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Glu11 Site Cleavage and N-Terminally Truncated Aβ Production upon BACE Overexpression
Abstract
Amyloid beta peptides (A beta) are generated by the proteolytic processing of the amyloid beta precursor protein (APP). The newly identified beta-site APP-cleaving enzyme (BACE) cleaves APP at Asp1 as well as between Tyr10 and Glu11 of A beta, producing C-terminal fragments (CTFs) C99 and C89, respectively. Subsequent cleavage by gamma-secretase gives rise to A beta 1-40/42 and A beta 11-40/42. Although both full-length and A beta peptides truncated at residue 11 have been identified in amyloid plaques in the AD brain, the relative proportion of these two cleavage products produced by BACE and secreted into the medium by cultured cells is unknown. Using cell lines stably overexpressing BACE, we found that A beta 11-40 and A beta 11-42 are major A beta cleavage products generated by BACE. We further showed that BACE utilizes both full-length APP as well as C99 as substrates for the production of C89, and that A beta 11-40/42 can be generated by sequential cleavage of single APP molecules by BACE and gamma-secretase. Taken together, the abundance of A beta 11-40/42 produced by BACE suggests that their roles in AD pathogenesis may be underestimated.
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BACE-1 can catalyze amyloidolytic processing by cleavage between Tyr10 and Glu11 of the Aβ sequence, the β'-cleavage site.
“BACE-1 can also catalyze amyloidolytic processing by cleavage between Tyr10 and Glu11 of the Aβ sequence (Huse et al., 2002; Liu et al., 2002; Kimura et al., 2016), the so-called β’-cleavage site (Figure 1).”
From Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP (2019) · cites this paper as Liu et al., 2002
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- Abbreviations Aβ, amyloid β peptide
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Casas, C., Sergeant, N., Itier, J.-M., Blanchard, V., Wirths, O., van der Kolk, N., Vingtdeux, V., van de Steeg, E., Ret, G., Canton, T., et al. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63388-3 · Cited by 400
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Rodent Aβ Modulates the Solubility and Distribution of Amyloid Deposits in Transgenic Mice
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The Proteasome and Oxidative Stress in Alzheimer's Disease
Bonet-Costa, V., Pomatto, L. C.-D., & Davies, K. J. A. (2016) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6802 · Cited by 99
GGA1 Is Expressed in the Human Brain and Affects the Generation of Amyloid β-Peptide
Wahle, T., Thal, D. R., Sastre, M., Rentmeister, A., Bogdanovic, N., Famulok, M., Heneka, M. T., & Walter, J. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1982-06.2006 · Cited by 88
García-González, L., Pilat, D., Baranger, K., & Rivera, S. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00244 · Cited by 88
Kang, E. L., Biscaro, B., Piazza, F., & Tesco, G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407072 · Cited by 55
Transcriptional and post‐transcriptional regulation of β‐secretase
Tamagno, E., Guglielmotto, M., Monteleone, D., Vercelli, A., & Tabaton, M. (2012) · IUBMB Life · doi:10.1002/iub.1099 · Cited by 40
Metadata
- Authors
- Liu, K., Doms, R. W., & Lee, V. M.-Y.
- Affiliations
- The Center for Neurodegenerative Disease Research, Department of Pathology and Laboratory Medicine, and Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-02-08
- Volume
- 41
- Issue
- 9
- Pages
- 3128-3136
- ISSN
- 0006-2960
- 1520-4995
- Cited by
- 96
- References
- 1
- Language
- en
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