The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Inhibition of cathepsin B reduces β-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: evidence for cathepsin B as a candidate β-secretase of Alzheimer's disease
Abstract
The regulated secretory pathway of neurons is the major source of extracellular Aβ that accumulates in Alzheimer's disease (AD). Extracellular Aβ secreted from that pathway is generated by β-secretase processing of amyloid precursor protein (APP). Previously, cysteine protease activity was demonstrated as the major β-secretase activity in regulated secretory vesicles of neuronal chromaffin cells. In this study, the representative cysteine protease activity in these secretory vesicles was purified and identified as cathepsin B by peptide sequencing. Immunoelectron microscopy demonstrated colocalization of cathepsin B with Aβ in these vesicles. The selective cathepsin B inhibitor, CA074, blocked the conversion of endogenous APP to Aβ in isolated regulated secretory vesicles. In chromaffin cells, CA074Me (a cell permeable form of CA074) reduced by about 50% the extracellular Aβ released by the regulated secretory pathway, but CA074Me had no effect on Aβ released by the constitutive pathway. Furthermore, CA074Me inhibited processing of APP into the COOH-terminal β-secretase-like cleavage product. These results provide evidence for cathepsin B as a candidate β-secretase in regulated secretory vesicles of neuronal chromaffin cells. These findings implicate cathepsin B as β-secretase in the regulated secretory pathway of brain neurons, suggesting that inhibitors of cathepsin B may be considered as therapeutic agents to reduce Aβ in AD.
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Cites
Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876 · cited 1×
“Studies of the constitutive secretory pathway for Ab production indicate the aspartyl protease BACE 1 is a b-secretase in that pathway (Hussain et al., 1999; Sinha et al., 1999; Vassar et al., 1999; Yan et al., 1999; Lin et al., 2000).”
BackgroundCitron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J. (1992) · Nature · doi:10.1038/360672a0 · Cited by 1,757
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Nitsch, R. M., Farber, S. A., Growdon, J. H., & Wurtman, R. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.11.5191 · Cited by 244
Cited by
APP processing in Alzheimer’s disease.
Zhang, Y.-W., Thompson, R., Zhang, H., & Xu, H. (2011) · Molecular Brain · doi:10.1186/1756-6606-4-3 · Cited by 983
An overview of APP processing enzymes and products.
Chow, V. W., Mattson, M. P., Wong, P. C., & Gleichmann, M. (2010) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8104-z · Cited by 684
Antiamyloidogenic and Neuroprotective Functions of Cathepsin B: Implications for Alzheimer's Disease
Mueller-Steiner, S., Zhou, Y., Arai, H., Roberson, E. D., Sun, B., Chen, J., Wang, X., Yu, G., Esposito, L., Mucke, L., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.07.027 · Cited by 465
Hoegen, T., Tremel, N., Klein, M., Angele, B., Wagner, H., Kirschning, C., Pfister, H.-W., Fontana, A., Hammerschmidt, S., & Koedel, U. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100790 · Cited by 211
Mandel, S., Rechavi, G., & Gozes, I. (2007) · Developmental Biology · doi:10.1016/j.ydbio.2006.11.039 · Cited by 167
Metadata
- Authors
- Hook, V., Toneff, T., Bogyo, M., Greenbaum, D., Medzihradszky, K. F., Neveu, J., Lane, W., Hook, G., & Reisine, T.
- Venue
- Biological Chemistry
- Publisher
- Walter de Gruyter GmbH
- Published
- 2005-01-01
- Volume
- 386
- Issue
- 9
- Pages
- 931-40
- ISSN
- 1431-6730 (ISSN-L)
- 1437-4315
- OpenAlex
- W1964589079
- Cited by
- 174
- References
- 4
- FWCI
- 6.57
- Type
- journal article
- Language
- en
- Open access
- closed
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- Hook, V., Toneff, T., Bogyo, M., Greenbaum, D., Medzihradszky, K. F., Neveu, J., Lane, W., Hook, G., & Reisine, T. (2005). Inhibition of cathepsin B reduces β-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: evidence for cathepsin B as a candidate β-secretase of Alzheimer's disease. Biological Chemistry. https://doi.org/10.1515/bc.2005.108
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
