fonović, U. P., Kos, J., & Mitrović, A. (2024) · Biochimie · doi:10.1016/j.biochi.2024.04.010 · Cited by 29
Novel 1,2,3-triazole-aurone hybrids as cathepsin B inhibitors: One-pot synthesis, anti-proliferative, and drug modeling studies
Saroha, B., Kumar, G., Kumar, S., Kumari, M., Rani, M., Raghav, N., Sahoo, P. K., Ghosh, S., Mahata, S., & Nasare, V. D. (2022) · European Journal of Medicinal Chemistry Reports · doi:10.1016/j.ejmcr.2022.100056 · Cited by 29
Role of chaperone-mediated autophagy in degrading Huntington's disease-associated huntingtin protein
Qi, L., & Zhang, X. (2013) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmt133 · Cited by 29
Cathepsin B inhibition blocks neurite outgrowth in cultured neurons by regulating lysosomal trafficking and remodeling
Jiang, M., Meng, J., Zeng, F., Qing, H., Hook, G., HOOK, V. Y. H., Wu, Z., & Ni, J. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15032 · Cited by 28
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
Cathepsin K Inhibitors: Their Potential as Anti-Osteoporosis Agents
Deaton, D. N., & Kumar, S. (2004) · Progress in medicinal chemistry · doi:10.1016/s0079-6468(04)42006-2 · Cited by 28
Do molecular signals from the conceptus influence endometrium decidualization in rodents?
Herington, J. L., & Bany, B. M. (2009) · Journal of Experimental Zoology Part B Molecular and Developmental Evolution · doi:10.1002/jez.b.21308 · Cited by 28
The anti-angiogenic activity of NSITC, a specific cathepsin L inhibitor.
Rebbaa, A., Chu, F., Sudha, T., Gallati, C., Dier, U., Dyskin, E., Yalçın, M., Bianchini, C., Shaker, O. G., & Mousa, S. A. (2009) · PubMed · Cited by 28
Retracted
The polyphenol EGCG directly targets intracellular amyloid‐β aggregates and promotes their lysosomal degradation
Secker, C., Motzny, A., Kostova, S., Buntru, A., Helmecke, L., Reus, L., Steinfort, R., Brusendorf, L., Boeddrich, A., Neuendorf, N., et al. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15842 · Cited by 28
A murrel cysteine protease, cathepsin L: bioinformatics characterization, gene expression and proteolytic activity
Kumaresan, V., Bhatt, P., Palanisamy, R., Gnanam, A. J., Pasupuleti, M., & Arockiaraj, J. (2014) · Biologia · doi:10.2478/s11756-013-0326-8 · Cited by 27
Activated cathepsin L is associated with the switch from autophagy to apoptotic death of SH-SY5Y cells exposed to 6-hydroxydopamine
Li, L., Gao, L., Song, Y.-Z., Qin, Z., & Liang, Z. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.01.102 · Cited by 26
Integrated single cell data analysis reveals cell specific networks and novel coactivation markers
Ghazanfar, S., Bisogni, A. J., Ormerod, J. T., Lin, D. M., & Yang, J. Y. H. (2016) · BMC Systems Biology · doi:10.1186/s12918-016-0370-4 · Cited by 25
Split top: A maternal cathepsin B that regulates dorsoventral patterning and morphogenesis
Langdon, Y., Fuentes, R., Zhang, H., Abrams, E. W., Marlow, F. L., & Mullins, M. C. (2016) · Development · doi:10.1242/dev.128900 · Cited by 26
Cathepsin C Aggravates Neuroinflammation Involved in Disturbances of Behaviour and Neurochemistry in Acute and Chronic Stress-Induced Murine Model of Depression
Zhang, Y., Fan, K., Liu, Y., Liu, G., Yang, X., & Ma, J. (2017) · Neurochemical Research · doi:10.1007/s11064-017-2320-y · Cited by 27
Structure-Guided Development of Selective TbcatB Inhibitors
Mallari, J. P., Shelat, A. A., Kosinski, A. M., Caffrey, C. R., Connelly, M., Zhu, F., McKerrow, J. H., & Guy, R. K. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900908p · Cited by 25
The Emerging Relevance of the Cysteine Protease Cathepsin S in Disease
Small, D. M., Burden, R. E., & Scott, C. J. (2011) · Clinical Reviews in Bone and Mineral Metabolism · doi:10.1007/s12018-011-9095-5 · Cited by 25
Autophagy Intertwines with Different Diseases—Recent Strategies for Therapeutic Approaches
Ramesh, J., Ronsard, L., Gao, A., & Venugopal, B. (2019) · Diseases · doi:10.3390/diseases7010015 · Cited by 26
Penetrating Traumatic Brain Injury Triggers Dysregulation of Cathepsin B Protein Levels Independent of Cysteine Protease Activity in Brain and Cerebral Spinal Fluid
Boutté, A. M., HOOK, V. Y. H., Thangavelu, B., Sarkis, G. A., Abbatiello, B. N., Hook, G., Jacobsen, J. S., Robertson, C. S., Gilsdorf, J. S., Yang, Z., et al. (2020) · Journal of Neurotrauma · doi:10.1089/neu.2019.6537 · Cited by 25
6-Hydroxydopamine induces cystatin C-mediated cysteine protease suppression and cathepsin D activation
LEE, D., Womble, T. A., MASON, C., Jackson, I. N., Lamango, N. S., Severs, W. B., & Palm, D. E. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2006.12.006 · Cited by 25
Inhibitors of cathepsins B and L induce autophagy and cell death in neuroblastoma cells
Cartledge, D. M., Colella, R., Glazewski, L., Lu, G., & Mason, R. W. (2012) · Investigational New Drugs · doi:10.1007/s10637-012-9826-6 · Cited by 26
Defective Autophagy in Fibroblasts May Contribute to Fibrogenesis in Autoimmune Processes
Principe, D. D., Vona, R., Giordani, L., Straface, E., & Giammarioli, A. M. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211798357791 · Cited by 23
Lysosome imaging in cancer cells by pyrene-benzothiazolium dyes: An alternative imaging approach for LAMP-1 expression based visualization methods to avoid background interference
Abeywickrama, C. S., Wijesinghe, K. J., Stahelin, R. V., & Pang, Y. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.103144 · Cited by 22
Mannose 6-Phosphorylated Proteins Are Required for Tumor Necrosis Factor-induced Apoptosis
Tardy, C., Autefage, H., Garcia, V., Levade, T., & Andrieu‐Abadie, N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408261200 · Cited by 22
Concomitant lack of MMP9 and uPA disturbs physiological tissue remodeling
Lund, I. K., Nielsen, B. S., Almholt, K., Rønø, B., Hald, A., Illemann, M., Green, K. A., Christensen, I. J., Rømer, J., & Lund, L. R. (2011) · Developmental Biology · doi:10.1016/j.ydbio.2011.07.021 · Cited by 21
Cathepsin L Acutely Alters Microvessel Integrity within the Neurovascular Unit during Focal Cerebral Ischemia
Gu, Y.-H., Kanazawa, M., Hung, S. Y., Wang, X., Fukuda, S., Koziol, J. A., & del Zoppo, G. J. (2015) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2015.170 · Cited by 21
Cp1/cathepsin L is required for autolysosomal clearance in Drosophila
Xu, T., Nicolson, S., Sandow, J. J., Dayan, S., Jiang, X., Manning, J. A., Webb, A. I., Kumar, S., & Denton, D. (2020) · Autophagy · doi:10.1080/15548627.2020.1838105 · Cited by 21
Expression of the human Cathepsin L inhibitor hurpin in mice: skin alterations and increased carcinogenesis
Walz, M., Kellermann, S., Bylaitė, M., Andrée, B., Rüther, U., Paus, R., Kloepper, J. E., REIFENBERGER, J., & Ruzicka, T. (2007) · Experimental Dermatology · doi:10.1111/j.1600-0625.2007.00579.x · Cited by 21
Cathepsin L Plays a Role in Quinolinic Acid-Induced NF-Κb Activation and Excitotoxicity in Rat Striatal Neurons
Wang, Y.-R., Qin, S., Han, R., Wu, J., Liang, Z., Qin, Z., & Wang, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075702 · Cited by 20

Authors: Felbor, U., Kessler, B., Mothes, W., Goebel, H. H., Ploegh, H. L., Bronson, R. T., & Olsen, B. R.
Affiliations: Tufts University (US)
ORCID: Felbor, Ute
Kessler, Benedikt
Mothes, Walther
Goebel, Hans H.
Ploegh, Hidde L.
Bronson, Roderick T.
Olsen, Bjorn R.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2002-06-04
Volume: 99
Issue: 12
Pages: 7883-7888
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.112632299
PMC: PMC122989
OpenAlex: W1984073321
Cited by: 334
References: 44
Citations by year: 2026: 6 · 2025: 7 · 2024: 9 · 2023: 10 · 2022: 17 · 2021: 7 · 2020: 16 · 2019: 12 · 2018: 8 · 2017: 9 · 2016: 15 · 2015: 14 · 2014: 11 · 2013: 19 · 2012: 16
FWCI: 5.31
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
The Mouseion at the JAXlibrary (Jackson Laboratory) (submittedVersion)
Funders: AstraZeneca
Deutsche Forschungsgemeinschaft
National Institutes of Health
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: cathepsin B, cathepsin L, cysteine protease, neuronal loss, brain atrophy, neurodegeneration, apoptosis, reactive astrogliosis, Purkinje cells, granule cells, cerebral cortex, cerebellum, embryonic lethality, knockout mice
MeSH terms: Animals, Atrophy, Brain, Cathepsin B, Cathepsins, Cerebellum, Cysteine Endopeptidases, Genotype, Lysosomes, Neurons, Endosomes, Apoptosis, Mice, Knockout, Mice, Cathepsin L

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Neuronal loss and brain atrophy in mice lacking cathepsins B and L

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