Sulfhydrated Sirtuin-1 Increasing Its Deacetylation Activity Is an Essential Epigenetics Mechanism of Anti-Atherogenesis by Hydrogen Sulfide
Hydrogen sulfide (H2S) has a protective role in the pathogenesis of atherosclerosis by multiple pathways. Sirtuin-1 ( ) is a histone deacetylase, as an essential mediated longevity gene, and has an anti-atherogenic effect by regulating the acetylation of some functional proteins. Whether is involved...
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| Vydané v: | Antioxidants & redox signaling Ročník 30; číslo 2; s. 184 |
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| Hlavní autori: | , , , , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | English |
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10.01.2019
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| Abstract | Hydrogen sulfide (H2S) has a protective role in the pathogenesis of atherosclerosis by multiple pathways. Sirtuin-1 (
) is a histone deacetylase, as an essential mediated longevity gene, and has an anti-atherogenic effect by regulating the acetylation of some functional proteins. Whether
is involved in protecting H2S in atherosclerosis and its mechanism remains unclear.
In ApoE-knockout atherosclerosis mice, treatment with an H2S donor (NaHS or GYY4137) reduced atherosclerotic plaque area, macrophage infiltration, aortic inflammation, and plasma lipid level. H2S treatment increased aorta and liver
mRNA expression. Overexpression or slicing cystathionine gamma lyase (CSE) also changed intracellular
expression. CSE/H2S treatment increased
deacetylation in endothelium and hepatocytes and macrophages, then induced deacetylation of its target proteins (P53, P65, and sterol response element binding protein), thereby reducing endothelial and macrophage inflammation and inhibiting macrophage cholesterol uptake and cholesterol
synthesis of liver. Also, CSE/H2S induced
sulfhydration at its two zinc finger domains, increased its zinc ion binding activity to stabilize the alpha-helix structure, lowered its ubiquitination, and reduced its degradation.
H2S is a novel
activator by direct sulfhydration. Because
has a role in longevity, H2S may be a protector for aging-related diseases.
Endogenous CSE/H2S directly sulfhydrated
, enhanced
binding to zinc ion, then promoted its deacetylation activity, and increased
stability, thus reducing atherosclerotic plaque formation. |
|---|---|
| AbstractList | Hydrogen sulfide (H2S) has a protective role in the pathogenesis of atherosclerosis by multiple pathways. Sirtuin-1 (
) is a histone deacetylase, as an essential mediated longevity gene, and has an anti-atherogenic effect by regulating the acetylation of some functional proteins. Whether
is involved in protecting H2S in atherosclerosis and its mechanism remains unclear.
In ApoE-knockout atherosclerosis mice, treatment with an H2S donor (NaHS or GYY4137) reduced atherosclerotic plaque area, macrophage infiltration, aortic inflammation, and plasma lipid level. H2S treatment increased aorta and liver
mRNA expression. Overexpression or slicing cystathionine gamma lyase (CSE) also changed intracellular
expression. CSE/H2S treatment increased
deacetylation in endothelium and hepatocytes and macrophages, then induced deacetylation of its target proteins (P53, P65, and sterol response element binding protein), thereby reducing endothelial and macrophage inflammation and inhibiting macrophage cholesterol uptake and cholesterol
synthesis of liver. Also, CSE/H2S induced
sulfhydration at its two zinc finger domains, increased its zinc ion binding activity to stabilize the alpha-helix structure, lowered its ubiquitination, and reduced its degradation.
H2S is a novel
activator by direct sulfhydration. Because
has a role in longevity, H2S may be a protector for aging-related diseases.
Endogenous CSE/H2S directly sulfhydrated
, enhanced
binding to zinc ion, then promoted its deacetylation activity, and increased
stability, thus reducing atherosclerotic plaque formation. Aims: Hydrogen sulfide (H2S) has a protective role in the pathogenesis of atherosclerosis by multiple pathways. Sirtuin-1 (SIRT1) is a histone deacetylase, as an essential mediated longevity gene, and has an anti-atherogenic effect by regulating the acetylation of some functional proteins. Whether SIRT1 is involved in protecting H2S in atherosclerosis and its mechanism remains unclear. Results: In ApoE-knockout atherosclerosis mice, treatment with an H2S donor (NaHS or GYY4137) reduced atherosclerotic plaque area, macrophage infiltration, aortic inflammation, and plasma lipid level. H2S treatment increased aorta and liver SIRT1 mRNA expression. Overexpression or slicing cystathionine gamma lyase (CSE) also changed intracellular SIRT1 expression. CSE/H2S treatment increased SIRT1 deacetylation in endothelium and hepatocytes and macrophages, then induced deacetylation of its target proteins (P53, P65, and sterol response element binding protein), thereby reducing endothelial and macrophage inflammation and inhibiting macrophage cholesterol uptake and cholesterol de novo synthesis of liver. Also, CSE/H2S induced SIRT1 sulfhydration at its two zinc finger domains, increased its zinc ion binding activity to stabilize the alpha-helix structure, lowered its ubiquitination, and reduced its degradation. Innovation: H2S is a novel SIRT1 activator by direct sulfhydration. Because SIRT1 has a role in longevity, H2S may be a protector for aging-related diseases. Conclusion: Endogenous CSE/H2S directly sulfhydrated SIRT1, enhanced SIRT1 binding to zinc ion, then promoted its deacetylation activity, and increased SIRT1 stability, thus reducing atherosclerotic plaque formation.Aims: Hydrogen sulfide (H2S) has a protective role in the pathogenesis of atherosclerosis by multiple pathways. Sirtuin-1 (SIRT1) is a histone deacetylase, as an essential mediated longevity gene, and has an anti-atherogenic effect by regulating the acetylation of some functional proteins. Whether SIRT1 is involved in protecting H2S in atherosclerosis and its mechanism remains unclear. Results: In ApoE-knockout atherosclerosis mice, treatment with an H2S donor (NaHS or GYY4137) reduced atherosclerotic plaque area, macrophage infiltration, aortic inflammation, and plasma lipid level. H2S treatment increased aorta and liver SIRT1 mRNA expression. Overexpression or slicing cystathionine gamma lyase (CSE) also changed intracellular SIRT1 expression. CSE/H2S treatment increased SIRT1 deacetylation in endothelium and hepatocytes and macrophages, then induced deacetylation of its target proteins (P53, P65, and sterol response element binding protein), thereby reducing endothelial and macrophage inflammation and inhibiting macrophage cholesterol uptake and cholesterol de novo synthesis of liver. Also, CSE/H2S induced SIRT1 sulfhydration at its two zinc finger domains, increased its zinc ion binding activity to stabilize the alpha-helix structure, lowered its ubiquitination, and reduced its degradation. Innovation: H2S is a novel SIRT1 activator by direct sulfhydration. Because SIRT1 has a role in longevity, H2S may be a protector for aging-related diseases. Conclusion: Endogenous CSE/H2S directly sulfhydrated SIRT1, enhanced SIRT1 binding to zinc ion, then promoted its deacetylation activity, and increased SIRT1 stability, thus reducing atherosclerotic plaque formation. |
| Author | Geng, Bin Xu, Guoheng Cai, Junyan Zheng, Fengjiao Cai, Jun Cui, Qinghua Du, Congkuo Xu, Wenjing Lin, Xianjuan Yang, Jichun Tang, Chaoshu |
| Author_xml | – sequence: 1 givenname: Congkuo surname: Du fullname: Du, Congkuo organization: 1 MOE Key Lab of Cardiovascular Sciences, Department of Physiology and Pathophysiology, Department of Biomedical Informatics, Center for Noncoding RNA Medicine, School of Basic Medical Science, Peking University Health Science Center. Beijing , People's Republic of China – sequence: 2 givenname: Xianjuan surname: Lin fullname: Lin, Xianjuan organization: 1 MOE Key Lab of Cardiovascular Sciences, Department of Physiology and Pathophysiology, Department of Biomedical Informatics, Center for Noncoding RNA Medicine, School of Basic Medical Science, Peking University Health Science Center. Beijing , People's Republic of China – sequence: 3 givenname: Wenjing surname: Xu fullname: Xu, Wenjing organization: 1 MOE Key Lab of Cardiovascular Sciences, Department of Physiology and Pathophysiology, Department of Biomedical Informatics, Center for Noncoding RNA Medicine, School of Basic Medical Science, Peking University Health Science Center. Beijing , People's Republic of China – sequence: 4 givenname: Fengjiao surname: Zheng fullname: Zheng, Fengjiao organization: 1 MOE Key Lab of Cardiovascular Sciences, Department of Physiology and Pathophysiology, Department of Biomedical Informatics, Center for Noncoding RNA Medicine, School of Basic Medical Science, Peking University Health Science Center. Beijing , People's Republic of China – sequence: 5 givenname: Junyan surname: Cai fullname: Cai, Junyan organization: 1 MOE Key Lab of Cardiovascular Sciences, Department of Physiology and Pathophysiology, Department of Biomedical Informatics, Center for Noncoding RNA Medicine, School of Basic Medical Science, Peking University Health Science Center. Beijing , People's Republic of China – sequence: 6 givenname: Jichun surname: Yang fullname: Yang, Jichun organization: 1 MOE Key Lab of Cardiovascular Sciences, Department of Physiology and Pathophysiology, Department of Biomedical Informatics, Center for Noncoding RNA Medicine, School of Basic Medical Science, Peking University Health Science Center. Beijing , People's Republic of China – sequence: 7 givenname: Qinghua surname: Cui fullname: Cui, Qinghua organization: 1 MOE Key Lab of Cardiovascular Sciences, Department of Physiology and Pathophysiology, Department of Biomedical Informatics, Center for Noncoding RNA Medicine, School of Basic Medical Science, Peking University Health Science Center. Beijing , People's Republic of China – sequence: 8 givenname: Chaoshu surname: Tang fullname: Tang, Chaoshu organization: 1 MOE Key Lab of Cardiovascular Sciences, Department of Physiology and Pathophysiology, Department of Biomedical Informatics, Center for Noncoding RNA Medicine, School of Basic Medical Science, Peking University Health Science Center. Beijing , People's Republic of China – sequence: 9 givenname: Jun surname: Cai fullname: Cai, Jun organization: 2 State Key Laboratory of Cardiovascular Disease, Hypertension Center , Fuwai Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, People's Republic of China – sequence: 10 givenname: Guoheng surname: Xu fullname: Xu, Guoheng organization: 1 MOE Key Lab of Cardiovascular Sciences, Department of Physiology and Pathophysiology, Department of Biomedical Informatics, Center for Noncoding RNA Medicine, School of Basic Medical Science, Peking University Health Science Center. Beijing , People's Republic of China – sequence: 11 givenname: Bin surname: Geng fullname: Geng, Bin organization: 2 State Key Laboratory of Cardiovascular Disease, Hypertension Center , Fuwai Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, People's Republic of China |
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| Keywords | atherosclerosis sirtuin1 sulfhydration hydrogen sulfide cystathionine gamma lyase |
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| Snippet | Hydrogen sulfide (H2S) has a protective role in the pathogenesis of atherosclerosis by multiple pathways. Sirtuin-1 (
) is a histone deacetylase, as an... Aims: Hydrogen sulfide (H2S) has a protective role in the pathogenesis of atherosclerosis by multiple pathways. Sirtuin-1 (SIRT1) is a histone deacetylase, as... |
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| SubjectTerms | Acetylation Animals Apolipoproteins E - deficiency Atherosclerosis - drug therapy Atherosclerosis - etiology Atherosclerosis - metabolism Atherosclerosis - pathology Biomarkers Cell Line Cholesterol - metabolism Disease Models, Animal Endothelium - metabolism Epigenesis, Genetic Foam Cells - metabolism Foam Cells - pathology Gene Expression Humans Hydrogen Sulfide - pharmacology Immunohistochemistry Mice Mice, Knockout Plaque, Atherosclerotic - drug therapy Plaque, Atherosclerotic - etiology Plaque, Atherosclerotic - metabolism Plaque, Atherosclerotic - pathology Protein Processing, Post-Translational Sirtuin 1 - genetics Sirtuin 1 - metabolism Ubiquitination |
| Title | Sulfhydrated Sirtuin-1 Increasing Its Deacetylation Activity Is an Essential Epigenetics Mechanism of Anti-Atherogenesis by Hydrogen Sulfide |
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