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Amyloid-β containing isoaspartate 7 as potential biomarker and drug target in Alzheimer's disease

Sergey Aleksandrovich Kozin 1
Sergey Aleksandrovich Kozin
Vladimir Aleksandrovich Mitkevich 1
Vladimir Aleksandrovich Mitkevich
Alexander Aleksandrovich Makarov 1
Alexander Aleksandrovich Makarov
Published 2016-07-07
Focus articleVolume 26, Issue 4, 269-275
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Kozin S. A., Mitkevich V. A., Makarov A. A. Amyloid-β containing isoaspartate 7 as potential biomarker and drug target in Alzheimer's disease // Mendeleev Communications. 2016. Vol. 26. No. 4. pp. 269-275.
GOST all authors (up to 50) Copy
Kozin S. A., Mitkevich V. A., Makarov A. A. Amyloid-β containing isoaspartate 7 as potential biomarker and drug target in Alzheimer's disease // Mendeleev Communications. 2016. Vol. 26. No. 4. pp. 269-275.
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TY - JOUR
DO - 10.1016/j.mencom.2016.07.001
UR - https://mendcomm.colab.ws/publications/10.1016/j.mencom.2016.07.001
TI - Amyloid-β containing isoaspartate 7 as potential biomarker and drug target in Alzheimer's disease
T2 - Mendeleev Communications
AU - Kozin, Sergey Aleksandrovich
AU - Mitkevich, Vladimir Aleksandrovich
AU - Makarov, Alexander Aleksandrovich
PY - 2016
DA - 2016/07/07
PB - Mendeleev Communications
SP - 269-275
IS - 4
VL - 26
ER -
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@article{2016_Kozin,
author = {Sergey Aleksandrovich Kozin and Vladimir Aleksandrovich Mitkevich and Alexander Aleksandrovich Makarov},
title = {Amyloid-β containing isoaspartate 7 as potential biomarker and drug target in Alzheimer's disease},
journal = {Mendeleev Communications},
year = {2016},
volume = {26},
publisher = {Mendeleev Communications},
month = {Jul},
url = {https://mendcomm.colab.ws/publications/10.1016/j.mencom.2016.07.001},
number = {4},
pages = {269--275},
doi = {10.1016/j.mencom.2016.07.001}
}
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Kozin, Sergey Aleksandrovich, et al. “Amyloid-β containing isoaspartate 7 as potential biomarker and drug target in Alzheimer's disease.” Mendeleev Communications, vol. 26, no. 4, Jul. 2016, pp. 269-275. https://mendcomm.colab.ws/publications/10.1016/j.mencom.2016.07.001.
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Abstract

Recent data about structure, interaction with biometals, aggregation state, proteolysis by angiotensin converting enzyme, neurotoxicity and amyloidogenicity of amyloid-β containing isoaspartate 7 (isoAsp7-Aβ) in comparison with intact amyloid-β are summarized. Possible role of isoAsp7-Aβ as a prospective biomarker for molecular diagnostics and drug target in anti-amyloid therapy of Alzheimer's disease is discussed.

References

1.
10.1016/j.mencom.2016.07.001_bib0005
Alzheimer
Neurologisches Centralblatt, 1906
2.
10.1016/j.mencom.2016.07.001_bib0010
Alzheimer's & Dementia, 2014
3.
10.1016/j.mencom.2016.07.001_bib0015
Gavrilova
Farmakoterapiya bolezni Altsgeimera (Pharmacological Treatment of Alzheimer's Disease), 2007
4.
Alzheimer's Disease
Querfurth H.W., LaFerla F.M.
New England Journal of Medicine, 2010
5.
Alzheimer's Disease
Cummings J.L.
New England Journal of Medicine, 2004
6.
Alzheimer’s disease drug-development pipeline: few candidates, frequent failures
Cummings J.L., Morstorf T., Zhong K.
Alzheimer's Research and Therapy, 2014
8.
Treatment Strategies Targeting Amyloid  -Protein
Schenk D., Basi G.S., Pangalos M.N.
Cold Spring Harbor perspectives in medicine, 2012
9.
Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
Shankar G.M., Li S., Mehta T.H., Garcia-Munoz A., Shepardson N.E., Smith I., Brett F.M., Farrell M.A., Rowan M.J., Lemere C.A., Regan C.M., Walsh D.M., Sabatini B.L., Selkoe D.J.
Nature Medicine, 2008
10.
Blood-Borne Amyloid-  Dimer Correlates with Clinical Markers of Alzheimer's Disease
Villemagne V.L., Perez K.A., Pike K.E., Kok W.M., Rowe C.C., White A.R., Bourgeat P., Salvado O., Bedo J., Hutton C.A., Faux N.G., Masters C.L., Barnham K.J.
Journal of Neuroscience, 2010
13.
Zinc Binding to Alzheimer's Aβ(1–16) Peptide Results in Stable Soluble Complex
Kozin S.A., Zirah S., Rebuffat S., Hui Bon Hoa G., Debey P.
Biochemical and Biophysical Research Communications, 2001
14.
Zinc-induced dimerization of the amyloid-β metal-binding domain 1–16 is mediated by residues 11–14
Kozin S.A., Mezentsev Y.V., Kulikova A.A., Indeykina M.I., Golovin A.V., Ivanov A.S., Tsvetkov P.O., Makarov A.A.
Molecular BioSystems, 2011
15.
Zinc ions promote Alzheimer A  aggregation via population shift of polymorphic states
Miller Y., Ma B., Nussinov R.
Proceedings of the National Academy of Sciences of the United States of America, 2010
16.
3D structure of Alzheimer's amyloid- (1-42) fibrils
Lührs T., Ritter C., Adrian M., Riek-Loher D., Bohrmann B., Döbeli H., Schubert D., Riek R.
Proceedings of the National Academy of Sciences of the United States of America, 2005
17.
p3 peptide, a truncated form of Aβ devoid of synaptotoxic effect, does not assemble into soluble oligomers
Dulin F., Léveillé F., Ortega J.B., Mornon J., Buisson A., Callebaut I., Colloc'h N.
FEBS Letters, 2008
18.
Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., Rowan M.J., Selkoe D.J.
Nature, 2002
19.
Untangling the pathophysio-chemistry of β-amyloid
Mattson M.P.
Nature Structural and Molecular Biology, 1995
21.
Cytosolic and nuclear aggregation of the amyloid ?-peptide following its expression in the endoplasmic reticulum
22.
Nuclear and Cytoplasmic Localization of the β-Amyloid Peptide (1–43) in Transfected 293 Cells
Johnstone E.M., Babbey L.E., Stephenson D., Paul D.C., Santerre R.F., Clemens J.A., Williams D.C., Little S.P.
Biochemical and Biophysical Research Communications, 1996
23.
Intracellular Aβ42 activates p53 promoter: a pathway to neurodegeneration in Alzheimer's disease
Ohyagi Y., Asahara H., Chui D., Tsuruta Y., Sakae N., Miyoshi K., Yamada T., Kikuchi H., Taniwaki T., Murai H., Ikezoe K., Furuya H., Kawarabayashi T., Shoji M., Checler F., et. al.
FASEB Journal, 2004
24.
Zinc-Induced Interaction of the Metal-Binding Domain of Amyloid-β Peptide with DNA
Khmeleva S.A., Mezentsev Y.V., Kozin S.A., Tsvetkov P.O., Ivanov A.S., Bodoev N.V., Makarov A.A., Radko S.P.
Journal of Alzheimer's Disease, 2013
25.
Induction of β(A4)-amyloid in primates by injection of Alzheimer’s disease brain homogenate
Baker H.F., Ridley R.M., Duchen L.W., Crow T.J., Bruton C.J.
Molecular Neurobiology, 1994
26.
Very long term studies of the seeding of β-amyloidosis in primates
Ridley R.M., Baker H.F., Windle C.P., Cummings R.M.
Journal of Neural Transmission, 2005
27.
Soluble A  Seeds Are Potent Inducers of Cerebral  -Amyloid Deposition
Langer F., Eisele Y.S., Fritschi S.K., Staufenbiel M., Walker L.C., Jucker M.
Journal of Neuroscience, 2011
28.
De novo induction of amyloid-β deposition in vivo
Morales R., Duran-Aniotz C., Castilla J., Estrada L.D., Soto C.
Molecular Psychiatry, 2011
29.
Exogenous seeding of cerebral β-amyloid deposition in βAPP-transgenic rats
Rosen R.F., Fritz J.J., Dooyema J., Cintron A.F., Hamaguchi T., Lah J.J., LeVine H., Jucker M., Walker L.C.
Journal of Neurochemistry, 2011
30.
Bioluminescence imaging of Aβ deposition in bigenic mouse models of Alzheimer's disease
Watts J.C., Giles K., Grillo S.K., Lemus A., DeArmond S.J., Prusiner S.B.
Proceedings of the National Academy of Sciences of the United States of America, 2011
31.
Induction of cerebral β-amyloidosis: Intracerebral versus systemic Aβ inoculation
Eisele Y.S., Bolmont T., Heikenwalder M., Langer F., Jacobson L.H., Yan Z., Roth K., Aguzzi A., Staufenbiel M., Walker L.C., Jucker M.
Proceedings of the National Academy of Sciences of the United States of America, 2009
32.
Peripherally Applied Aβ-Containing Inoculates Induce Cerebral β-Amyloidosis
Eisele Y.S., Obermüller U., Heilbronner G., Baumann F., Kaeser S.A., Wolburg H., Walker L.C., Staufenbiel M., Heikenwalder M., Jucker M.
Science, 2010
33.
Exogenous Induction of Cerebral  -Amyloidogenesis Is Governed by Agent and Host
Meyer-Luehmann M., Coomaraswamy J., Bolmont T., Kaeser S., Schaefer C., Kilger E., Neuenschwander A., Abramowski D., Frey P., Jaton A.L., Vigouret J., Paganetti P., Walsh D.M., Mathews P.M., Ghiso J., et. al.
Science, 2006
34.
Purified and synthetic Alzheimer's amyloid beta (A ) prions
Stöhr J., Watts J.C., Mensinger Z.L., Oehler A., Grillo S.K., DeArmond S.J., Prusiner S.B., Giles K.
Proceedings of the National Academy of Sciences of the United States of America, 2012
35.
Extracellular phosphorylation of the amyloid β-peptide promotes formation of toxic aggregates during the pathogenesis of Alzheimer's disease
Kumar S., Rezaei-Ghaleh N., Terwel D., Thal D.R., Richard M., Hoch M., Mc Donald J.M., Wüllner U., Glebov K., Heneka M.T., Walsh D.M., Zweckstetter M., Walter J.
EMBO Journal, 2011
36.
Prion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-β
Nussbaum J.M., Schilling S., Cynis H., Silva A., Swanson E., Wangsanut T., Tayler K., Wiltgen B., Hatami A., Rönicke R., Reymann K., Hutter-Paier B., Alexandru A., Jagla W., Graubner S., et. al.
Nature, 2012
37.
Isomerization of the Asp7 Residue Results in Zinc‐Induced Oligomerization of Alzheimer’s Disease Amyloid β(1–16) Peptide
Tsvetkov P.O., Popov I.A., Nikolaev E.N., Archakov A.I., Makarov A.A., Kozin S.A.
ChemBioChem, 2008
40.
Supermetallization of peptides and proteins during electrospray ionization
Kostyukevich Y., Kononikhin A., Popov I., Indeykina M., Kozin S.A., Makarov A.A., Nikolaev E.
Journal of Mass Spectrometry, 2015
41.
Characterization of the ZnII Binding to the Peptide Amyloid-β1-16 linked to Alzheimer's Disease
Mekmouche Y., Coppel Y., Hochgräfe K., Guilloreau L., Talmard C., Mazarguil H., Faller P.
ChemBioChem, 2005
42.
Zinc binding properties of the amyloid fragment Aβ(1–16) studied by electrospray-ionization mass spectrometry
Zirah S., Rebuffat S., Kozin S.A., Debey P., Fournier F., Lesage D., Tabet J.
International Journal of Mass Spectrometry, 2003
43.
Structural Changes of Region 1-16 of the Alzheimer Disease Amyloid β-Peptide upon Zinc Binding and in Vitro Aging
Zirah S., Kozin S.A., Mazur A.K., Blond A., Cheminant M., Ségalas-Milazzo I., Debey P., Rebuffat S.
Journal of Biological Chemistry, 2006
44.
Minimal Zn2+ Binding Site of Amyloid-β
Tsvetkov P.O., Kulikova A.A., Golovin A.V., Tkachev Y.V., Archakov A.I., Kozin S.A., Makarov A.A.
Biophysical Journal, 2010
45.
The English (H6R) familial Alzheimer's disease mutation facilitates zinc-induced dimerization of the amyloid-β metal-binding domain
Kozin S.A., Kulikova A.A., Istrate A.N., Tsvetkov P.O., Zhokhov S.S., Mezentsev Y.V., Kechko O.I., Ivanov A.S., Polshakov V.I., Makarov A.A.
Metallomics, 2015
46.
Phosphorylation of Ser8 promotes zinc-induced dimerization of the amyloid-β metal-binding domain
Kulikova A.A., Tsvetkov P.O., Indeykina M.I., Popov I.A., Zhokhov S.S., Golovin A.V., Polshakov V.I., Kozin S.A., Nudler E., Makarov A.A.
Molecular BioSystems, 2014
48.
Structural studies of the tethered N-terminus of the Alzheimer's disease amyloid-β peptide
Nisbet R.M., Nuttall S.D., Robert R., Caine J.M., Dolezal O., Hattarki M., Pearce L.A., Davydova N., Masters C.L., Varghese J.N., Streltsov V.A.
Proteins: Structure, Function and Genetics, 2013
49.
10.1016/j.mencom.2016.07.001_bib0245
Adzhubei
J. Biomol. Struct. Dyn., 2016
50.
Polyproline-II Helix in Proteins: Structure and Function
Adzhubei A.A., Sternberg M.J., Makarov A.A.
Journal of Molecular Biology, 2013
52.
Alzheimer's disease amyloidogenic glycoprotein: expression pattern in rat brain suggests a role in cell contact.
Shivers B.D., Hilbich C., Multhaup G., Salbaum M., Beyreuther K., Seeburg P.H.
EMBO Journal, 1988
53.
NMR solution structure of rat Aβ(1-16): Toward understanding the mechanism of rats' resistance to Alzheimer's disease
Istrate A., Tsvetkov P., Mantsyzov A., Kulikova A., Kozin S., Makarov A., Polshakov V.
Biophysical Journal, 2012
54.
ESI-MS identification of the minimal zinc-binding center in natural isoforms of β-amyloid domain 1–16
Popov I.A., Indeikina M.I., Kononikhin A.S., Starodubtseva N.L., Kozin S.A., Makarov A.A., Nikolaev E.N.
Molecular Biology, 2013
55.
Interplay of histidine residues of the Alzheimer's disease Aβ peptide governs its Zn-induced oligomerization
Istrate A.N., Kozin S.A., Zhokhov S.S., Mantsyzov A.B., Kechko O.I., Pastore A., Makarov A.A., Polshakov V.I.
Scientific Reports, 2016
56.
10.1016/j.mencom.2016.07.001_bib0280
Mezentsev
J. Biomol. Struct. Dyn., 2016
57.
Biological Significance of Isoaspartate and Its Repair System
Shimizu T., Matsuoka Y., Shirasawa T.
Biological and Pharmaceutical Bulletin, 2005
59.
Isoaspartate Formation and Neurodegeneration in Alzheimer's Disease
Shimizu T., Watanabe A., Ogawara M., Mori H., Shirasawa T.
Archives of Biochemistry and Biophysics, 2000
60.
Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease.
Roher A.E., Lowenson J.D., Clarke S., Wolkow C., Wang R., Cotter R.J., Reardon I.M., Zürcher-Neely H.A., Heinrikson R.L., Ball M.J.
Journal of Biological Chemistry, 1993
61.
beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease.
Roher A.E., Lowenson J.D., Clarke S., Woods A.S., Cotter R.J., Gowing E., Ball M.J.
Proceedings of the National Academy of Sciences of the United States of America, 1993
62.
10.1016/j.mencom.2016.07.001_bib0310
Tsvetkov
Biofizika, 2009
64.
HSP70 protects human neuroblastoma cells from apoptosis and oxidative stress induced by amyloid peptide isoAsp7-Aβ(1–42)
Yurinskaya M.M., Mitkevich V.A., Kozin S.A., Evgen'ev M.B., Makarov A.A., Vinokurov M.G.
Cell Death and Disease, 2015
65.
Heat-shock protein HSP70 protects neuroblastoma cells SK-N-SH from the neurotoxic effects of hydrogen peroxide and the β-amyloid peptide
Yurinskaya M.M., Mit’kevich V.A., Barykin E.P., Garbuz D.G., Evgen’ev M.B., Makarov A.A., Vinokurov M.G.
Molecular Biology, 2015
66.
Isomerization of Asp7 increases the toxic effects of amyloid β and its phosphorylated form in SH-SY5Y neuroblastoma cells
Barykin E.P., Petrushanko I.Y., Burnysheva K.M., Makarov A.A., Mitkevich V.A.
Molecular Biology, 2016
67.
Isomerization of Asp7 leads to increased toxic effect of amyloid-β42 on human neuronal cells
Mitkevich V.A., Petrushanko I.Y., Yegorov Y.E., Simonenko O.V., Vishnyakova K.S., Kulikova A.A., Tsvetkov P.O., Makarov A.A., Kozin S.A.
Cell Death and Disease, 2013
69.
Heat-shock protein HSP70 reduces the secretion of TNFα by neuroblastoma cells and human monocytes induced with beta-amyloid peptides
Yurinskaya M.M., Mit’kevich V.A., Evgen’ev M.B., Makarov A.A., Vinokurov M.G.
Molecular Biology, 2016
70.
Synthesis, aggregation, and neurotoxicity of the Alzheimer's Abeta1-42 amyloid peptide and its isoaspartyl isomers.
Fukuda H., Shimizu T., Nakajima M., Mori H., Shirasawa T.
Bioorganic and Medicinal Chemistry Letters, 1999
73.
Quantification of Modified Amyloid β Peptides in Alzheimer Disease and Down Syndrome Brains
Hosoda R., Saido T.C., Otvos L., Arai T., Mann D.M., Lee V.M., Trojanowski J.Q., Iwatsubo T.
Journal of Neuropathology and Experimental Neurology, 1998
75.
Peripherally Applied Synthetic Peptide isoAsp7-Aβ(1-42) Triggers Cerebral β-Amyloidosis
Kozin S.A., Cheglakov I.B., Ovsepyan A.A., Telegin G.B., Tsvetkov P.O., Lisitsa A.V., Makarov A.A.
Neurotoxicity Research, 2013
76.
Accelerated Amyloid Deposition in the Brains of Transgenic Mice Coexpressing Mutant Presenilin 1 and Amyloid Precursor Proteins
Borchelt D.R., Ratovitski T., van Lare J., Lee M.K., Gonzales V., Jenkins N.A., Copeland N.G., Price D.L., Sisodia S.S.
Neuron, 1997
77.
Characterization of amyloid deposition in the APPswe/PS1dE9 mouse model of Alzheimer disease
Garcia-Alloza M., Robbins E.M., Zhang-Nunes S.X., Purcell S.M., Betensky R.A., Raju S., Prada C., Greenberg S.M., Bacskai B.J., Frosch M.P.
Neurobiology of Disease, 2006
78.
Chemical characterization of A beta 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease
Gowing E., Roher A.E., Woods A.S., Cotter R.J., Chaney M., Little S.P., Ball M.J.
Journal of Biological Chemistry, 1994
79.
A novel pathway for amyloid precursor protein processing
Portelius E., Price E., Brinkmalm G., Stiteler M., Olsson M., Persson R., Westman-Brinkmalm A., Zetterberg H., Simon A.J., Blennow K.
Neurobiology of Aging, 2011
80.
Intracerebral Injection of Metal-Binding Domain of Aβ Comprising the Isomerized Asp7 Increases the Amyloid Burden in Transgenic Mice
Kulikova A.A., Cheglakov I.B., Kukharsky M.S., Ovchinnikov R.K., Kozin S.A., Makarov A.A.
Neurotoxicity Research, 2016
81.
Capabilities of MS for Analytical Quantitative Determination of the Ratio of α- and βAsp7 Isoforms of the Amyloid-β Peptide in Binary Mixtures
Indeykina M.I., Popov I.A., Kozin S.A., Kononikhin A.S., Kharybin O.N., Tsvetkov P.O., Makarov A.A., Nikolaev E.N.
Analytical Chemistry, 2011
83.
Decreased amyloid-β and increased neuronal hyperactivity by immunotherapy in Alzheimer's models
Busche M.A., Grienberger C., Keskin A.D., Song B., Neumann U., Staufenbiel M., Förstl H., Konnerth A.
Nature Neuroscience, 2015
84.
Regulation of Presynaptic Ca2+, Synaptic Plasticity and Contextual Fear Conditioning by a N-terminal  -Amyloid Fragment
Lawrence J.L., Tong M., Alfulaij N., Sherrin T., Contarino M., White M.M., Bellinger F.P., Todorovic C., Nichols R.A.
Journal of Neuroscience, 2014
85.
Peripherally Applied Synthetic Tetrapeptides HAEE and RADD Slow Down the Development of Cerebral β-Amyloidosis in AβPP/PS1 Transgenic Mice
Tsvetkov P.O., Cheglakov I.B., Ovsepyan A.A., Mediannikov O.Y., Morozov A.O., Telegin G.B., Kozin S.A.
Journal of Alzheimer's Disease, 2015
86.
Aisen P.S., Gauthier S., Ferris S.H., Saumier D., Haine D., Garceau D., Duong A., Suhy J., Oh J., Lau W.C., Sampalis J.
Archives of Medical Science, 2011
87.
Targeting soluble Aβ peptide with Tramiprosate for the treatment of brain amyloidosis
Gervais F., Paquette J., Morissette C., Krzywkowski P., Yu M., Azzi M., Lacombe D., Kong X., Aman A., Laurin J., Szarek W.A., Tremblay P.
Neurobiology of Aging, 2007