Cu transfer from amyloid-4-16 to metallothionein-3: the role of the neurotransmitter glutamate and metallothionein-3 Zn(ii)-load states

被引：22

作者：

Santoro, Alice ^{[1
]}

Wezynfeld, Nina Ewa ^{[1
,2
]}

Stefaniak, Ewelina ^{[2
]}

Pomorski, Adam ^{[3
]}

Plonka, Dawid ^{[2
]}

Krezel, Artur ^{[3
]}

Bal, Wojciech ^{[2
]}

Faller, Peter ^{[1
]}

机构：

[1] Univ Strasbourg, CNRS, UMR 7177, Inst Chim, 4 Rue Blaise Pascal, F-67000 Strasbourg, France

[2] Polish Acad Sci, Inst Biochem & Biophys, Pawinskiego 5a, PL-02106 Warsaw, Poland

[3] Univ Wroclaw, Fac Biotechnol, Dept Biol Chem, F Joliot Curie 14a, PL-50383 Wroclaw, Poland

来源：

CHEMICAL COMMUNICATIONS | 2018年 / 54卷 / 89期

关键词：

ALZHEIMERS-DISEASE; COPPER; PEPTIDES; PROTEIN; ZN-7-METALLOTHIONEIN-3; MECHANISMS; BINDING; IONS; SWAP;

D O I：

10.1039/c8cc06221h

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Copper transfer from Cu(ii)amyloid-(4-16) to human Zn-7-metallothionein-3 can be accelerated by glutamate and by lowering the Zn-load of metallothionein-3 with EDTA. Glutamate facilitates the Cu(ii) release, and Zn4-6-metallothionein-3 react more rapidly. These mechanisms are additive, proving the intricate and interconnected network of zinc and copper trafficking between biomolecules.

引用

页码：12634 / 12637

页数：4

共 13 条

[1] A chemometric-assisted voltammetric analysis of free and Zn(II)-loaded metallothionein-3 states
Peris-Diaz, Manuel David
Richtera, Lukas
Zitka, Ondrej
Krezel, Artur
Adam, Vojtech
BIOELECTROCHEMISTRY, 2020, 134
[2] Structural Characterization of Cu(I)/Zn(II)-metallothionein-3 by Ion Mobility Mass Spectrometry and Top-Down Mass Spectrometry
Peris-Diaz, Manuel David
Wu, Sylwia
Mosna, Karolina
Liggett, Ellen
Barkhanskiy, Alexey
Orzel, Alicja
Barran, Perdita
Krezel, Artur
ANALYTICAL CHEMISTRY, 2023, 95 (29) : 10966 - 10974
[3] A distinct Cu4-thiolate cluster of human metallothionein-3 is located in the N-terminal domain
Roschitzki, B
Vasák, M
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 2002, 7 (06): : 611 - 616
[4] Resistance of Cu(Aβ4-16) to Copper Capture by Metallothionein-3 Supports a Function for the Aβ4-42 Peptide as a Synaptic CuII Scavenger
Wezynfeld, Nina E.
Stefaniak, Ewelina
Stachucy, Kinga
Drozd, Agnieszka
Plonka, Dawid
Drew, Simon C.
Krezel, Artur
Bal, Wojciech
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2016, 55 (29) : 8235 - 8238
[5] A distinct Cu4-thiolate cluster of human metallothionein-3 is located in the N-terminal domain
Bernd Roschitzki
Milan Vašák
JBIC Journal of Biological Inorganic Chemistry, 2002, 7 : 611 - 616
[6] Metallothionein-3 and carbonic anhydrase metalation properties with Zn(II) and Cd(II) change as a result of protein-protein interactions
Yuan, Amelia T.
Stillman, Martin J.
METALLOMICS, 2023, 15 (10)
[7] Metallothionein-3: 63Cu(I) binds to human 68Zn7-βα MT3 with no preference for Cu4-β cluster formation
Melenbacher, Adyn
Stillman, Martin J. J.
FEBS JOURNAL, 2023, 290 (17) : 4316 - 4341
[8] Oxidative pathways of apo, partially, and fully Zn(II)- and Cd(II)-metalated human metallothionein-3 are dominated by disulfide bond formation
Yuan, Amelia T.
Stillman, Martin J.
FEBS JOURNAL, 2025, 292 (03) : 619 - 634
[9] Membrane insertion exacerbates the α-Synuclein-Cu(II) dopamine oxidase activity: Metallothionein-3 targets and silences all α-synuclein-Cu(II) complexes
Calvo, Jenifer S.
Mulpuri, Neha V.
Dao, Alex
Qazi, Nabeeha K.
Meloni, Gabriele
FREE RADICAL BIOLOGY AND MEDICINE, 2020, 158 : 149 - 161
[10] Cysteine and glutathione trigger the Cu-Zn swap between Cu(II)-amyloid-β4-16 peptide and Zn7-metallothionein-3
Santoro, Alice
Wezynfeld, Nina Ewa
Vasak, Milan
Bal, Wojciech
Faller, Peter
CHEMICAL COMMUNICATIONS, 2017, 53 (85) : 11634 - 11637

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