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Neuronal loss and brain atrophy in mice lacking cathepsins B and L
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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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“CTSD protein levels are elevated in CTSB/CTSL double KO mice (Felbor et al., 2002), suggesting intralysosomal CTSD proteolysis, even though the involved protease(s) are unclear.”
From Lysosomal Dysfunction in Down Syndrome Is APP-Dependent and Mediated by APP-βCTF (C99) (2019) · cites this paper as Felbor et al., 2002
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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 924
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
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-citationFoghsgaard, 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
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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Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069
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Boya, P., & Kroemer, G. (2008) · Oncogene · doi:10.1038/onc.2008.310 · Cited by 1,456
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Chandran, K., Sullivan, N. J., Felbor, U., Whelan, S. P. J., & Cunningham, J. M. (2005) · Science · doi:10.1126/science.1110656 · Cited by 826
Self-citationGuicciardi, M. E., Leist, M., & Gores, G. J. (2004) · Oncogene · doi:10.1038/sj.onc.1207512 · Cited by 731
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Moon, H. Y., Becke, A., Berron, D., Becker, B., Sah, N., Benoni, G., Janke, E., Lubejko, S. T., Greig, N. H., Mattison, J. A., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.025 · Cited by 628
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Gocheva, V., Zeng, W., Ke, D., Klimstra, D. S., Reinheckel, T., Peters, C., Hanahan, D., & Joyce, J. A. (2006) · Genes & Development · doi:10.1101/gad.1407406 · Cited by 583
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Colacurcio, D. J., & Nixon, R. A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.05.004 · Cited by 548
Park, B., Brinkmann, M. M., Spooner, E., Lee, C. C., Kim, Y., & Ploegh, H. L. (2008) · Nature Immunology · doi:10.1038/ni.1669 · Cited by 478
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Yang, D.-S., Stavrides, P., Mohan, P. S., Kaushik, S., Kumar, A., Ohno, M., Schmidt, S. D., Wesson, D., Bandyopadhyay, U., Jiang, Y., et al. (2011) · Brain · doi:10.1093/brain/awq341 · Cited by 429
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Chwieralski, C. E., Welte, T., & Bühling, F. (2006) · APOPTOSIS · doi:10.1007/s10495-006-3486-y · Cited by 437
Chu, Y., Dodiya, H. B., Aebischer, P., Olanow, C. W., & Kordower, J. H. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.05.023 · Cited by 447
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Repnik, U., Stoka, V., Türk, V., & Turk, B. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.08.016 · Cited by 412
Nixon, R. A. (2017) · The FASEB Journal · doi:10.1096/fj.201700359 · Cited by 400
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Duncan, E. M., Muratore‐Schroeder, T. L., Cook, R. G., Garcia, B. A., Shabanowitz, J., Hunt, D. F., & Allis, C. D. (2008) · Cell · doi:10.1016/j.cell.2008.09.055 · Cited by 372
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Nixon, R. A., Yang, D.-S., & Lee, J.-H. (2008) · Autophagy · doi:10.4161/auto.6259 · Cited by 362
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Liaudet‐Coopman, E., Beaujouin, M., Derocq, D., Garcia, M., Glondu-Lassis, M., Laurent‐Matha, V., Prébois, C., Rochefort, H., & Vignon, F. (2005) · Cancer Letters · doi:10.1016/j.canlet.2005.06.007 · Cited by 361
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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
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Song, Q., Meng, B., Xu, H., & Mao, Z. (2020) · Translational Neurodegeneration · doi:10.1186/s40035-020-00196-0 · Cited by 244
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Mizunoe, Y., Sudo, Y., Okita, N., Hiraoka, H., Mikami, K., Narahara, T., Negishi, A., Yoshida, M., Higashibata, R., Watanabe, S., et al. (2017) · Autophagy · doi:10.1080/15548627.2016.1274850 · Cited by 111
Houseweart, M. K., Pennacchio, L. A., Vilaythong, A., Peters, C., Noebels, J. L., & Myers, R. (2003) · Journal of Neurobiology · doi:10.1002/neu.10253 · Cited by 107
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Tatti, M., Motta, M., Bartolomeo, S. D., Scarpa, S., Cianfanelli, V., Cecconi, F., & Salvioli, R. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds367 · Cited by 80
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Li, L., Wang, X., Fei, X., Xia, L., Qin, Z., & Liang, Z. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.11.068 · Cited by 68
García‐García, A., Anandhan, A., Burns, M., Chen, H., Zhou, Y., & Franco, R. (2013) · Toxicological Sciences · doi:10.1093/toxsci/kft188 · Cited by 65
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Hook, G. R., Yu, J., Sipes, N., Pierschbacher, M., Hook, V., & Kindy, M. (2014) · Journal of Neurotrauma · doi:10.1089/neu.2013.2944 · Cited by 51
Fan, K., Wu, X., Fan, B., Li, N., Lin, Y., Yao, Y., & Ma, J. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-96 · Cited by 67
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Li, Y., Mei, T., Han, S., Han, T., Sun, Y., Zhang, H., & An, F. (2020) · Chinese Chemical Letters · doi:10.1016/j.cclet.2020.05.027 · Cited by 61
Kothapalli, K. S. D., Anthony, J. C., Pan, B. S., Hsieh, A. T., Nathanielsz, P. W., & Brenna, J. T. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000370 · Cited by 63
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Self-citation
Metadata
- Authors
- Felbor, U., Kessler, B., Mothes, W., Goebel, H. H., Ploegh, H. L., Bronson, R. T., & Olsen, B. R.
- Affiliations
- Tufts University (US)
- ORCID
- 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
- 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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