The Experts below are selected from a list of 45 Experts worldwide ranked by ideXlab platform
Holger Prokisch - One of the best experts on this subject based on the ideXlab platform.
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SDHAF1, encoding a LYR complex-II specific assembly factor, is mutated in SDH-defective infantile leukoencephalopathy
Nature Genetics, 2009Co-Authors: Daniele Ghezzi, Paola Goffrini, Graziella Uziel, Rita Horvath, Thomas Klopstock, Hanns Lochmüller, Pio D'adamo, Paolo Gasparini, Tim M. Strom, Holger ProkischAbstract:Massimo Zeviani and colleagues identify a factor, called SDHAF1, required for assembly of the mitochondrial Succinate Dehydrogenase Ubiquinone reductase complex by conducting a genetic analysis of two families segregating a rare, progressive leukoencephalopathy. We report mutations in SDHAF1 , encoding a new LYR-motif protein, in infantile leukoencephalopathy with defective Succinate Dehydrogenase (SDH, complex II). Disruption of the yeast homolog or expression of variants corresponding to human mutants caused SDH deficiency and failure of OXPHOS-dependent growth, whereas SDH activity and amount were restored in mutant fibroblasts proportionally with re-expression of the wild-type gene. SDHAF1 is the first bona fide SDH assembly factor reported in any organism.
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SDHAF1, encoding a LYR complex-II specific assembly factor, is mutated in SDH-defective infantile leukoencephalopathy.
Nature Genetics, 2009Co-Authors: Daniele Ghezzi, Paola Goffrini, Graziella Uziel, Rita Horvath, Thomas Klopstock, Hanns Lochmüller, Pio D'adamo, Paolo Gasparini, Tim M. Strom, Holger ProkischAbstract:Massimo Zeviani and colleagues identify a factor, called SDHAF1, required for assembly of the mitochondrial Succinate Dehydrogenase Ubiquinone reductase complex by conducting a genetic analysis of two families segregating a rare, progressive leukoencephalopathy.
Ying-ming Liou - One of the best experts on this subject based on the ideXlab platform.
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Molecular identification for epigallocatechin-3- gallate-mediated antioxidant intervention on the H 2 O 2 -induced oxidative stress in H9c2 rat
2020Co-Authors: Wei-cheng Chen, Shih-rong Hsieh, Chun-hwei Chiu, Ying-ming LiouAbstract:Background: Epigallocatechin-3-gallate (EGCG) has been documented for its beneficial effects protecting oxidative stress to cardiac cells. Previously, we have shown the EGCG-mediated cardiac protection by attenuating reactive oxygen species and cytosolic Ca 2+ in cardiac cells during oxidative stress and myocardial ischemia. Here, we aimed to seek a deeper elucidation of the molecular anti-oxidative capabilities of EGCG in an H2O2-induced oxidative stress model of myocardial ischemia injury using H9c2 rat cardiomyoblasts. Results: Proteomics analysis was used to determine the differential expression of proteins in H9c2 cells cultured in the conditions of control, 400 μ MH 2O2 exposure for 30 min with and/or without 10 to 20 μM EGCG pre-treatment. In this model, eight proteins associated with energy metabolism, mitochondrial electron transfer, redox regulation, signal transduction, and RNA binding were identified to take part in EGCG-ameliorating H2O2-induced injury in H9c2 cells. H2O2 exposure increased oxidative stress evidenced by increases in reactive oxygen species and cytosolic Ca 2+ overload, increases in glycolytic protein, α-enolase, decreases in antioxidant protein, peroxiredoxin-4, as well as decreases in mitochondrial proteins, including aldehyde Dehydrogenase-2 ,o rnithine aminotransferase, and Succinate Dehydrogenase Ubiquinone flavoprotein subunit. All of these effects were reversed by EGCG pre-treatment. In addition, EGCG attenuated the H2O2-induced increases of Type II inositol 3, 4-bisphosphate 4-phosphatase and relieved its subsequent inhibition of the downstream signalling for Akt and glycogen synthase kinase-3β (GSK-3β)/cyclin D1 in H9c2 cells. Pre-treatment with EGCG or GSK-3β inhibitor (SB 216763) significantly improved the H2O2-induced suppression on cell viability, phosphorylation of pAkt (S473) and pGSK-3β (S9), and level of cyclin D1 in cells. Conclusions: Collectively, these findings suggest that EGCG blunts the H2O2-induced oxidative effect on the Akt activity through the modulation of PIP3 synthesis leading to the subsequent inactivation of GSK-3β mediated cardiac cell injury.
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Molecular identification for epigallocatechin-3-gallate-mediated antioxidant intervention on the H2O2-induced oxidative stress in H9c2 rat cardiomyoblasts
Journal of Biomedical Science, 2014Co-Authors: Wei-cheng Chen, Shih-rong Hsieh, Chun-hwei Chiu, Ying-ming LiouAbstract:Epigallocatechin-3-gallate (EGCG) has been documented for its beneficial effects protecting oxidative stress to cardiac cells. Previously, we have shown the EGCG-mediated cardiac protection by attenuating reactive oxygen species and cytosolic Ca2+ in cardiac cells during oxidative stress and myocardial ischemia. Here, we aimed to seek a deeper elucidation of the molecular anti-oxidative capabilities of EGCG in an H2O2-induced oxidative stress model of myocardial ischemia injury using H9c2 rat cardiomyoblasts. Proteomics analysis was used to determine the differential expression of proteins in H9c2 cells cultured in the conditions of control, 400 μM H2O2 exposure for 30 min with and/or without 10 to 20 μM EGCG pre-treatment. In this model, eight proteins associated with energy metabolism, mitochondrial electron transfer, redox regulation, signal transduction, and RNA binding were identified to take part in EGCG-ameliorating H2O2-induced injury in H9c2 cells. H2O2 exposure increased oxidative stress evidenced by increases in reactive oxygen species and cytosolic Ca2+ overload, increases in glycolytic protein, α-enolase, decreases in antioxidant protein, peroxiredoxin-4, as well as decreases in mitochondrial proteins, including aldehyde Dehydrogenase-2, ornithine aminotransferase, and Succinate Dehydrogenase Ubiquinone flavoprotein subunit. All of these effects were reversed by EGCG pre-treatment. In addition, EGCG attenuated the H2O2-induced increases of Type II inositol 3, 4-bisphosphate 4-phosphatase and relieved its subsequent inhibition of the downstream signalling for Akt and glycogen synthase kinase-3β (GSK-3β)/cyclin D1 in H9c2 cells. Pre-treatment with EGCG or GSK-3β inhibitor (SB 216763) significantly improved the H2O2-induced suppression on cell viability, phosphorylation of pAkt (S473) and pGSK-3β (S9), and level of cyclin D1 in cells. Collectively, these findings suggest that EGCG blunts the H2O2-induced oxidative effect on the Akt activity through the modulation of PIP3 synthesis leading to the subsequent inactivation of GSK-3β mediated cardiac cell injury.
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Molecular identification for epigallocatechin-3-gallate-mediated antioxidant intervention on the H_2O_2-induced oxidative stress in H9c2 rat cardiomyoblasts
Journal of Biomedical Science, 2014Co-Authors: Wei-cheng Chen, Shih-rong Hsieh, Chun-hwei Chiu, Ying-ming LiouAbstract:Background Epigallocatechin-3-gallate (EGCG) has been documented for its beneficial effects protecting oxidative stress to cardiac cells. Previously, we have shown the EGCG-mediated cardiac protection by attenuating reactive oxygen species and cytosolic Ca^2+ in cardiac cells during oxidative stress and myocardial ischemia. Here, we aimed to seek a deeper elucidation of the molecular anti-oxidative capabilities of EGCG in an H_2O_2-induced oxidative stress model of myocardial ischemia injury using H9c2 rat cardiomyoblasts. Results Proteomics analysis was used to determine the differential expression of proteins in H9c2 cells cultured in the conditions of control, 400 μM H_2O_2 exposure for 30 min with and/or without 10 to 20 μM EGCG pre-treatment. In this model, eight proteins associated with energy metabolism, mitochondrial electron transfer, redox regulation, signal transduction, and RNA binding were identified to take part in EGCG-ameliorating H_2O_2-induced injury in H9c2 cells. H_2O_2 exposure increased oxidative stress evidenced by increases in reactive oxygen species and cytosolic Ca^2+ overload, increases in glycolytic protein, α-enolase, decreases in antioxidant protein, peroxiredoxin-4 , as well as decreases in mitochondrial proteins, including aldehyde Dehydrogenase-2 , o rnithine aminotransferase , and Succinate Dehydrogenase Ubiquinone flavoprotein subunit . All of these effects were reversed by EGCG pre-treatment. In addition, EGCG attenuated the H_2O_2-induced increases of Type II inositol 3, 4-bisphosphate 4-phosphatase and relieved its subsequent inhibition of the downstream signalling for Akt and glycogen synthase kinase-3β (GSK-3β)/cyclin D1 in H9c2 cells. Pre-treatment with EGCG or GSK-3β inhibitor (SB 216763) significantly improved the H_2O_2-induced suppression on cell viability, phosphorylation of pAkt (S473) and pGSK-3β (S9), and level of cyclin D1 in cells. Conclusions Collectively, these findings suggest that EGCG blunts the H_2O_2-induced oxidative effect on the Akt activity through the modulation of PIP3 synthesis leading to the subsequent inactivation of GSK-3β mediated cardiac cell injury.
Daniele Ghezzi - One of the best experts on this subject based on the ideXlab platform.
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SDHAF1, encoding a LYR complex-II specific assembly factor, is mutated in SDH-defective infantile leukoencephalopathy
Nature Genetics, 2009Co-Authors: Daniele Ghezzi, Paola Goffrini, Graziella Uziel, Rita Horvath, Thomas Klopstock, Hanns Lochmüller, Pio D'adamo, Paolo Gasparini, Tim M. Strom, Holger ProkischAbstract:Massimo Zeviani and colleagues identify a factor, called SDHAF1, required for assembly of the mitochondrial Succinate Dehydrogenase Ubiquinone reductase complex by conducting a genetic analysis of two families segregating a rare, progressive leukoencephalopathy. We report mutations in SDHAF1 , encoding a new LYR-motif protein, in infantile leukoencephalopathy with defective Succinate Dehydrogenase (SDH, complex II). Disruption of the yeast homolog or expression of variants corresponding to human mutants caused SDH deficiency and failure of OXPHOS-dependent growth, whereas SDH activity and amount were restored in mutant fibroblasts proportionally with re-expression of the wild-type gene. SDHAF1 is the first bona fide SDH assembly factor reported in any organism.
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SDHAF1, encoding a LYR complex-II specific assembly factor, is mutated in SDH-defective infantile leukoencephalopathy.
Nature Genetics, 2009Co-Authors: Daniele Ghezzi, Paola Goffrini, Graziella Uziel, Rita Horvath, Thomas Klopstock, Hanns Lochmüller, Pio D'adamo, Paolo Gasparini, Tim M. Strom, Holger ProkischAbstract:Massimo Zeviani and colleagues identify a factor, called SDHAF1, required for assembly of the mitochondrial Succinate Dehydrogenase Ubiquinone reductase complex by conducting a genetic analysis of two families segregating a rare, progressive leukoencephalopathy.
Rita Horvath - One of the best experts on this subject based on the ideXlab platform.
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SDHAF1, encoding a LYR complex-II specific assembly factor, is mutated in SDH-defective infantile leukoencephalopathy
Nature Genetics, 2009Co-Authors: Daniele Ghezzi, Paola Goffrini, Graziella Uziel, Rita Horvath, Thomas Klopstock, Hanns Lochmüller, Pio D'adamo, Paolo Gasparini, Tim M. Strom, Holger ProkischAbstract:Massimo Zeviani and colleagues identify a factor, called SDHAF1, required for assembly of the mitochondrial Succinate Dehydrogenase Ubiquinone reductase complex by conducting a genetic analysis of two families segregating a rare, progressive leukoencephalopathy. We report mutations in SDHAF1 , encoding a new LYR-motif protein, in infantile leukoencephalopathy with defective Succinate Dehydrogenase (SDH, complex II). Disruption of the yeast homolog or expression of variants corresponding to human mutants caused SDH deficiency and failure of OXPHOS-dependent growth, whereas SDH activity and amount were restored in mutant fibroblasts proportionally with re-expression of the wild-type gene. SDHAF1 is the first bona fide SDH assembly factor reported in any organism.
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SDHAF1, encoding a LYR complex-II specific assembly factor, is mutated in SDH-defective infantile leukoencephalopathy.
Nature Genetics, 2009Co-Authors: Daniele Ghezzi, Paola Goffrini, Graziella Uziel, Rita Horvath, Thomas Klopstock, Hanns Lochmüller, Pio D'adamo, Paolo Gasparini, Tim M. Strom, Holger ProkischAbstract:Massimo Zeviani and colleagues identify a factor, called SDHAF1, required for assembly of the mitochondrial Succinate Dehydrogenase Ubiquinone reductase complex by conducting a genetic analysis of two families segregating a rare, progressive leukoencephalopathy.
Thomas Klopstock - One of the best experts on this subject based on the ideXlab platform.
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SDHAF1, encoding a LYR complex-II specific assembly factor, is mutated in SDH-defective infantile leukoencephalopathy
Nature Genetics, 2009Co-Authors: Daniele Ghezzi, Paola Goffrini, Graziella Uziel, Rita Horvath, Thomas Klopstock, Hanns Lochmüller, Pio D'adamo, Paolo Gasparini, Tim M. Strom, Holger ProkischAbstract:Massimo Zeviani and colleagues identify a factor, called SDHAF1, required for assembly of the mitochondrial Succinate Dehydrogenase Ubiquinone reductase complex by conducting a genetic analysis of two families segregating a rare, progressive leukoencephalopathy. We report mutations in SDHAF1 , encoding a new LYR-motif protein, in infantile leukoencephalopathy with defective Succinate Dehydrogenase (SDH, complex II). Disruption of the yeast homolog or expression of variants corresponding to human mutants caused SDH deficiency and failure of OXPHOS-dependent growth, whereas SDH activity and amount were restored in mutant fibroblasts proportionally with re-expression of the wild-type gene. SDHAF1 is the first bona fide SDH assembly factor reported in any organism.
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SDHAF1, encoding a LYR complex-II specific assembly factor, is mutated in SDH-defective infantile leukoencephalopathy.
Nature Genetics, 2009Co-Authors: Daniele Ghezzi, Paola Goffrini, Graziella Uziel, Rita Horvath, Thomas Klopstock, Hanns Lochmüller, Pio D'adamo, Paolo Gasparini, Tim M. Strom, Holger ProkischAbstract:Massimo Zeviani and colleagues identify a factor, called SDHAF1, required for assembly of the mitochondrial Succinate Dehydrogenase Ubiquinone reductase complex by conducting a genetic analysis of two families segregating a rare, progressive leukoencephalopathy.
