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 type: Journal Article
Publication date: 2018-01-10
PubMed ID:
29321566
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.
Citations by journals
1
|
|
Mass Spectrometry Reviews
|
Mass Spectrometry Reviews
1 publication, 10%
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Protein and Peptide Letters
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Protein and Peptide Letters
1 publication, 10%
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Journal of Alzheimer's Disease
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Journal of Alzheimer's Disease
1 publication, 10%
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Frontiers in Neuroscience
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Frontiers in Neuroscience
1 publication, 10%
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Acta neuropathologica communications
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Acta neuropathologica communications
1 publication, 10%
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Tissue and Cell
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Tissue and Cell
1 publication, 10%
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Journal of Neurochemistry
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Journal of Neurochemistry
1 publication, 10%
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International Journal of Epidemiology
|
International Journal of Epidemiology
1 publication, 10%
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Process Biochemistry
|
Process Biochemistry
1 publication, 10%
|
1
|
Citations by publishers
1
2
|
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Wiley
|
Wiley
2 publications, 20%
|
Elsevier
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Elsevier
2 publications, 20%
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Bentham Science
|
Bentham Science
1 publication, 10%
|
IOS Press
|
IOS Press
1 publication, 10%
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Frontiers Media S.A.
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Frontiers Media S.A.
1 publication, 10%
|
Springer Nature
|
Springer Nature
1 publication, 10%
|
Oxford University Press
|
Oxford University Press
1 publication, 10%
|
1
2
|
- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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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
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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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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 -
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@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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