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The pivotal role of protein acetylation in linking glucose and fatty acid metabolism to β-cell function
by
Bi, Yufang
, Zhang, Linlin
, Zhang, Yuqing
, Zhou, Feiye
, Bai, Mengyao
, Liu, Yun
, Zhou, Libin
, Wang, Xiao
, Zhu, Qin
, Ning, Guang
in
13/106
/ 631/337/458/1275
/ 64/60
/ 692/163/2743/137/773
/ 82/58
/ 96/1
/ 96/44
/ Acetylation
/ Animals
/ Antibodies
/ Biochemistry
/ Biomedical and Life Sciences
/ Cell Biology
/ Cell Culture
/ Energy metabolism
/ Enzyme Stability
/ Enzymes
/ Fasting
/ Fatty acids
/ Fatty Acids - metabolism
/ Glucose
/ Glucose - metabolism
/ HEK293 Cells
/ Humans
/ Immunology
/ Insulin
/ Insulin secretion
/ Insulin Secretion - physiology
/ Insulin-Secreting Cells - physiology
/ Life Sciences
/ Male
/ Metabolic pathways
/ Metabolism
/ Mice
/ Mice, Inbred C57BL
/ Mice, Knockout
/ Mitochondria
/ Mitochondrial Trifunctional Protein, alpha Subunit - metabolism
/ Oxidation
/ Oxidation-Reduction
/ Palmitic acid
/ Protein turnover
/ Proteins
/ Rats
/ Rats, Sprague-Dawley
/ Secretion
/ Sirtuin 3 - genetics
/ Sirtuin 3 - metabolism
/ Sirtuins - metabolism
/ Transfection
2019
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The pivotal role of protein acetylation in linking glucose and fatty acid metabolism to β-cell function
by
Bi, Yufang
, Zhang, Linlin
, Zhang, Yuqing
, Zhou, Feiye
, Bai, Mengyao
, Liu, Yun
, Zhou, Libin
, Wang, Xiao
, Zhu, Qin
, Ning, Guang
in
13/106
/ 631/337/458/1275
/ 64/60
/ 692/163/2743/137/773
/ 82/58
/ 96/1
/ 96/44
/ Acetylation
/ Animals
/ Antibodies
/ Biochemistry
/ Biomedical and Life Sciences
/ Cell Biology
/ Cell Culture
/ Energy metabolism
/ Enzyme Stability
/ Enzymes
/ Fasting
/ Fatty acids
/ Fatty Acids - metabolism
/ Glucose
/ Glucose - metabolism
/ HEK293 Cells
/ Humans
/ Immunology
/ Insulin
/ Insulin secretion
/ Insulin Secretion - physiology
/ Insulin-Secreting Cells - physiology
/ Life Sciences
/ Male
/ Metabolic pathways
/ Metabolism
/ Mice
/ Mice, Inbred C57BL
/ Mice, Knockout
/ Mitochondria
/ Mitochondrial Trifunctional Protein, alpha Subunit - metabolism
/ Oxidation
/ Oxidation-Reduction
/ Palmitic acid
/ Protein turnover
/ Proteins
/ Rats
/ Rats, Sprague-Dawley
/ Secretion
/ Sirtuin 3 - genetics
/ Sirtuin 3 - metabolism
/ Sirtuins - metabolism
/ Transfection
2019
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The pivotal role of protein acetylation in linking glucose and fatty acid metabolism to β-cell function
by
Bi, Yufang
, Zhang, Linlin
, Zhang, Yuqing
, Zhou, Feiye
, Bai, Mengyao
, Liu, Yun
, Zhou, Libin
, Wang, Xiao
, Zhu, Qin
, Ning, Guang
in
13/106
/ 631/337/458/1275
/ 64/60
/ 692/163/2743/137/773
/ 82/58
/ 96/1
/ 96/44
/ Acetylation
/ Animals
/ Antibodies
/ Biochemistry
/ Biomedical and Life Sciences
/ Cell Biology
/ Cell Culture
/ Energy metabolism
/ Enzyme Stability
/ Enzymes
/ Fasting
/ Fatty acids
/ Fatty Acids - metabolism
/ Glucose
/ Glucose - metabolism
/ HEK293 Cells
/ Humans
/ Immunology
/ Insulin
/ Insulin secretion
/ Insulin Secretion - physiology
/ Insulin-Secreting Cells - physiology
/ Life Sciences
/ Male
/ Metabolic pathways
/ Metabolism
/ Mice
/ Mice, Inbred C57BL
/ Mice, Knockout
/ Mitochondria
/ Mitochondrial Trifunctional Protein, alpha Subunit - metabolism
/ Oxidation
/ Oxidation-Reduction
/ Palmitic acid
/ Protein turnover
/ Proteins
/ Rats
/ Rats, Sprague-Dawley
/ Secretion
/ Sirtuin 3 - genetics
/ Sirtuin 3 - metabolism
/ Sirtuins - metabolism
/ Transfection
2019
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The pivotal role of protein acetylation in linking glucose and fatty acid metabolism to β-cell function
Journal Article
The pivotal role of protein acetylation in linking glucose and fatty acid metabolism to β-cell function
2019
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Overview
Protein acetylation has a crucial role in energy metabolism. Here we performed the first large-scale profiling of acetylome in rat islets, showing that almost all enzymes in core metabolic pathways related to insulin secretion were acetylated. Label-free quantitative acetylome of islets in response to high glucose revealed hyperacetylation of enzymes involved in fatty acid β-oxidation (FAO), including trifunctional enzyme subunit alpha (ECHA). Acetylation decreased the protein stability of ECHA and its ability to promote FAO. The overexpression of SIRT3, a major mitochondrial deacetylase, prevented the degradation of ECHA via decreasing its acetylation level in β-cells. SIRT3 expression was upregulated in rat islets upon exposure to low glucose or fasting. SIRT3 overexpression in islets markedly decreased palmitate-potentiated insulin secretion, whereas islets from SIRT3 knockout mice secreted more insulin, with an opposite action on FAO. ECHA overexpression partially reversed SIRT3 deficiency-elicited insulin hypersecretion. Our study highlights the potential role of protein acetylation in insulin secretion.
Publisher
Nature Publishing Group UK,Springer Nature B.V
Subject
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