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The Metalloprotease Meprin β Generates Amino Terminal-truncated Amyloid β Peptide Species
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Meprin-β expression in BACE-1/2 knockout fibroblasts is sufficient to generate Aβ.
“meprin-β expression in BACE-1/2 knockout fibroblasts was sufficient to generate Aβ (Bien et al., 2012).”
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 Bien et al., 2012
Meprin-β can behave as a β-secretase.
“suggesting that meprin-β can behave as a β-secretase.”
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 Bien et al., 2012
Meprin-β mRNA and protein levels are increased in AD patients compared to age-matched healthy individuals.
“several studies have reported increased mRNA and protein levels of meprin-β in AD patients compared to age-matched healthy individuals (Bien et al., 2012; Schlenzig et al., 2018).”
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 Bien et al., 2012
In vitro, meprin-β cleaves APP at the β-cleavage site and after the first and second amino acids of the Aβ sequence.
“Using a synthetic peptide mimicking APP/Aβ sequence, it was shown in vitro that meprin-β was able to cleave APP at the β-cleavage site and after the first and second amino acids of the Aβ sequence”
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 Bien et al., 2012
Meprin-β preferentially generates Aβ1-40 and an N-terminally truncated Aβ (Aβ2-X).
“and preferentially generates Aβ1–40 and a N-terminally truncated Aβ (Aβ2–X)”
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 Bien et al., 2012
Aβ2-X is more prone to aggregation than Aβ1-40.
“which is more prone to aggregation than Aβ1–40.”
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 Bien et al., 2012
Unlike BACE-1, meprin-β cleaves APP on the plasma membrane before it undergoes endocytosis.
“Unlike BACE-1, meprin-β cleaves APP on the plasma membrane before it undergoes endocytosis”
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 Bien et al., 2012
Aβ2-X can only be generated by membrane-bound meprin-β and not by the soluble form after ADAM10/17-mediated shedding.
“Aβ2–X can only be generated by membrane-bound meprin-β and not by the soluble form after ADAM10/17-mediated shedding (Bien et al., 2012).”
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 Bien et al., 2012
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Sorted by citations
Spitzer, P., Condic, M., Herrmann, M., Oberstein, T. J., Scharin-Mehlmann, M., Gilbert, D. F., Friedrich, O., Grömer, T., Kornhuber, J., Lang, R., et al. (2016) · Scientific Reports · doi:10.1038/srep32228 · Cited by 128
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Secretases in Alzheimer's disease: Novel insights into proteolysis of APP and TREM2
Lichtenthaler, S. F., Tschirner, S. K., & Steiner, H. (2022) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2021.09.003 · Cited by 60
Experimental evidence for temporal uncoupling of brain Aβ deposition and neurodegenerative sequelae
Rother, C., Uhlmann, R. E., Müller, S. A., Schelle, J., Skodras, A., Obermüller, U., Häsler, L. M., Lambert, M., Baumann, F., Xu, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34538-5 · Cited by 28
Meprin 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
- Bien, J., Jefferson, T., Čaušević, M., Jumpertz, T., Munter, L., Multhaup, G., Weggen, S., Becker-Pauly, C., & Pietrzik, C. U.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2012-09
- Volume
- 287
- Issue
- 40
- Pages
- 33304-33313
- ISSN
- 0021-9258
- Cited by
- 136
- References
- 5
- Language
- en
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