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Open access
Scientific Reports, volume 8, issue 1, publication number 298

N-domain of angiotensin-converting enzyme hydrolyzes human and rat amyloid-beta(1-16) peptides as arginine specific endopeptidase potentially enhancing risk of Alzheimer's disease

Kugaevskaya Elena V 1
Veselovsky Alexander V. 1
Indeykina Maria I 2, 3, 4
Solovyeva Nina I 1
Zharkova Maria S 1
Popov Igor A. 2, 3, 4
Nikolaev Eugene N 3, 4, 5
Makarov Alexander A. 2
Kozin Sergey A. 2
Publication typeJournal Article
Publication date2018-01-10
Quartile SCImago
Q1
Quartile WOS
Q2
Impact factor4.6
ISSN20452322
Multidisciplinary
Abstract
Alzheimer’s disease (AD) is a multifactorial neurodegenerative disorder. Amyloid-β (Aβ) aggregation is likely to be the major cause of AD. In contrast to humans and other mammals, that share the same Aβ sequence, rats and mice are invulnerable to AD-like neurodegenerative pathologies, and Aβ of these rodents (ratAβ) has three amino acid substitutions in the metal-binding domain 1-16 (MBD). Angiotensin-converting enzyme (ACE) cleaves Aβ-derived peptide substrates, however, there are contradictions concerning the localization of the cleavage sites within Aβ and the roles of each of the two ACE catalytically active domains in the hydrolysis. In the current study by using mass spectrometry and molecular modelling we have tested a set of peptides corresponding to MBDs of Aβ and ratAβ to get insights on the interactions between ACE and these Aβ species. It has been shown that the N-domain of ACE (N-ACE) acts as an arginine specific endopeptidase on the Aβ and ratAβ MBDs with C-amidated termini, thus assuming that full-length Aβ and ratAβ can be hydrolyzed by N-ACE in the same endopeptidase mode. Taken together with the recent data on the molecular mechanism of zinc-dependent oligomerization of Aβ, our results suggest a modulating role of N-ACE in AD pathogenesis.

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Kugaevskaya E. V. et al. N-domain of angiotensin-converting enzyme hydrolyzes human and rat amyloid-beta(1-16) peptides as arginine specific endopeptidase potentially enhancing risk of Alzheimer's disease // Scientific Reports. 2018. Vol. 8. No. 1. 298
GOST all authors (up to 50) Copy
Kugaevskaya E. V., Veselovsky A. V., Indeykina M. I., Solovyeva N. I., Zharkova M. S., Popov I. A., Nikolaev E. N., Mantsyzov A. B., Makarov A. A., Kozin S. A. N-domain of angiotensin-converting enzyme hydrolyzes human and rat amyloid-beta(1-16) peptides as arginine specific endopeptidase potentially enhancing risk of Alzheimer's disease // Scientific Reports. 2018. Vol. 8. No. 1. 298
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RIS Copy
TY - JOUR
DO - 10.1038/S41598-017-18567-5
UR - https://doi.org/10.1038%2FS41598-017-18567-5
TI - N-domain of angiotensin-converting enzyme hydrolyzes human and rat amyloid-beta(1-16) peptides as arginine specific endopeptidase potentially enhancing risk of Alzheimer's disease
T2 - Scientific Reports
AU - Kugaevskaya, Elena V
AU - Veselovsky, Alexander V.
AU - Indeykina, Maria I
AU - Solovyeva, Nina I
AU - Zharkova, Maria S
AU - Popov, Igor A.
AU - Nikolaev, Eugene N
AU - Makarov, Alexander A.
AU - Mantsyzov, Alexey B
AU - Kozin, Sergey A.
PY - 2018
DA - 2018/01/10 00:00:00
PB - Springer Nature
IS - 1
VL - 8
PMID - 29321566
SN - 2045-2322
ER -
BibTex
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BibTex Copy
@article{2018_Kugaevskaya
author = {Elena V Kugaevskaya and Alexander V. Veselovsky and Maria I Indeykina and Nina I Solovyeva and Maria S Zharkova and Igor A. Popov and Eugene N Nikolaev and Alexander A. Makarov and Alexey B Mantsyzov and Sergey A. Kozin},
title = {N-domain of angiotensin-converting enzyme hydrolyzes human and rat amyloid-beta(1-16) peptides as arginine specific endopeptidase potentially enhancing risk of Alzheimer's disease},
journal = {Scientific Reports},
year = {2018},
volume = {8},
publisher = {Springer Nature},
month = {jan},
url = {https://doi.org/10.1038%2FS41598-017-18567-5},
number = {1},
doi = {10.1038/S41598-017-18567-5}
}
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