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Metalloprotease Meprin β Generates Nontoxic N-terminal Amyloid Precursor Protein Fragments in Vivo
Abstract
Identification of physiologically relevant substrates is still the most challenging part in protease research for understanding the biological activity of these enzymes. The zinc-dependent metalloprotease meprin β is known to be expressed in many tissues with functions in health and disease. Here, we demonstrate unique interactions between meprin β and the amyloid precursor protein (APP). Although APP is intensively studied as a ubiquitously expressed cell surface protein, which is involved in Alzheimer disease, its precise physiological role and relevance remain elusive. Based on a novel proteomics technique termed terminal amine isotopic labeling of substrates (TAILS), APP was identified as a substrate for meprin β. Processing of APP by meprin β was subsequently validated using in vitro and in vivo approaches. N-terminal APP fragments of about 11 and 20 kDa were found in human and mouse brain lysates but not in meprin β(-/-) mouse brain lysates. Although these APP fragments were in the range of those responsible for caspase-induced neurodegeneration, we did not detect cytotoxicity to primary neurons treated by these fragments. Our data demonstrate that meprin β is a physiologically relevant enzyme in APP processing.
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N-APP fragments are detected in mouse brains and in the brains of healthy individuals and patients with AD.
“N-APP were detected in mice brains as well as in the brains of healthy individuals and patients with AD”
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 Jefferson et al., 2011
Meprin-β is required for the physiological processing of APP.
“validating the role of meprin-β in the physiological processing of APP (Jefferson et al., 2011).”
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 Jefferson et al., 2011
Meprin-β can cleave APP near the N-terminal end to generate truncated fragments of 11 and 20 kDa (N-APP).
“meprin-β can cleave APP near the N-terminal end to generate truncated fragments of 11 and 20 kDa (N-APP)”
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 Jefferson et al., 2011
Meprin-β-generated APP fragments did not induce toxicity in neuronal cultures.
“These APP fragments did not induce toxicity in neuronal cultures”
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 Jefferson et al., 2011
N-APP fragments are not detected in meprin-β knockout mice.
“but not in meprin-β knockout mice”
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 Jefferson et al., 2011
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“Meprin (cid:2) -secretase (MEP) may cleave APP-695 at three sites in the N-terminal region after aa 124, 305, and 308 [15].”
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Self-citationMeprin β: A novel regulator of blood–brain barrier integrity
Gindorf, M., Storck, S. E., Ohler, A., Scharfenberg, F., Becker-Pauly, C., & Pietrzik, C. U. (2021) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x20905206 · Cited by 21
Self-citation
Metadata
- Authors
- Jefferson, T., Čaušević, M., auf dem Keller, U., Schilling, O., Isbert, S., Geyer, R., Maier, W., Tschickardt, S., Jumpertz, T., Weggen, S., Bond, J. S., Overall, C. M., Pietrzik, C. U., & Becker-Pauly, C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2011-08
- Volume
- 286
- Issue
- 31
- Pages
- 27741-27750
- ISSN
- 0021-9258
- Cited by
- 108
- References
- 4
- Language
- en
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