Metal swap between Zn 7 metallothionein 3 and amyloid β Cu protects against amyloid β toxicity
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1 Metal swap between Zn 7 metallothionein 3 and amyloid β Cu protects against amyloid β toxicity Supplementary Information Gabriele Meloni 1, Vanessa Sonois 2,3, Tamara Delaine 2, Luc Guilloreau 2, Audrey Gillet 2, Justin Teissié 3, Peter Faller 2 & Milan Vašák 1 1 Department of Biochemistry, University of Zürich, Winterthurerstrasse 190, CH 8057 Zürich, Switzerland, 2 Laboratoire de Chimie de Coordination and 3 Institut de Pharmacologie et Biologie Structurale, 205 route de Narbonne, Toulouse Cedex, France
2 Supplementary Figure 1 Supplementary Figure 1. The d d region of absorption spectra of soluble Aβ 1 16 Cu(II) in the presence and absence of Zn 7 MT 3. Absorption spectra of 257 µm Aβ 1 16 Cu(II) (red), upon the reaction with 0.2 mol equivalent Zn 7 MT 3 (green), and of Aβ 1 16, (black) in 20 mm Hepes NaOH, 100 mm NaCl, ph 7.4. The absence of d d transitions of Aβ 1 16 Cu(II) upon the reaction with Zn 7 MT 3 confirms the metal swap. 2
3 Supplementary Figure 2 Supplementary Figure 2. Circular dichroism (CD) spectra confirming the formation of Cu(I) 4 Zn 4 MT 3 upon the reaction of Zn 7 MT 3 with Aβ 1 40 Cu(II). CD spectra of 25 µm Aβ 1 40 (black), upon the reaction of 25 µm CuCl 2 with 25 µm Zn 7 MT 3 (cyan), and upon the reaction of 25 µm Aβ 1 40 Cu(II) with 25 µm Zn 7 MT 3 (blue) overlaid with the arithmetic sum of the cyan and black spectra (red) in 20 mm Tris HCl, 100 mm, NaCl, ph 7.4. The identity of the blue and red spectra confirms the cooperative formation of Cu(I) 4 Zn 4 MT 3 in the reaction between Aβ 1 40 Cu(II) and Zn 7 MT Meloni, G., Faller, P. & Vašák, M. Redox silencing of copper in metal linked neurodegenerative disorders: reaction of Zn 7 metallothionein 3 with Cu 2+ ions. J. Biol. Chem. 282, (2007). 3
4 Supplementary Figure 3 Supplementary Figure 3. ESI MS data of the reaction products between Aβ 1 28 Cu(II) and Zn 7 MT 3. ESI MS data showing the formation of Aβ Zn(II) upon the reaction of Aβ Cu(II) with 67 Zn 7 MT 3. The samples were prepared using > 95% enriched 67 Zn and 63 Cu isotopes. Observed masses are summarized in the Supplementary Table 1. 4
5 Supplementary Figure 4 Supplementary Figure 4. Effect of the ROS production on cell viability. SH SY5Y neuroblastoma cells viability was determined by MTT assay after 24 h incubation at 37 C (cells were cultured in DMEM containing fetal calf serum): A) control; B) 40 µm Aβ 1 40 Cu(II); C) 40 µm Aβ 1 40 Cu(II) + 20 µm Zn 7 MT 3; D); 40 µm Aβ 1 40 Cu(II) + 20 µm Cu 8 MT 3; E) 20 µm Zn 7 MT 3; F) 40 µm Aβ 1 40 Zn(II); G) 40 µm Aβ 1 40 ; H) 40 µm Cu(II); all experiments were carried out in the presence of 300 µm ascorbate. For comparison cell viability in the presence of increasing H 2 O 2 concentrations is also shown. H 2 O 2 was used as the source of ROS in the cell culture medium. H 2 O 2 concentrations: I) 1 mm; J) 300 µm; K) 100 µm; L) 60 µm; M) 30 µm; N) 10 µm; O) 0.1 µm. The studies showed that the cellular toxicity stems from the ROS generated by redox cycling of Cu(II) in the presence of ascorbate. 5
6 Supplementary Figure 5 Supplementary Figure 5. Aβ 1 40 Cu(II) formation in the diluted DMEM buffer determined by EPR and ultrafiltration experiments. a) EPR spectra of 40 µm Cu(II) (red) and 40 µm Aβ 1 40 Cu(II) (blue) in DMEM diluted 1:10 with 20 mm Hepes NaOH, 100 mm NaCl, ph 7.4. As a control the EPR spectrum of 40 µm Aβ 1 40 Cu(II) (black) in 20 mm Hepes NaOH, 100 mm NaCl, ph 7.4, is also shown. The spectrum of Aβ 1 40 Cu(II) in the medium (blue) resembles much more the spectrum of the Aβ 1 40 Cu(II) (black) than Cu(II) in the medium (red), suggesting that most of the Cu(II) was bound to Aβ 1 40 in these conditions. This is best seen for the g signal (indicated by an arrow). The analyses of EPR spectra indicate that in DMEM diluted 1:10 with 20 mm Hepes NaOH, 100 mm NaCl, ph 7.4, the Aβ 1 40 Cu(II) complex represents the major species (~70%, see also panel b). b) Distribution of Cu(II) (40 µm) in DMEM diluted 1:10 with 20 mm Hepes NaOH, 100 mm NaCl, ph 7.4, in the presence and absence of Aβ 1 40 (40 µm). The copper concentration was determined by atomic absorption spectroscopy following the sample separation on a 3 kda cut off membrane. F and S indicate the flow through and the retained fractions, respectively. The results are the average of three independent measurements following normalization. Error bars show s.d.. The degree of Aβ 1 40 retention by 3 kda ultrafiltration membrane (> 90%) was assessed by size-exclusion chromatography. 6
7 Supplementary Figure 6 Supplementary Figure 6. Luminescence spectra of Zn 7 MT 3 upon the reaction with Aβ 1 40 Cu(II) in diluted DMEM buffer. Luminescence spectra of 40 µm Cu(II) (black), 40 µm Aβ 1 40 Cu(II) (green) and upon the addition of 10 µm Zn 7 MT 3 (blue) in DMEM diluted 1:10 with 20 mm Hepes NaOH, 100 mm NaCl, ph 7.4. As a control the luminescence spectrum of 10 µm Zn 7 MT 3 to which 4 mol equivalents of Cu(II) were added (red). The identity of the blue and red spectra confirms the formation of Cu(I) 4 Zn 4 MT 3. 7
8 Supplementary Figure 7 Supplementary Figure 7. ESI MS characterization of Aβ 1-28, Aβ 1-40 and human apomt-3. a) ESI MS spectra of Aβ 1-28 in 10 mm NH 4 OAc, 50% acetonitrile (ph = 7.5). The calculated mass of the peptide is Da. b) ESI MS spectra of Aβ 1-40 in 10 mm NH 4 OAc, 50% MeOH (ph = 7.5). The calculated mass of the peptide is Da. The mass peaks designated (*) indicate the Na + adducts. c) c) ESI MS spectra of apomt 3 in 0.2% formic acid, 50% acetonitrile (ph = 2). The calculated mass of the protein is Da. 8
9 Supplementary Table 1 Supplementary Table 1. ESI MS data summarizing molecular masses of the reaction products between Aβ 1 28 Cu(II) and Zn 7 MT 3. The superscripts in the table refer to the ESI MS spectra shown in Supplementary Fig. 3. Aβ 1 28 a Samples Aβ Cu(II) b Aβ Zn(II) c Aβ 1 28 Cu(II) + Zn 7 MT 3 (after mixing) d Aβ 1 28 Cu(II) + Zn 7 MT 3 (approx. 1 min after reaction) e Species observed Aβ 1 28 (Da) Aβ 1 28 Cu(II) (Da) Aβ 1 28 Zn(II) (Da) (3323.1) Supplementary Table 2 Supplementary Table 2. ESI MS data summarizing the MT 3 complexes formed upon the reaction of Zn 7 MT 3 with free Cu(II) and Aβ 1 28 Cu(II). ESI MS data confirm the formation of Cu(I) 4 Zn 4 MT 3 upon the reaction of Zn 7 MT 3 with Aβ 1 28 Cu(II) (all samples contained both metals at natural abundance). For comparison the masses of species obtained upon the titration of Zn 7 MT 3 with free Cu(II) are also presented 1. Samples Zn 7 MT 3 Zn 7 MT 3 + Cu(II) Aβ 1 28 Cu(II) + Zn 7 MT 3 Species observed Zn 7 MT 3 (Da) Cu(I) 4 Zn 4 MT 3 (Da) Meloni, G., Faller, P. & Vašák, M. Redox silencing of copper in metal linked neurodegenerative disorders: reaction of Zn 7 metallothionein 3 with Cu 2+ ions. J. Biol. Chem. 282, (2007). 9
10 Supplementary Methods ESI Q TOF MS measurements. Samples were prepared by mixing Aβ 1 28 Cu(II) (125 µm) with Zn 7 MT 3 (285 µm) in 10 mm 4 ethylmorpholine buffer, ph 7.2, at stoichiometries of 1:1, 4:1, and 8:1. Both the presence of isotopic distribution of Cu and Zn together with their closely similar atomic masses make the identification of various metalloforms by MS rather difficult. To facilitate their detection the samples were prepared using > 95% enriched 63 Cu and 67 Zn isotopes. Upon mixing, the samples were diluted into 50% 10 mm ammonium acetate, 50% methanol (or 50% acetonitrile), ph 7.5, and immediately analyzed. Mass spectra have been obtained on a nano ESI MS Q TOF Ultima API mass sprectrometer (Micromass, UK). Cell viability assay followed with 5 carboxyfluorescein diacetate, acetoxymethyl ester. Human neuroblastoma SH SY5Y cells were grown in DMEM (Invitrogen) supplemented with 10% fetal calf serum (Eurobio), L glutamine (2 mm) and 0.5% gentamycin at 37 C in humidified 5% CO 2 air. To assess the effects of Aβ 1 40 Cu(II) and Zn 7 MT 3 on the Aβ 1 40 induced toxicity, cells were exposed to freshly prepared 40 µm Aβ 1 40 Cu(II) in the presence of 20 µm Zn 7 MT 3 or Cu 8 MT 3 and 300 µm ascorbate was added. As a control, cells were grown in the absence and presence of Aβ 1 40 Cu(II). Cell viability was measured in 24 well plates using the fluorescence dye 5 CFDA, AM added to the medium. Briefly, cells exposed to cell permeant 5 CFDA, which is hydrolyzed by intracellular esterases, produces a green fluorescence when exposed to 492 nm light and is used to identify live cells. Cell viability is expressed as the ratio of the signal obtained from treated and control cultures without Aβ 1 40 Cu(II). The cell viability was assessed after 24 h by fluorescence microscopy using a CCD camera. Since the fluorescence dye 5 CFDA, AM was found sensitive to H 2 O 2, cell viability in the presence of H 2 O 2 was determined through the reduction of MTT. In the MTT assay 24 well plates were used. 25 µl of MTT (5 mg/ml solution in phosphate buffered saline (PBS)) was added to each well (containing 500 µl 10
11 medium) and incubated for 3 h. Subsequently, 1 ml DMSO was added and the reduced MTT was measured by absorption at 570 nm. Similar cell viability experiments were also performed in DMEM medium diluted 1:10 with 20 mm Hepes NaOH, 100 mm NaCl, ph 7.4, and in the absence of fetal calf serum. 11
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