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Abmart Inc atp7a
Immunohistochemical staining of the FDX1, DLST, <t>ATP7A,</t> ATP7B, Cleaved-Caspase1and IL-18 protein expression in brain tissues after tMCAO (n = 4). ( A ) The protein expression of each component in the figure exhibited positive results in the 24h-tMCAO model, and subsequently demonstrated a weakened intensity following DSF treatment, which was consistent with the findings from the Western blot experiment. Statistical results of each group ( B ). *P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001; and ns not significant. Scale bar = 50 μm.
Atp7a, supplied by Abmart Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Disulfiram downregulates ferredoxin 1 to maintain copper homeostasis and inhibit inflammation in cerebral ischemia/reperfusion injury"

Article Title: Disulfiram downregulates ferredoxin 1 to maintain copper homeostasis and inhibit inflammation in cerebral ischemia/reperfusion injury

Journal: Scientific Reports

doi: 10.1038/s41598-024-64981-x

Immunohistochemical staining of the FDX1, DLST, ATP7A, ATP7B, Cleaved-Caspase1and IL-18 protein expression in brain tissues after tMCAO (n = 4). ( A ) The protein expression of each component in the figure exhibited positive results in the 24h-tMCAO model, and subsequently demonstrated a weakened intensity following DSF treatment, which was consistent with the findings from the Western blot experiment. Statistical results of each group ( B ). *P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001; and ns not significant. Scale bar = 50 μm.
Figure Legend Snippet: Immunohistochemical staining of the FDX1, DLST, ATP7A, ATP7B, Cleaved-Caspase1and IL-18 protein expression in brain tissues after tMCAO (n = 4). ( A ) The protein expression of each component in the figure exhibited positive results in the 24h-tMCAO model, and subsequently demonstrated a weakened intensity following DSF treatment, which was consistent with the findings from the Western blot experiment. Statistical results of each group ( B ). *P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001; and ns not significant. Scale bar = 50 μm.

Techniques Used: Immunohistochemical staining, Staining, Expressing, Western Blot


Structured Review

Abmart Inc atp7a
Atp7a, supplied by Abmart Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti atp7a  (Danaher Inc)


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    Danaher Inc anti atp7a
    Anti Atp7a, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology atp7a antibody d 9 alexa fluor 488
    Atp7a Antibody D 9 Alexa Fluor 488, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology atp7a antibody d 9 alexa fluor 488
    Atp7a Antibody D 9 Alexa Fluor 488, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    State Key Laboratories aldh2 aldehyde dehydrogenase 2 atp7a atpase copper
    Aldh2 Aldehyde Dehydrogenase 2 Atp7a Atpase Copper, supplied by State Key Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    atp7a  (Danaher Inc)


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    Danaher Inc atp7a
    A Inductively coupled plasma‒mass spectrometry (ICP‒MS) revealed an increase in the content of myocardial copper ions in mice with sleep fragmentation (SF) and myocardial ischemia‒reperfusion injury (MI/RI) ( n = 5, 5, 6, 6 for Control, SF, I/R, SF + I/R) Control vs. SF: P = 0.0077, the rest all P < 0.0001. I/R, ischemia‒reperfusion. B Schematic diagram of copper transport in cardiomyocytes. C , D RT‒qPCR analyses of the mRNA levels of Slc31a1 and <t>Atp7a</t> ( n = 5 mice per group, P = 0.0485 for C , P = 0.0550 for D) . E Validation of the expression levels of ATP7A in the myocardium by Western blotting. F Statistical analysis of ATP7A expression, which was normalized to tubulin ( n = 5 mice per group, P = 0.0372). G Representative images of immunofluorescence staining of the myocardium by confocal microscopy (red, WGA; green, ATP7A; blue, DAPI) captured from the anterolateral wall of the mid-lower segment of the left ventricle. The red arrow indicates ATP7A located around the cell nucleus, while the white arrow indicates ATP7A free in the cytoplasm. Scale bar, 20 µm. H – J Cardiac electrophysiology telemetry revealed that SF mice show faster resting heart rate (HR) and lower high frequency power spectral density (HF) ( n = 7 mice per group, P = < 0.0001 for I , P = 0.0030 for J) . K Representative images of sympathetic nerve terminals in mouse myocardial tissue slices were obtained by immunofluorescence staining of tyrosine hydroxylase (left: global image of the heart; middle: local image of the heart; right: 3D reconstruction of sympathetic nerves in thick slices of the heart). L , M The domination of myocardial sympathetic nerves was quantified by the percentage of TH-expressing area and the mean fluorescence intensity ( n = 10 mice per group, P = 0.0001 for L , P < 0.0001 for M) . N , O ELISA was performed to detect norepinephrine (NE) and epinephrine (EPI) in the cardiac tissue homogenate ( n = 8 mice per group, P = 0.0006 for N , P = 0.1908 for O) . Data are presented as the mean ± s.e.m. The significance of differences was evaluated using an unpaired two-tailed t test. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
    Atp7a, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Sleep fragmentation exacerbates myocardial ischemia‒reperfusion injury by promoting copper overload in cardiomyocytes"

    Article Title: Sleep fragmentation exacerbates myocardial ischemia‒reperfusion injury by promoting copper overload in cardiomyocytes

    Journal: Nature Communications

    doi: 10.1038/s41467-024-48227-y

    A Inductively coupled plasma‒mass spectrometry (ICP‒MS) revealed an increase in the content of myocardial copper ions in mice with sleep fragmentation (SF) and myocardial ischemia‒reperfusion injury (MI/RI) ( n = 5, 5, 6, 6 for Control, SF, I/R, SF + I/R) Control vs. SF: P = 0.0077, the rest all P < 0.0001. I/R, ischemia‒reperfusion. B Schematic diagram of copper transport in cardiomyocytes. C , D RT‒qPCR analyses of the mRNA levels of Slc31a1 and Atp7a ( n = 5 mice per group, P = 0.0485 for C , P = 0.0550 for D) . E Validation of the expression levels of ATP7A in the myocardium by Western blotting. F Statistical analysis of ATP7A expression, which was normalized to tubulin ( n = 5 mice per group, P = 0.0372). G Representative images of immunofluorescence staining of the myocardium by confocal microscopy (red, WGA; green, ATP7A; blue, DAPI) captured from the anterolateral wall of the mid-lower segment of the left ventricle. The red arrow indicates ATP7A located around the cell nucleus, while the white arrow indicates ATP7A free in the cytoplasm. Scale bar, 20 µm. H – J Cardiac electrophysiology telemetry revealed that SF mice show faster resting heart rate (HR) and lower high frequency power spectral density (HF) ( n = 7 mice per group, P = < 0.0001 for I , P = 0.0030 for J) . K Representative images of sympathetic nerve terminals in mouse myocardial tissue slices were obtained by immunofluorescence staining of tyrosine hydroxylase (left: global image of the heart; middle: local image of the heart; right: 3D reconstruction of sympathetic nerves in thick slices of the heart). L , M The domination of myocardial sympathetic nerves was quantified by the percentage of TH-expressing area and the mean fluorescence intensity ( n = 10 mice per group, P = 0.0001 for L , P < 0.0001 for M) . N , O ELISA was performed to detect norepinephrine (NE) and epinephrine (EPI) in the cardiac tissue homogenate ( n = 8 mice per group, P = 0.0006 for N , P = 0.1908 for O) . Data are presented as the mean ± s.e.m. The significance of differences was evaluated using an unpaired two-tailed t test. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
    Figure Legend Snippet: A Inductively coupled plasma‒mass spectrometry (ICP‒MS) revealed an increase in the content of myocardial copper ions in mice with sleep fragmentation (SF) and myocardial ischemia‒reperfusion injury (MI/RI) ( n = 5, 5, 6, 6 for Control, SF, I/R, SF + I/R) Control vs. SF: P = 0.0077, the rest all P < 0.0001. I/R, ischemia‒reperfusion. B Schematic diagram of copper transport in cardiomyocytes. C , D RT‒qPCR analyses of the mRNA levels of Slc31a1 and Atp7a ( n = 5 mice per group, P = 0.0485 for C , P = 0.0550 for D) . E Validation of the expression levels of ATP7A in the myocardium by Western blotting. F Statistical analysis of ATP7A expression, which was normalized to tubulin ( n = 5 mice per group, P = 0.0372). G Representative images of immunofluorescence staining of the myocardium by confocal microscopy (red, WGA; green, ATP7A; blue, DAPI) captured from the anterolateral wall of the mid-lower segment of the left ventricle. The red arrow indicates ATP7A located around the cell nucleus, while the white arrow indicates ATP7A free in the cytoplasm. Scale bar, 20 µm. H – J Cardiac electrophysiology telemetry revealed that SF mice show faster resting heart rate (HR) and lower high frequency power spectral density (HF) ( n = 7 mice per group, P = < 0.0001 for I , P = 0.0030 for J) . K Representative images of sympathetic nerve terminals in mouse myocardial tissue slices were obtained by immunofluorescence staining of tyrosine hydroxylase (left: global image of the heart; middle: local image of the heart; right: 3D reconstruction of sympathetic nerves in thick slices of the heart). L , M The domination of myocardial sympathetic nerves was quantified by the percentage of TH-expressing area and the mean fluorescence intensity ( n = 10 mice per group, P = 0.0001 for L , P < 0.0001 for M) . N , O ELISA was performed to detect norepinephrine (NE) and epinephrine (EPI) in the cardiac tissue homogenate ( n = 8 mice per group, P = 0.0006 for N , P = 0.1908 for O) . Data are presented as the mean ± s.e.m. The significance of differences was evaluated using an unpaired two-tailed t test. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.

    Techniques Used: Expressing, Western Blot, Immunofluorescence, Staining, Confocal Microscopy, Fluorescence, Enzyme-linked Immunosorbent Assay, Two Tailed Test

    A Schematic diagram of the experimental groups in the cell model. HL-1 cells were treated with 10 µM CuCl 2 in the presence of solvent (DMSO), 1 µM NE or 10 µM NE for 24 h. B Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence imaging by confocal microscopy (red: Coppersensor1 (CS1; indicates intracellular copper ions), green: ATP7A, blue: DAPI). Scale bar = 20 μm. C CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments, Cu vs. Cu+NE Low : P = 0.0124, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0014). D Representative images of DLAT oligomer immunofluorescence imaging by confocal microscopy. Scale bar = 20 μm. E DLAT oligomer levels were quantified by calculating the mean fluorescence intensity ( n = 10 cells examined over 5 independent experiments, Cu vs. Cu+NE Low : P = 0.5537, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001). F Validation of the levels of DLAT oligomers, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating HL-1 cells with 10 µM CuCl 2 in the presence of NE (1 µM, 10 µM) or DMSO for 24 h. G – K Statistical analysis of DLAT oligomers (Cu vs. Cu+NE Low : P = 0.0217, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0066), DLAT monomer (Cu vs. Cu+NE Low : P = 0.0198, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0129), Lip-DLST (Cu vs. Cu+NE Low : P = 0.0447, Cu vs. Cu+NE High : P = 0.0003, Cu+NE Low vs. Cu+NE High : P = 0.0536), FDX1 (Cu vs. Cu+NE Low : P = 0.0022, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001) and HSP70 (Cu vs. Cu+NE Low : P = 0.0018, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0005). The data on these proteins were normalized to GAPDH ( n = 6 independent experiments). L HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 8 independent experiments, Cu vs. Cu+1uM NE: P = 0.0007, Cu vs. Cu+5uM NE: P = 0.0029, Cu vs. Cu+10uM NE: P < 0.0001, Cu vs. Cu+50uM NE: P < 0.0001). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
    Figure Legend Snippet: A Schematic diagram of the experimental groups in the cell model. HL-1 cells were treated with 10 µM CuCl 2 in the presence of solvent (DMSO), 1 µM NE or 10 µM NE for 24 h. B Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence imaging by confocal microscopy (red: Coppersensor1 (CS1; indicates intracellular copper ions), green: ATP7A, blue: DAPI). Scale bar = 20 μm. C CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments, Cu vs. Cu+NE Low : P = 0.0124, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0014). D Representative images of DLAT oligomer immunofluorescence imaging by confocal microscopy. Scale bar = 20 μm. E DLAT oligomer levels were quantified by calculating the mean fluorescence intensity ( n = 10 cells examined over 5 independent experiments, Cu vs. Cu+NE Low : P = 0.5537, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001). F Validation of the levels of DLAT oligomers, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating HL-1 cells with 10 µM CuCl 2 in the presence of NE (1 µM, 10 µM) or DMSO for 24 h. G – K Statistical analysis of DLAT oligomers (Cu vs. Cu+NE Low : P = 0.0217, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0066), DLAT monomer (Cu vs. Cu+NE Low : P = 0.0198, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0129), Lip-DLST (Cu vs. Cu+NE Low : P = 0.0447, Cu vs. Cu+NE High : P = 0.0003, Cu+NE Low vs. Cu+NE High : P = 0.0536), FDX1 (Cu vs. Cu+NE Low : P = 0.0022, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001) and HSP70 (Cu vs. Cu+NE Low : P = 0.0018, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0005). The data on these proteins were normalized to GAPDH ( n = 6 independent experiments). L HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 8 independent experiments, Cu vs. Cu+1uM NE: P = 0.0007, Cu vs. Cu+5uM NE: P = 0.0029, Cu vs. Cu+10uM NE: P < 0.0001, Cu vs. Cu+50uM NE: P < 0.0001). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.

    Techniques Used: Solvent, Immunofluorescence, Imaging, Confocal Microscopy, Staining, Fluorescence, Western Blot, CCK-8 Assay

    A Validation of the expression levels of VPS35. Statistical analysis of VPS35 expression ( n = 3, independent experiments for B ; n = 5 mice for C) . D Validation of the overexpression of VPS35 and Flag in HL-1 cells 96 h after transfection with the lentivirus. E Statistical analysis of VPS35 overexpression (OE) ( n = 3 independent experiments, P = 0.0091). F Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence images by confocal microscopy (red: CS1, green: ATP7A, blue: DAPI). G CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments). H Validation of the levels of DLAT oligomerization, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating vector- and VPS35-overexpressing HL-1 cells with 10 µM CuCl 2 and 10 µM NE for 24 h. I – N Statistical analysis of the levels of DLAT oligomers, DLAT monomer, Lip-DLAT, Lip-DLST, FDX1 and HSP70. The data on Lip-DLAT and Lip-DLST were normalized to tubulin, and the other data were normalized to GAPDH ( n = 4 independent experiments). O Vector- and VPS35-overexpressing HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 6 independent experiments). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA for B , G and I – N , unpaired two-tailed t-test for C and E , and two-way ANOVA for O . Source data are provided as a Source Data file.
    Figure Legend Snippet: A Validation of the expression levels of VPS35. Statistical analysis of VPS35 expression ( n = 3, independent experiments for B ; n = 5 mice for C) . D Validation of the overexpression of VPS35 and Flag in HL-1 cells 96 h after transfection with the lentivirus. E Statistical analysis of VPS35 overexpression (OE) ( n = 3 independent experiments, P = 0.0091). F Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence images by confocal microscopy (red: CS1, green: ATP7A, blue: DAPI). G CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments). H Validation of the levels of DLAT oligomerization, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating vector- and VPS35-overexpressing HL-1 cells with 10 µM CuCl 2 and 10 µM NE for 24 h. I – N Statistical analysis of the levels of DLAT oligomers, DLAT monomer, Lip-DLAT, Lip-DLST, FDX1 and HSP70. The data on Lip-DLAT and Lip-DLST were normalized to tubulin, and the other data were normalized to GAPDH ( n = 4 independent experiments). O Vector- and VPS35-overexpressing HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 6 independent experiments). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA for B , G and I – N , unpaired two-tailed t-test for C and E , and two-way ANOVA for O . Source data are provided as a Source Data file.

    Techniques Used: Expressing, Over Expression, Transfection, Immunofluorescence, Confocal Microscopy, Staining, Fluorescence, Western Blot, Plasmid Preparation, CCK-8 Assay, Two Tailed Test


    Structured Review

    Carl Zeiss atp7a
    A Inductively coupled plasma‒mass spectrometry (ICP‒MS) revealed an increase in the content of myocardial copper ions in mice with sleep fragmentation (SF) and myocardial ischemia‒reperfusion injury (MI/RI) ( n = 5, 5, 6, 6 for Control, SF, I/R, SF + I/R) Control vs. SF: P = 0.0077, the rest all P < 0.0001. I/R, ischemia‒reperfusion. B Schematic diagram of copper transport in cardiomyocytes. C , D RT‒qPCR analyses of the mRNA levels of Slc31a1 and <t>Atp7a</t> ( n = 5 mice per group, P = 0.0485 for C , P = 0.0550 for D) . E Validation of the expression levels of ATP7A in the myocardium by Western blotting. F Statistical analysis of ATP7A expression, which was normalized to tubulin ( n = 5 mice per group, P = 0.0372). G Representative images of immunofluorescence staining of the myocardium by confocal microscopy (red, WGA; green, ATP7A; blue, DAPI) captured from the anterolateral wall of the mid-lower segment of the left ventricle. The red arrow indicates ATP7A located around the cell nucleus, while the white arrow indicates ATP7A free in the cytoplasm. Scale bar, 20 µm. H – J Cardiac electrophysiology telemetry revealed that SF mice show faster resting heart rate (HR) and lower high frequency power spectral density (HF) ( n = 7 mice per group, P = < 0.0001 for I , P = 0.0030 for J) . K Representative images of sympathetic nerve terminals in mouse myocardial tissue slices were obtained by immunofluorescence staining of tyrosine hydroxylase (left: global image of the heart; middle: local image of the heart; right: 3D reconstruction of sympathetic nerves in thick slices of the heart). L , M The domination of myocardial sympathetic nerves was quantified by the percentage of TH-expressing area and the mean fluorescence intensity ( n = 10 mice per group, P = 0.0001 for L , P < 0.0001 for M) . N , O ELISA was performed to detect norepinephrine (NE) and epinephrine (EPI) in the cardiac tissue homogenate ( n = 8 mice per group, P = 0.0006 for N , P = 0.1908 for O) . Data are presented as the mean ± s.e.m. The significance of differences was evaluated using an unpaired two-tailed t test. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
    Atp7a, supplied by Carl Zeiss, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/atp7a/product/Carl Zeiss
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    atp7a - by Bioz Stars, 2024-07
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    Images

    1) Product Images from "Sleep fragmentation exacerbates myocardial ischemia‒reperfusion injury by promoting copper overload in cardiomyocytes"

    Article Title: Sleep fragmentation exacerbates myocardial ischemia‒reperfusion injury by promoting copper overload in cardiomyocytes

    Journal: Nature Communications

    doi: 10.1038/s41467-024-48227-y

    A Inductively coupled plasma‒mass spectrometry (ICP‒MS) revealed an increase in the content of myocardial copper ions in mice with sleep fragmentation (SF) and myocardial ischemia‒reperfusion injury (MI/RI) ( n = 5, 5, 6, 6 for Control, SF, I/R, SF + I/R) Control vs. SF: P = 0.0077, the rest all P < 0.0001. I/R, ischemia‒reperfusion. B Schematic diagram of copper transport in cardiomyocytes. C , D RT‒qPCR analyses of the mRNA levels of Slc31a1 and Atp7a ( n = 5 mice per group, P = 0.0485 for C , P = 0.0550 for D) . E Validation of the expression levels of ATP7A in the myocardium by Western blotting. F Statistical analysis of ATP7A expression, which was normalized to tubulin ( n = 5 mice per group, P = 0.0372). G Representative images of immunofluorescence staining of the myocardium by confocal microscopy (red, WGA; green, ATP7A; blue, DAPI) captured from the anterolateral wall of the mid-lower segment of the left ventricle. The red arrow indicates ATP7A located around the cell nucleus, while the white arrow indicates ATP7A free in the cytoplasm. Scale bar, 20 µm. H – J Cardiac electrophysiology telemetry revealed that SF mice show faster resting heart rate (HR) and lower high frequency power spectral density (HF) ( n = 7 mice per group, P = < 0.0001 for I , P = 0.0030 for J) . K Representative images of sympathetic nerve terminals in mouse myocardial tissue slices were obtained by immunofluorescence staining of tyrosine hydroxylase (left: global image of the heart; middle: local image of the heart; right: 3D reconstruction of sympathetic nerves in thick slices of the heart). L , M The domination of myocardial sympathetic nerves was quantified by the percentage of TH-expressing area and the mean fluorescence intensity ( n = 10 mice per group, P = 0.0001 for L , P < 0.0001 for M) . N , O ELISA was performed to detect norepinephrine (NE) and epinephrine (EPI) in the cardiac tissue homogenate ( n = 8 mice per group, P = 0.0006 for N , P = 0.1908 for O) . Data are presented as the mean ± s.e.m. The significance of differences was evaluated using an unpaired two-tailed t test. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
    Figure Legend Snippet: A Inductively coupled plasma‒mass spectrometry (ICP‒MS) revealed an increase in the content of myocardial copper ions in mice with sleep fragmentation (SF) and myocardial ischemia‒reperfusion injury (MI/RI) ( n = 5, 5, 6, 6 for Control, SF, I/R, SF + I/R) Control vs. SF: P = 0.0077, the rest all P < 0.0001. I/R, ischemia‒reperfusion. B Schematic diagram of copper transport in cardiomyocytes. C , D RT‒qPCR analyses of the mRNA levels of Slc31a1 and Atp7a ( n = 5 mice per group, P = 0.0485 for C , P = 0.0550 for D) . E Validation of the expression levels of ATP7A in the myocardium by Western blotting. F Statistical analysis of ATP7A expression, which was normalized to tubulin ( n = 5 mice per group, P = 0.0372). G Representative images of immunofluorescence staining of the myocardium by confocal microscopy (red, WGA; green, ATP7A; blue, DAPI) captured from the anterolateral wall of the mid-lower segment of the left ventricle. The red arrow indicates ATP7A located around the cell nucleus, while the white arrow indicates ATP7A free in the cytoplasm. Scale bar, 20 µm. H – J Cardiac electrophysiology telemetry revealed that SF mice show faster resting heart rate (HR) and lower high frequency power spectral density (HF) ( n = 7 mice per group, P = < 0.0001 for I , P = 0.0030 for J) . K Representative images of sympathetic nerve terminals in mouse myocardial tissue slices were obtained by immunofluorescence staining of tyrosine hydroxylase (left: global image of the heart; middle: local image of the heart; right: 3D reconstruction of sympathetic nerves in thick slices of the heart). L , M The domination of myocardial sympathetic nerves was quantified by the percentage of TH-expressing area and the mean fluorescence intensity ( n = 10 mice per group, P = 0.0001 for L , P < 0.0001 for M) . N , O ELISA was performed to detect norepinephrine (NE) and epinephrine (EPI) in the cardiac tissue homogenate ( n = 8 mice per group, P = 0.0006 for N , P = 0.1908 for O) . Data are presented as the mean ± s.e.m. The significance of differences was evaluated using an unpaired two-tailed t test. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.

    Techniques Used: Expressing, Western Blot, Immunofluorescence, Staining, Confocal Microscopy, Fluorescence, Enzyme-linked Immunosorbent Assay, Two Tailed Test

    A Schematic diagram of the experimental groups in the cell model. HL-1 cells were treated with 10 µM CuCl 2 in the presence of solvent (DMSO), 1 µM NE or 10 µM NE for 24 h. B Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence imaging by confocal microscopy (red: Coppersensor1 (CS1; indicates intracellular copper ions), green: ATP7A, blue: DAPI). Scale bar = 20 μm. C CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments, Cu vs. Cu+NE Low : P = 0.0124, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0014). D Representative images of DLAT oligomer immunofluorescence imaging by confocal microscopy. Scale bar = 20 μm. E DLAT oligomer levels were quantified by calculating the mean fluorescence intensity ( n = 10 cells examined over 5 independent experiments, Cu vs. Cu+NE Low : P = 0.5537, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001). F Validation of the levels of DLAT oligomers, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating HL-1 cells with 10 µM CuCl 2 in the presence of NE (1 µM, 10 µM) or DMSO for 24 h. G – K Statistical analysis of DLAT oligomers (Cu vs. Cu+NE Low : P = 0.0217, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0066), DLAT monomer (Cu vs. Cu+NE Low : P = 0.0198, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0129), Lip-DLST (Cu vs. Cu+NE Low : P = 0.0447, Cu vs. Cu+NE High : P = 0.0003, Cu+NE Low vs. Cu+NE High : P = 0.0536), FDX1 (Cu vs. Cu+NE Low : P = 0.0022, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001) and HSP70 (Cu vs. Cu+NE Low : P = 0.0018, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0005). The data on these proteins were normalized to GAPDH ( n = 6 independent experiments). L HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 8 independent experiments, Cu vs. Cu+1uM NE: P = 0.0007, Cu vs. Cu+5uM NE: P = 0.0029, Cu vs. Cu+10uM NE: P < 0.0001, Cu vs. Cu+50uM NE: P < 0.0001). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
    Figure Legend Snippet: A Schematic diagram of the experimental groups in the cell model. HL-1 cells were treated with 10 µM CuCl 2 in the presence of solvent (DMSO), 1 µM NE or 10 µM NE for 24 h. B Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence imaging by confocal microscopy (red: Coppersensor1 (CS1; indicates intracellular copper ions), green: ATP7A, blue: DAPI). Scale bar = 20 μm. C CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments, Cu vs. Cu+NE Low : P = 0.0124, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0014). D Representative images of DLAT oligomer immunofluorescence imaging by confocal microscopy. Scale bar = 20 μm. E DLAT oligomer levels were quantified by calculating the mean fluorescence intensity ( n = 10 cells examined over 5 independent experiments, Cu vs. Cu+NE Low : P = 0.5537, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001). F Validation of the levels of DLAT oligomers, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating HL-1 cells with 10 µM CuCl 2 in the presence of NE (1 µM, 10 µM) or DMSO for 24 h. G – K Statistical analysis of DLAT oligomers (Cu vs. Cu+NE Low : P = 0.0217, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0066), DLAT monomer (Cu vs. Cu+NE Low : P = 0.0198, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0129), Lip-DLST (Cu vs. Cu+NE Low : P = 0.0447, Cu vs. Cu+NE High : P = 0.0003, Cu+NE Low vs. Cu+NE High : P = 0.0536), FDX1 (Cu vs. Cu+NE Low : P = 0.0022, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001) and HSP70 (Cu vs. Cu+NE Low : P = 0.0018, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0005). The data on these proteins were normalized to GAPDH ( n = 6 independent experiments). L HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 8 independent experiments, Cu vs. Cu+1uM NE: P = 0.0007, Cu vs. Cu+5uM NE: P = 0.0029, Cu vs. Cu+10uM NE: P < 0.0001, Cu vs. Cu+50uM NE: P < 0.0001). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.

    Techniques Used: Solvent, Immunofluorescence, Imaging, Confocal Microscopy, Staining, Fluorescence, Western Blot, CCK-8 Assay

    A Validation of the expression levels of VPS35. Statistical analysis of VPS35 expression ( n = 3, independent experiments for B ; n = 5 mice for C) . D Validation of the overexpression of VPS35 and Flag in HL-1 cells 96 h after transfection with the lentivirus. E Statistical analysis of VPS35 overexpression (OE) ( n = 3 independent experiments, P = 0.0091). F Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence images by confocal microscopy (red: CS1, green: ATP7A, blue: DAPI). G CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments). H Validation of the levels of DLAT oligomerization, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating vector- and VPS35-overexpressing HL-1 cells with 10 µM CuCl 2 and 10 µM NE for 24 h. I – N Statistical analysis of the levels of DLAT oligomers, DLAT monomer, Lip-DLAT, Lip-DLST, FDX1 and HSP70. The data on Lip-DLAT and Lip-DLST were normalized to tubulin, and the other data were normalized to GAPDH ( n = 4 independent experiments). O Vector- and VPS35-overexpressing HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 6 independent experiments). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA for B , G and I – N , unpaired two-tailed t-test for C and E , and two-way ANOVA for O . Source data are provided as a Source Data file.
    Figure Legend Snippet: A Validation of the expression levels of VPS35. Statistical analysis of VPS35 expression ( n = 3, independent experiments for B ; n = 5 mice for C) . D Validation of the overexpression of VPS35 and Flag in HL-1 cells 96 h after transfection with the lentivirus. E Statistical analysis of VPS35 overexpression (OE) ( n = 3 independent experiments, P = 0.0091). F Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence images by confocal microscopy (red: CS1, green: ATP7A, blue: DAPI). G CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments). H Validation of the levels of DLAT oligomerization, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating vector- and VPS35-overexpressing HL-1 cells with 10 µM CuCl 2 and 10 µM NE for 24 h. I – N Statistical analysis of the levels of DLAT oligomers, DLAT monomer, Lip-DLAT, Lip-DLST, FDX1 and HSP70. The data on Lip-DLAT and Lip-DLST were normalized to tubulin, and the other data were normalized to GAPDH ( n = 4 independent experiments). O Vector- and VPS35-overexpressing HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 6 independent experiments). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA for B , G and I – N , unpaired two-tailed t-test for C and E , and two-way ANOVA for O . Source data are provided as a Source Data file.

    Techniques Used: Expressing, Over Expression, Transfection, Immunofluorescence, Confocal Microscopy, Staining, Fluorescence, Western Blot, Plasmid Preparation, CCK-8 Assay, Two Tailed Test


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    MyBiosource Biotechnology atp7a
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    ABclonal Biotechnology c reative c om m ons l icense atp7a
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    Abmart Inc atp7a
    Immunohistochemical staining of the FDX1, DLST, <t>ATP7A,</t> ATP7B, Cleaved-Caspase1and IL-18 protein expression in brain tissues after tMCAO (n = 4). ( A ) The protein expression of each component in the figure exhibited positive results in the 24h-tMCAO model, and subsequently demonstrated a weakened intensity following DSF treatment, which was consistent with the findings from the Western blot experiment. Statistical results of each group ( B ). *P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001; and ns not significant. Scale bar = 50 μm.
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    Danaher Inc anti atp7a
    Immunohistochemical staining of the FDX1, DLST, <t>ATP7A,</t> ATP7B, Cleaved-Caspase1and IL-18 protein expression in brain tissues after tMCAO (n = 4). ( A ) The protein expression of each component in the figure exhibited positive results in the 24h-tMCAO model, and subsequently demonstrated a weakened intensity following DSF treatment, which was consistent with the findings from the Western blot experiment. Statistical results of each group ( B ). *P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001; and ns not significant. Scale bar = 50 μm.
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    Santa Cruz Biotechnology atp7a antibody d 9 alexa fluor 488
    Immunohistochemical staining of the FDX1, DLST, <t>ATP7A,</t> ATP7B, Cleaved-Caspase1and IL-18 protein expression in brain tissues after tMCAO (n = 4). ( A ) The protein expression of each component in the figure exhibited positive results in the 24h-tMCAO model, and subsequently demonstrated a weakened intensity following DSF treatment, which was consistent with the findings from the Western blot experiment. Statistical results of each group ( B ). *P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001; and ns not significant. Scale bar = 50 μm.
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    State Key Laboratories aldh2 aldehyde dehydrogenase 2 atp7a atpase copper
    Immunohistochemical staining of the FDX1, DLST, <t>ATP7A,</t> ATP7B, Cleaved-Caspase1and IL-18 protein expression in brain tissues after tMCAO (n = 4). ( A ) The protein expression of each component in the figure exhibited positive results in the 24h-tMCAO model, and subsequently demonstrated a weakened intensity following DSF treatment, which was consistent with the findings from the Western blot experiment. Statistical results of each group ( B ). *P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001; and ns not significant. Scale bar = 50 μm.
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    Danaher Inc atp7a
    A Inductively coupled plasma‒mass spectrometry (ICP‒MS) revealed an increase in the content of myocardial copper ions in mice with sleep fragmentation (SF) and myocardial ischemia‒reperfusion injury (MI/RI) ( n = 5, 5, 6, 6 for Control, SF, I/R, SF + I/R) Control vs. SF: P = 0.0077, the rest all P < 0.0001. I/R, ischemia‒reperfusion. B Schematic diagram of copper transport in cardiomyocytes. C , D RT‒qPCR analyses of the mRNA levels of Slc31a1 and <t>Atp7a</t> ( n = 5 mice per group, P = 0.0485 for C , P = 0.0550 for D) . E Validation of the expression levels of ATP7A in the myocardium by Western blotting. F Statistical analysis of ATP7A expression, which was normalized to tubulin ( n = 5 mice per group, P = 0.0372). G Representative images of immunofluorescence staining of the myocardium by confocal microscopy (red, WGA; green, ATP7A; blue, DAPI) captured from the anterolateral wall of the mid-lower segment of the left ventricle. The red arrow indicates ATP7A located around the cell nucleus, while the white arrow indicates ATP7A free in the cytoplasm. Scale bar, 20 µm. H – J Cardiac electrophysiology telemetry revealed that SF mice show faster resting heart rate (HR) and lower high frequency power spectral density (HF) ( n = 7 mice per group, P = < 0.0001 for I , P = 0.0030 for J) . K Representative images of sympathetic nerve terminals in mouse myocardial tissue slices were obtained by immunofluorescence staining of tyrosine hydroxylase (left: global image of the heart; middle: local image of the heart; right: 3D reconstruction of sympathetic nerves in thick slices of the heart). L , M The domination of myocardial sympathetic nerves was quantified by the percentage of TH-expressing area and the mean fluorescence intensity ( n = 10 mice per group, P = 0.0001 for L , P < 0.0001 for M) . N , O ELISA was performed to detect norepinephrine (NE) and epinephrine (EPI) in the cardiac tissue homogenate ( n = 8 mice per group, P = 0.0006 for N , P = 0.1908 for O) . Data are presented as the mean ± s.e.m. The significance of differences was evaluated using an unpaired two-tailed t test. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
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    Carl Zeiss atp7a
    A Inductively coupled plasma‒mass spectrometry (ICP‒MS) revealed an increase in the content of myocardial copper ions in mice with sleep fragmentation (SF) and myocardial ischemia‒reperfusion injury (MI/RI) ( n = 5, 5, 6, 6 for Control, SF, I/R, SF + I/R) Control vs. SF: P = 0.0077, the rest all P < 0.0001. I/R, ischemia‒reperfusion. B Schematic diagram of copper transport in cardiomyocytes. C , D RT‒qPCR analyses of the mRNA levels of Slc31a1 and <t>Atp7a</t> ( n = 5 mice per group, P = 0.0485 for C , P = 0.0550 for D) . E Validation of the expression levels of ATP7A in the myocardium by Western blotting. F Statistical analysis of ATP7A expression, which was normalized to tubulin ( n = 5 mice per group, P = 0.0372). G Representative images of immunofluorescence staining of the myocardium by confocal microscopy (red, WGA; green, ATP7A; blue, DAPI) captured from the anterolateral wall of the mid-lower segment of the left ventricle. The red arrow indicates ATP7A located around the cell nucleus, while the white arrow indicates ATP7A free in the cytoplasm. Scale bar, 20 µm. H – J Cardiac electrophysiology telemetry revealed that SF mice show faster resting heart rate (HR) and lower high frequency power spectral density (HF) ( n = 7 mice per group, P = < 0.0001 for I , P = 0.0030 for J) . K Representative images of sympathetic nerve terminals in mouse myocardial tissue slices were obtained by immunofluorescence staining of tyrosine hydroxylase (left: global image of the heart; middle: local image of the heart; right: 3D reconstruction of sympathetic nerves in thick slices of the heart). L , M The domination of myocardial sympathetic nerves was quantified by the percentage of TH-expressing area and the mean fluorescence intensity ( n = 10 mice per group, P = 0.0001 for L , P < 0.0001 for M) . N , O ELISA was performed to detect norepinephrine (NE) and epinephrine (EPI) in the cardiac tissue homogenate ( n = 8 mice per group, P = 0.0006 for N , P = 0.1908 for O) . Data are presented as the mean ± s.e.m. The significance of differences was evaluated using an unpaired two-tailed t test. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
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    MyBiosource Biotechnology atp7a
    A Inductively coupled plasma‒mass spectrometry (ICP‒MS) revealed an increase in the content of myocardial copper ions in mice with sleep fragmentation (SF) and myocardial ischemia‒reperfusion injury (MI/RI) ( n = 5, 5, 6, 6 for Control, SF, I/R, SF + I/R) Control vs. SF: P = 0.0077, the rest all P < 0.0001. I/R, ischemia‒reperfusion. B Schematic diagram of copper transport in cardiomyocytes. C , D RT‒qPCR analyses of the mRNA levels of Slc31a1 and <t>Atp7a</t> ( n = 5 mice per group, P = 0.0485 for C , P = 0.0550 for D) . E Validation of the expression levels of ATP7A in the myocardium by Western blotting. F Statistical analysis of ATP7A expression, which was normalized to tubulin ( n = 5 mice per group, P = 0.0372). G Representative images of immunofluorescence staining of the myocardium by confocal microscopy (red, WGA; green, ATP7A; blue, DAPI) captured from the anterolateral wall of the mid-lower segment of the left ventricle. The red arrow indicates ATP7A located around the cell nucleus, while the white arrow indicates ATP7A free in the cytoplasm. Scale bar, 20 µm. H – J Cardiac electrophysiology telemetry revealed that SF mice show faster resting heart rate (HR) and lower high frequency power spectral density (HF) ( n = 7 mice per group, P = < 0.0001 for I , P = 0.0030 for J) . K Representative images of sympathetic nerve terminals in mouse myocardial tissue slices were obtained by immunofluorescence staining of tyrosine hydroxylase (left: global image of the heart; middle: local image of the heart; right: 3D reconstruction of sympathetic nerves in thick slices of the heart). L , M The domination of myocardial sympathetic nerves was quantified by the percentage of TH-expressing area and the mean fluorescence intensity ( n = 10 mice per group, P = 0.0001 for L , P < 0.0001 for M) . N , O ELISA was performed to detect norepinephrine (NE) and epinephrine (EPI) in the cardiac tissue homogenate ( n = 8 mice per group, P = 0.0006 for N , P = 0.1908 for O) . Data are presented as the mean ± s.e.m. The significance of differences was evaluated using an unpaired two-tailed t test. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
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    ABclonal Biotechnology c reative c om m ons l icense atp7a
    A Inductively coupled plasma‒mass spectrometry (ICP‒MS) revealed an increase in the content of myocardial copper ions in mice with sleep fragmentation (SF) and myocardial ischemia‒reperfusion injury (MI/RI) ( n = 5, 5, 6, 6 for Control, SF, I/R, SF + I/R) Control vs. SF: P = 0.0077, the rest all P < 0.0001. I/R, ischemia‒reperfusion. B Schematic diagram of copper transport in cardiomyocytes. C , D RT‒qPCR analyses of the mRNA levels of Slc31a1 and <t>Atp7a</t> ( n = 5 mice per group, P = 0.0485 for C , P = 0.0550 for D) . E Validation of the expression levels of ATP7A in the myocardium by Western blotting. F Statistical analysis of ATP7A expression, which was normalized to tubulin ( n = 5 mice per group, P = 0.0372). G Representative images of immunofluorescence staining of the myocardium by confocal microscopy (red, WGA; green, ATP7A; blue, DAPI) captured from the anterolateral wall of the mid-lower segment of the left ventricle. The red arrow indicates ATP7A located around the cell nucleus, while the white arrow indicates ATP7A free in the cytoplasm. Scale bar, 20 µm. H – J Cardiac electrophysiology telemetry revealed that SF mice show faster resting heart rate (HR) and lower high frequency power spectral density (HF) ( n = 7 mice per group, P = < 0.0001 for I , P = 0.0030 for J) . K Representative images of sympathetic nerve terminals in mouse myocardial tissue slices were obtained by immunofluorescence staining of tyrosine hydroxylase (left: global image of the heart; middle: local image of the heart; right: 3D reconstruction of sympathetic nerves in thick slices of the heart). L , M The domination of myocardial sympathetic nerves was quantified by the percentage of TH-expressing area and the mean fluorescence intensity ( n = 10 mice per group, P = 0.0001 for L , P < 0.0001 for M) . N , O ELISA was performed to detect norepinephrine (NE) and epinephrine (EPI) in the cardiac tissue homogenate ( n = 8 mice per group, P = 0.0006 for N , P = 0.1908 for O) . Data are presented as the mean ± s.e.m. The significance of differences was evaluated using an unpaired two-tailed t test. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.
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    Immunohistochemical staining of the FDX1, DLST, ATP7A, ATP7B, Cleaved-Caspase1and IL-18 protein expression in brain tissues after tMCAO (n = 4). ( A ) The protein expression of each component in the figure exhibited positive results in the 24h-tMCAO model, and subsequently demonstrated a weakened intensity following DSF treatment, which was consistent with the findings from the Western blot experiment. Statistical results of each group ( B ). *P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001; and ns not significant. Scale bar = 50 μm.

    Journal: Scientific Reports

    Article Title: Disulfiram downregulates ferredoxin 1 to maintain copper homeostasis and inhibit inflammation in cerebral ischemia/reperfusion injury

    doi: 10.1038/s41598-024-64981-x

    Figure Lengend Snippet: Immunohistochemical staining of the FDX1, DLST, ATP7A, ATP7B, Cleaved-Caspase1and IL-18 protein expression in brain tissues after tMCAO (n = 4). ( A ) The protein expression of each component in the figure exhibited positive results in the 24h-tMCAO model, and subsequently demonstrated a weakened intensity following DSF treatment, which was consistent with the findings from the Western blot experiment. Statistical results of each group ( B ). *P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001; and ns not significant. Scale bar = 50 μm.

    Article Snippet: The sections were then blocked with fetal bovine serum for 1 h. Subsequently, the sections were incubated overnight at 4 ℃ with primary antibodies against FDX1 (T510671,1:200 dilution, Abmart, China), DLST (TD13671,1:200 dilution, Abmart, China), ATP7A (PA7106, 1:200 dilution, Abmart, China), ATP7B (TA0410, 1:200 dilution, Abmart, China), Caspase-1 (22915-1-AP, 1:200 dilution, Proteintech, USA), and IL-18 (10663-1-AP, 1:200 dilution, Proteintech, USA), followed by subsequent incubation with secondary antibodies (Boster, China) for 1 h at room temperature.

    Techniques: Immunohistochemical staining, Staining, Expressing, Western Blot

    A Inductively coupled plasma‒mass spectrometry (ICP‒MS) revealed an increase in the content of myocardial copper ions in mice with sleep fragmentation (SF) and myocardial ischemia‒reperfusion injury (MI/RI) ( n = 5, 5, 6, 6 for Control, SF, I/R, SF + I/R) Control vs. SF: P = 0.0077, the rest all P < 0.0001. I/R, ischemia‒reperfusion. B Schematic diagram of copper transport in cardiomyocytes. C , D RT‒qPCR analyses of the mRNA levels of Slc31a1 and Atp7a ( n = 5 mice per group, P = 0.0485 for C , P = 0.0550 for D) . E Validation of the expression levels of ATP7A in the myocardium by Western blotting. F Statistical analysis of ATP7A expression, which was normalized to tubulin ( n = 5 mice per group, P = 0.0372). G Representative images of immunofluorescence staining of the myocardium by confocal microscopy (red, WGA; green, ATP7A; blue, DAPI) captured from the anterolateral wall of the mid-lower segment of the left ventricle. The red arrow indicates ATP7A located around the cell nucleus, while the white arrow indicates ATP7A free in the cytoplasm. Scale bar, 20 µm. H – J Cardiac electrophysiology telemetry revealed that SF mice show faster resting heart rate (HR) and lower high frequency power spectral density (HF) ( n = 7 mice per group, P = < 0.0001 for I , P = 0.0030 for J) . K Representative images of sympathetic nerve terminals in mouse myocardial tissue slices were obtained by immunofluorescence staining of tyrosine hydroxylase (left: global image of the heart; middle: local image of the heart; right: 3D reconstruction of sympathetic nerves in thick slices of the heart). L , M The domination of myocardial sympathetic nerves was quantified by the percentage of TH-expressing area and the mean fluorescence intensity ( n = 10 mice per group, P = 0.0001 for L , P < 0.0001 for M) . N , O ELISA was performed to detect norepinephrine (NE) and epinephrine (EPI) in the cardiac tissue homogenate ( n = 8 mice per group, P = 0.0006 for N , P = 0.1908 for O) . Data are presented as the mean ± s.e.m. The significance of differences was evaluated using an unpaired two-tailed t test. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Sleep fragmentation exacerbates myocardial ischemia‒reperfusion injury by promoting copper overload in cardiomyocytes

    doi: 10.1038/s41467-024-48227-y

    Figure Lengend Snippet: A Inductively coupled plasma‒mass spectrometry (ICP‒MS) revealed an increase in the content of myocardial copper ions in mice with sleep fragmentation (SF) and myocardial ischemia‒reperfusion injury (MI/RI) ( n = 5, 5, 6, 6 for Control, SF, I/R, SF + I/R) Control vs. SF: P = 0.0077, the rest all P < 0.0001. I/R, ischemia‒reperfusion. B Schematic diagram of copper transport in cardiomyocytes. C , D RT‒qPCR analyses of the mRNA levels of Slc31a1 and Atp7a ( n = 5 mice per group, P = 0.0485 for C , P = 0.0550 for D) . E Validation of the expression levels of ATP7A in the myocardium by Western blotting. F Statistical analysis of ATP7A expression, which was normalized to tubulin ( n = 5 mice per group, P = 0.0372). G Representative images of immunofluorescence staining of the myocardium by confocal microscopy (red, WGA; green, ATP7A; blue, DAPI) captured from the anterolateral wall of the mid-lower segment of the left ventricle. The red arrow indicates ATP7A located around the cell nucleus, while the white arrow indicates ATP7A free in the cytoplasm. Scale bar, 20 µm. H – J Cardiac electrophysiology telemetry revealed that SF mice show faster resting heart rate (HR) and lower high frequency power spectral density (HF) ( n = 7 mice per group, P = < 0.0001 for I , P = 0.0030 for J) . K Representative images of sympathetic nerve terminals in mouse myocardial tissue slices were obtained by immunofluorescence staining of tyrosine hydroxylase (left: global image of the heart; middle: local image of the heart; right: 3D reconstruction of sympathetic nerves in thick slices of the heart). L , M The domination of myocardial sympathetic nerves was quantified by the percentage of TH-expressing area and the mean fluorescence intensity ( n = 10 mice per group, P = 0.0001 for L , P < 0.0001 for M) . N , O ELISA was performed to detect norepinephrine (NE) and epinephrine (EPI) in the cardiac tissue homogenate ( n = 8 mice per group, P = 0.0006 for N , P = 0.1908 for O) . Data are presented as the mean ± s.e.m. The significance of differences was evaluated using an unpaired two-tailed t test. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.

    Article Snippet: Histological sections were air-dried, washed off OCT, blocked with 5% goats’ serum for 60 min in room temperature, then incubated with antibody against DLAT (SANTA, sc-271534), TH (Abcam, ab137869) or ATP7A (SANTA, sc-271534) at 4 °C overnight and incubated with secondary antibody (Alexa Fluor 488 or Fluor 594) for 1 h at room temperature.

    Techniques: Expressing, Western Blot, Immunofluorescence, Staining, Confocal Microscopy, Fluorescence, Enzyme-linked Immunosorbent Assay, Two Tailed Test

    A Schematic diagram of the experimental groups in the cell model. HL-1 cells were treated with 10 µM CuCl 2 in the presence of solvent (DMSO), 1 µM NE or 10 µM NE for 24 h. B Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence imaging by confocal microscopy (red: Coppersensor1 (CS1; indicates intracellular copper ions), green: ATP7A, blue: DAPI). Scale bar = 20 μm. C CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments, Cu vs. Cu+NE Low : P = 0.0124, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0014). D Representative images of DLAT oligomer immunofluorescence imaging by confocal microscopy. Scale bar = 20 μm. E DLAT oligomer levels were quantified by calculating the mean fluorescence intensity ( n = 10 cells examined over 5 independent experiments, Cu vs. Cu+NE Low : P = 0.5537, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001). F Validation of the levels of DLAT oligomers, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating HL-1 cells with 10 µM CuCl 2 in the presence of NE (1 µM, 10 µM) or DMSO for 24 h. G – K Statistical analysis of DLAT oligomers (Cu vs. Cu+NE Low : P = 0.0217, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0066), DLAT monomer (Cu vs. Cu+NE Low : P = 0.0198, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0129), Lip-DLST (Cu vs. Cu+NE Low : P = 0.0447, Cu vs. Cu+NE High : P = 0.0003, Cu+NE Low vs. Cu+NE High : P = 0.0536), FDX1 (Cu vs. Cu+NE Low : P = 0.0022, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001) and HSP70 (Cu vs. Cu+NE Low : P = 0.0018, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0005). The data on these proteins were normalized to GAPDH ( n = 6 independent experiments). L HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 8 independent experiments, Cu vs. Cu+1uM NE: P = 0.0007, Cu vs. Cu+5uM NE: P = 0.0029, Cu vs. Cu+10uM NE: P < 0.0001, Cu vs. Cu+50uM NE: P < 0.0001). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Sleep fragmentation exacerbates myocardial ischemia‒reperfusion injury by promoting copper overload in cardiomyocytes

    doi: 10.1038/s41467-024-48227-y

    Figure Lengend Snippet: A Schematic diagram of the experimental groups in the cell model. HL-1 cells were treated with 10 µM CuCl 2 in the presence of solvent (DMSO), 1 µM NE or 10 µM NE for 24 h. B Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence imaging by confocal microscopy (red: Coppersensor1 (CS1; indicates intracellular copper ions), green: ATP7A, blue: DAPI). Scale bar = 20 μm. C CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments, Cu vs. Cu+NE Low : P = 0.0124, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0014). D Representative images of DLAT oligomer immunofluorescence imaging by confocal microscopy. Scale bar = 20 μm. E DLAT oligomer levels were quantified by calculating the mean fluorescence intensity ( n = 10 cells examined over 5 independent experiments, Cu vs. Cu+NE Low : P = 0.5537, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001). F Validation of the levels of DLAT oligomers, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating HL-1 cells with 10 µM CuCl 2 in the presence of NE (1 µM, 10 µM) or DMSO for 24 h. G – K Statistical analysis of DLAT oligomers (Cu vs. Cu+NE Low : P = 0.0217, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0066), DLAT monomer (Cu vs. Cu+NE Low : P = 0.0198, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0129), Lip-DLST (Cu vs. Cu+NE Low : P = 0.0447, Cu vs. Cu+NE High : P = 0.0003, Cu+NE Low vs. Cu+NE High : P = 0.0536), FDX1 (Cu vs. Cu+NE Low : P = 0.0022, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001) and HSP70 (Cu vs. Cu+NE Low : P = 0.0018, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0005). The data on these proteins were normalized to GAPDH ( n = 6 independent experiments). L HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 8 independent experiments, Cu vs. Cu+1uM NE: P = 0.0007, Cu vs. Cu+5uM NE: P = 0.0029, Cu vs. Cu+10uM NE: P < 0.0001, Cu vs. Cu+50uM NE: P < 0.0001). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.

    Article Snippet: Histological sections were air-dried, washed off OCT, blocked with 5% goats’ serum for 60 min in room temperature, then incubated with antibody against DLAT (SANTA, sc-271534), TH (Abcam, ab137869) or ATP7A (SANTA, sc-271534) at 4 °C overnight and incubated with secondary antibody (Alexa Fluor 488 or Fluor 594) for 1 h at room temperature.

    Techniques: Solvent, Immunofluorescence, Imaging, Confocal Microscopy, Staining, Fluorescence, Western Blot, CCK-8 Assay

    A Validation of the expression levels of VPS35. Statistical analysis of VPS35 expression ( n = 3, independent experiments for B ; n = 5 mice for C) . D Validation of the overexpression of VPS35 and Flag in HL-1 cells 96 h after transfection with the lentivirus. E Statistical analysis of VPS35 overexpression (OE) ( n = 3 independent experiments, P = 0.0091). F Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence images by confocal microscopy (red: CS1, green: ATP7A, blue: DAPI). G CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments). H Validation of the levels of DLAT oligomerization, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating vector- and VPS35-overexpressing HL-1 cells with 10 µM CuCl 2 and 10 µM NE for 24 h. I – N Statistical analysis of the levels of DLAT oligomers, DLAT monomer, Lip-DLAT, Lip-DLST, FDX1 and HSP70. The data on Lip-DLAT and Lip-DLST were normalized to tubulin, and the other data were normalized to GAPDH ( n = 4 independent experiments). O Vector- and VPS35-overexpressing HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 6 independent experiments). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA for B , G and I – N , unpaired two-tailed t-test for C and E , and two-way ANOVA for O . Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Sleep fragmentation exacerbates myocardial ischemia‒reperfusion injury by promoting copper overload in cardiomyocytes

    doi: 10.1038/s41467-024-48227-y

    Figure Lengend Snippet: A Validation of the expression levels of VPS35. Statistical analysis of VPS35 expression ( n = 3, independent experiments for B ; n = 5 mice for C) . D Validation of the overexpression of VPS35 and Flag in HL-1 cells 96 h after transfection with the lentivirus. E Statistical analysis of VPS35 overexpression (OE) ( n = 3 independent experiments, P = 0.0091). F Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence images by confocal microscopy (red: CS1, green: ATP7A, blue: DAPI). G CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments). H Validation of the levels of DLAT oligomerization, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating vector- and VPS35-overexpressing HL-1 cells with 10 µM CuCl 2 and 10 µM NE for 24 h. I – N Statistical analysis of the levels of DLAT oligomers, DLAT monomer, Lip-DLAT, Lip-DLST, FDX1 and HSP70. The data on Lip-DLAT and Lip-DLST were normalized to tubulin, and the other data were normalized to GAPDH ( n = 4 independent experiments). O Vector- and VPS35-overexpressing HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 6 independent experiments). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA for B , G and I – N , unpaired two-tailed t-test for C and E , and two-way ANOVA for O . Source data are provided as a Source Data file.

    Article Snippet: Histological sections were air-dried, washed off OCT, blocked with 5% goats’ serum for 60 min in room temperature, then incubated with antibody against DLAT (SANTA, sc-271534), TH (Abcam, ab137869) or ATP7A (SANTA, sc-271534) at 4 °C overnight and incubated with secondary antibody (Alexa Fluor 488 or Fluor 594) for 1 h at room temperature.

    Techniques: Expressing, Over Expression, Transfection, Immunofluorescence, Confocal Microscopy, Staining, Fluorescence, Western Blot, Plasmid Preparation, CCK-8 Assay, Two Tailed Test

    A Inductively coupled plasma‒mass spectrometry (ICP‒MS) revealed an increase in the content of myocardial copper ions in mice with sleep fragmentation (SF) and myocardial ischemia‒reperfusion injury (MI/RI) ( n = 5, 5, 6, 6 for Control, SF, I/R, SF + I/R) Control vs. SF: P = 0.0077, the rest all P < 0.0001. I/R, ischemia‒reperfusion. B Schematic diagram of copper transport in cardiomyocytes. C , D RT‒qPCR analyses of the mRNA levels of Slc31a1 and Atp7a ( n = 5 mice per group, P = 0.0485 for C , P = 0.0550 for D) . E Validation of the expression levels of ATP7A in the myocardium by Western blotting. F Statistical analysis of ATP7A expression, which was normalized to tubulin ( n = 5 mice per group, P = 0.0372). G Representative images of immunofluorescence staining of the myocardium by confocal microscopy (red, WGA; green, ATP7A; blue, DAPI) captured from the anterolateral wall of the mid-lower segment of the left ventricle. The red arrow indicates ATP7A located around the cell nucleus, while the white arrow indicates ATP7A free in the cytoplasm. Scale bar, 20 µm. H – J Cardiac electrophysiology telemetry revealed that SF mice show faster resting heart rate (HR) and lower high frequency power spectral density (HF) ( n = 7 mice per group, P = < 0.0001 for I , P = 0.0030 for J) . K Representative images of sympathetic nerve terminals in mouse myocardial tissue slices were obtained by immunofluorescence staining of tyrosine hydroxylase (left: global image of the heart; middle: local image of the heart; right: 3D reconstruction of sympathetic nerves in thick slices of the heart). L , M The domination of myocardial sympathetic nerves was quantified by the percentage of TH-expressing area and the mean fluorescence intensity ( n = 10 mice per group, P = 0.0001 for L , P < 0.0001 for M) . N , O ELISA was performed to detect norepinephrine (NE) and epinephrine (EPI) in the cardiac tissue homogenate ( n = 8 mice per group, P = 0.0006 for N , P = 0.1908 for O) . Data are presented as the mean ± s.e.m. The significance of differences was evaluated using an unpaired two-tailed t test. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Sleep fragmentation exacerbates myocardial ischemia‒reperfusion injury by promoting copper overload in cardiomyocytes

    doi: 10.1038/s41467-024-48227-y

    Figure Lengend Snippet: A Inductively coupled plasma‒mass spectrometry (ICP‒MS) revealed an increase in the content of myocardial copper ions in mice with sleep fragmentation (SF) and myocardial ischemia‒reperfusion injury (MI/RI) ( n = 5, 5, 6, 6 for Control, SF, I/R, SF + I/R) Control vs. SF: P = 0.0077, the rest all P < 0.0001. I/R, ischemia‒reperfusion. B Schematic diagram of copper transport in cardiomyocytes. C , D RT‒qPCR analyses of the mRNA levels of Slc31a1 and Atp7a ( n = 5 mice per group, P = 0.0485 for C , P = 0.0550 for D) . E Validation of the expression levels of ATP7A in the myocardium by Western blotting. F Statistical analysis of ATP7A expression, which was normalized to tubulin ( n = 5 mice per group, P = 0.0372). G Representative images of immunofluorescence staining of the myocardium by confocal microscopy (red, WGA; green, ATP7A; blue, DAPI) captured from the anterolateral wall of the mid-lower segment of the left ventricle. The red arrow indicates ATP7A located around the cell nucleus, while the white arrow indicates ATP7A free in the cytoplasm. Scale bar, 20 µm. H – J Cardiac electrophysiology telemetry revealed that SF mice show faster resting heart rate (HR) and lower high frequency power spectral density (HF) ( n = 7 mice per group, P = < 0.0001 for I , P = 0.0030 for J) . K Representative images of sympathetic nerve terminals in mouse myocardial tissue slices were obtained by immunofluorescence staining of tyrosine hydroxylase (left: global image of the heart; middle: local image of the heart; right: 3D reconstruction of sympathetic nerves in thick slices of the heart). L , M The domination of myocardial sympathetic nerves was quantified by the percentage of TH-expressing area and the mean fluorescence intensity ( n = 10 mice per group, P = 0.0001 for L , P < 0.0001 for M) . N , O ELISA was performed to detect norepinephrine (NE) and epinephrine (EPI) in the cardiac tissue homogenate ( n = 8 mice per group, P = 0.0006 for N , P = 0.1908 for O) . Data are presented as the mean ± s.e.m. The significance of differences was evaluated using an unpaired two-tailed t test. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.

    Article Snippet: The fluorescence results of other cells for ATP7A and DLAT were acquired with a 63× oil immersion lens using a microscope (ZEISS ApoTome.2) equipped with ZEN software (Carl Zeiss, v2009).

    Techniques: Expressing, Western Blot, Immunofluorescence, Staining, Confocal Microscopy, Fluorescence, Enzyme-linked Immunosorbent Assay, Two Tailed Test

    A Schematic diagram of the experimental groups in the cell model. HL-1 cells were treated with 10 µM CuCl 2 in the presence of solvent (DMSO), 1 µM NE or 10 µM NE for 24 h. B Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence imaging by confocal microscopy (red: Coppersensor1 (CS1; indicates intracellular copper ions), green: ATP7A, blue: DAPI). Scale bar = 20 μm. C CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments, Cu vs. Cu+NE Low : P = 0.0124, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0014). D Representative images of DLAT oligomer immunofluorescence imaging by confocal microscopy. Scale bar = 20 μm. E DLAT oligomer levels were quantified by calculating the mean fluorescence intensity ( n = 10 cells examined over 5 independent experiments, Cu vs. Cu+NE Low : P = 0.5537, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001). F Validation of the levels of DLAT oligomers, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating HL-1 cells with 10 µM CuCl 2 in the presence of NE (1 µM, 10 µM) or DMSO for 24 h. G – K Statistical analysis of DLAT oligomers (Cu vs. Cu+NE Low : P = 0.0217, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0066), DLAT monomer (Cu vs. Cu+NE Low : P = 0.0198, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0129), Lip-DLST (Cu vs. Cu+NE Low : P = 0.0447, Cu vs. Cu+NE High : P = 0.0003, Cu+NE Low vs. Cu+NE High : P = 0.0536), FDX1 (Cu vs. Cu+NE Low : P = 0.0022, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001) and HSP70 (Cu vs. Cu+NE Low : P = 0.0018, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0005). The data on these proteins were normalized to GAPDH ( n = 6 independent experiments). L HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 8 independent experiments, Cu vs. Cu+1uM NE: P = 0.0007, Cu vs. Cu+5uM NE: P = 0.0029, Cu vs. Cu+10uM NE: P < 0.0001, Cu vs. Cu+50uM NE: P < 0.0001). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Sleep fragmentation exacerbates myocardial ischemia‒reperfusion injury by promoting copper overload in cardiomyocytes

    doi: 10.1038/s41467-024-48227-y

    Figure Lengend Snippet: A Schematic diagram of the experimental groups in the cell model. HL-1 cells were treated with 10 µM CuCl 2 in the presence of solvent (DMSO), 1 µM NE or 10 µM NE for 24 h. B Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence imaging by confocal microscopy (red: Coppersensor1 (CS1; indicates intracellular copper ions), green: ATP7A, blue: DAPI). Scale bar = 20 μm. C CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments, Cu vs. Cu+NE Low : P = 0.0124, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0014). D Representative images of DLAT oligomer immunofluorescence imaging by confocal microscopy. Scale bar = 20 μm. E DLAT oligomer levels were quantified by calculating the mean fluorescence intensity ( n = 10 cells examined over 5 independent experiments, Cu vs. Cu+NE Low : P = 0.5537, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001). F Validation of the levels of DLAT oligomers, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating HL-1 cells with 10 µM CuCl 2 in the presence of NE (1 µM, 10 µM) or DMSO for 24 h. G – K Statistical analysis of DLAT oligomers (Cu vs. Cu+NE Low : P = 0.0217, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0066), DLAT monomer (Cu vs. Cu+NE Low : P = 0.0198, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0129), Lip-DLST (Cu vs. Cu+NE Low : P = 0.0447, Cu vs. Cu+NE High : P = 0.0003, Cu+NE Low vs. Cu+NE High : P = 0.0536), FDX1 (Cu vs. Cu+NE Low : P = 0.0022, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P < 0.0001) and HSP70 (Cu vs. Cu+NE Low : P = 0.0018, Cu vs. Cu+NE High : P < 0.0001, Cu+NE Low vs. Cu+NE High : P = 0.0005). The data on these proteins were normalized to GAPDH ( n = 6 independent experiments). L HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 8 independent experiments, Cu vs. Cu+1uM NE: P = 0.0007, Cu vs. Cu+5uM NE: P = 0.0029, Cu vs. Cu+10uM NE: P < 0.0001, Cu vs. Cu+50uM NE: P < 0.0001). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA. * P < 0.05, ** P < 0.01, *** P < 0.001. Source data are provided as a Source Data file.

    Article Snippet: The fluorescence results of other cells for ATP7A and DLAT were acquired with a 63× oil immersion lens using a microscope (ZEISS ApoTome.2) equipped with ZEN software (Carl Zeiss, v2009).

    Techniques: Solvent, Immunofluorescence, Imaging, Confocal Microscopy, Staining, Fluorescence, Western Blot, CCK-8 Assay

    A Validation of the expression levels of VPS35. Statistical analysis of VPS35 expression ( n = 3, independent experiments for B ; n = 5 mice for C) . D Validation of the overexpression of VPS35 and Flag in HL-1 cells 96 h after transfection with the lentivirus. E Statistical analysis of VPS35 overexpression (OE) ( n = 3 independent experiments, P = 0.0091). F Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence images by confocal microscopy (red: CS1, green: ATP7A, blue: DAPI). G CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments). H Validation of the levels of DLAT oligomerization, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating vector- and VPS35-overexpressing HL-1 cells with 10 µM CuCl 2 and 10 µM NE for 24 h. I – N Statistical analysis of the levels of DLAT oligomers, DLAT monomer, Lip-DLAT, Lip-DLST, FDX1 and HSP70. The data on Lip-DLAT and Lip-DLST were normalized to tubulin, and the other data were normalized to GAPDH ( n = 4 independent experiments). O Vector- and VPS35-overexpressing HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 6 independent experiments). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA for B , G and I – N , unpaired two-tailed t-test for C and E , and two-way ANOVA for O . Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Sleep fragmentation exacerbates myocardial ischemia‒reperfusion injury by promoting copper overload in cardiomyocytes

    doi: 10.1038/s41467-024-48227-y

    Figure Lengend Snippet: A Validation of the expression levels of VPS35. Statistical analysis of VPS35 expression ( n = 3, independent experiments for B ; n = 5 mice for C) . D Validation of the overexpression of VPS35 and Flag in HL-1 cells 96 h after transfection with the lentivirus. E Statistical analysis of VPS35 overexpression (OE) ( n = 3 independent experiments, P = 0.0091). F Representative images of copper overload and ATP7A localization in both wide-field and confocal immunofluorescence images by confocal microscopy (red: CS1, green: ATP7A, blue: DAPI). G CS1 staining was quantified by calculating the mean fluorescence intensity ( n = 8 independent experiments). H Validation of the levels of DLAT oligomerization, lipoylated proteins, iron-sulfur cluster proteins and HSP70 by Western blotting after treating vector- and VPS35-overexpressing HL-1 cells with 10 µM CuCl 2 and 10 µM NE for 24 h. I – N Statistical analysis of the levels of DLAT oligomers, DLAT monomer, Lip-DLAT, Lip-DLST, FDX1 and HSP70. The data on Lip-DLAT and Lip-DLST were normalized to tubulin, and the other data were normalized to GAPDH ( n = 4 independent experiments). O Vector- and VPS35-overexpressing HL-1 cells were treated with 10 µM CuCl2 in the presence of different concentrations of NE for 12 h, and cell viability was determined using a CCK-8 assay ( n = 6 independent experiments). All data are presented as the mean ± s.e.m. The significance of differences was evaluated using one-way ANOVA for B , G and I – N , unpaired two-tailed t-test for C and E , and two-way ANOVA for O . Source data are provided as a Source Data file.

    Article Snippet: The fluorescence results of other cells for ATP7A and DLAT were acquired with a 63× oil immersion lens using a microscope (ZEISS ApoTome.2) equipped with ZEN software (Carl Zeiss, v2009).

    Techniques: Expressing, Over Expression, Transfection, Immunofluorescence, Confocal Microscopy, Staining, Fluorescence, Western Blot, Plasmid Preparation, CCK-8 Assay, Two Tailed Test