Protein acetylation

Saxholm, Harald J.K.; Pestaña, Ángel; O'Connor, Lawrence T.; Sattler, Carol A.; Pitot, Henry C.

doi:10.1007/bf00239663

Cited by 15 publications

(6 citation statements)

References 86 publications

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“…Not only does acetyl-CoA lie at the intersection of various metabolic pathways, it also provides the acetyl group for numerous protein acetylation reactions (Saxholm et al 1982). Thus, acetyl-CoA is ideally situated to link metabolic status to the control of cellular activities.…”

Section: Acetylation Of Proteinsmentioning

confidence: 99%

On Acetyl-CoA as a Gauge of Cellular Metabolic State

Cai¹,

Tu²

2011

Cold Spring Harbor Symposia on Quantitative Biology

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Many activities within a cell must be intimately coordinated with its metabolic state. Understanding these connections to metabolism is critical to deciphering the regulation of a variety of cellular processes. However, despite intensive research in these areas, the precise mechanisms by which a cell monitors its metabolic state remain controversial and poorly understood. Herein, we discuss the thesis that intracellular levels of the metabolite acetyl-CoA represent a critical gauge of cellular metabolic state, which is cleverly monitored by the cell through dynamic acetylation modifications to direct a variety of outputs connected to energy metabolism, cell growth, and survival.

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Section: Acetylation Of Proteinsmentioning

confidence: 99%

On Acetyl-CoA as a Gauge of Cellular Metabolic State

Cai¹,

Tu²

2011

Cold Spring Harbor Symposia on Quantitative Biology

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“…CoA may act as an acyl group carrier to form acetyl-CoA and other related compounds; this is a way to transport carbon atoms within the cell. CoA is critical in the metabolism and synthesis of carbohydrates, proteins and fats [26,27]. Clinically, cysteamine has been used in the treatment of cystinosis and cystinuria [28,29].…”

Section: Introductionmentioning

confidence: 99%

Ghrelin accelerates the healing of cysteamine-induced duodenal ulcers in rats

et al. 2012

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SummaryBackgroundPrevious studies have shown that administration of ghrelin exhibits protective and therapeutic effects in the gut. The aim of the present investigation was to examine the influence of ghrelin administration on the course of cysteamine-induced duodenal ulcers, as well as effects on mucosal production of oxygen free radicals and duodenal antioxidant defense.Material/MethodsDuodenal ulcers were induced in male Wistar rats by cysteamine administered intragastrically at the dose of 200 mg/kg in 1 ml of saline, 3 times at 4-h intervals. Starting 24 h after the first dose of cysteamine, rats were treated intraperitoneally twice a day with saline or ghrelin given at the dose of 4, 8 or 16 nmol/kg/dose. Seven days after administration of the first dose of cysteamine, the study was terminated.ResultsInduction of ulcers by cysteamine was accompanied by a reduction in duodenal blood flow, mucosal DNA synthesis and mucosal activity of superoxide dismutase (SOD); whereas mucosal concentration of interleukin-1β and malonyldialdehyde (MDA – an index of lipid peroxidation) were increased. Treatment with ghrelin increased healing rate of duodenal ulcers and enhanced duodenal blood flow, mucosal DNA synthesis and mucosal activity of SOD, and reduced mucosal concentration of interleukin-1β and MDA.ConclusionsTreatment with ghrelin increases the healing rate of duodenal ulcers and this effect is related, at least in part, to improvement of duodenal mucosal blood flow, mucosal cell proliferation and antioxidant defense, as well as being related to reduction in mucosal oxidative stress and inflammatory response.

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“…The first observation of an acetylated peptide was made by Narita in 1958 ( 15 , 16 ). This was followed by others, highlighting amino-terminal acetylation of non-histone proteins.…”

Section: Protein Acetylation a Post-translational Mechanism Sensing mentioning

confidence: 99%

The Regulation of Insulin-Stimulated Cardiac Glucose Transport via Protein Acetylation

Renguet

Bultot

Beauloye

et al. 2018

Front. Cardiovasc. Med.

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Cellular catabolism is the cell capacity to generate energy from various substrates to sustain its function. To optimize this energy production, cells are able to switch between various metabolic pathways in accordance to substrate availability via a modulation of several regulatory enzymes. This metabolic flexibility is essential for the healthy heart, an organ requiring large quantities of ATP to sustain its contractile function. In type 2 diabetes, excess of non-glucidic nutrients such as fatty acids, branched-chain amino-acids, or ketones bodies, induces cardiac metabolic inflexibility. It is characterized by a preferential use of these alternative substrates to the detriment of glucose, this participating in cardiomyocytes dysfunction and development of diabetic cardiomyopathy. Identification of the molecular mechanisms leading to this metabolic inflexibility have been scrutinized during last decades. In 1963, Randle demonstrated that accumulation of some metabolites from fatty acid metabolism are able to allosterically inhibit regulatory steps of glucose metabolism leading to a preferential use of fatty acids by the heart. Nevertheless, this model does not fully recapitulate observations made in diabetic patients, calling for a more complex model. A new piece of the puzzle emerges from recent evidences gathered from different laboratories showing that metabolism of the non-glucidic substrates induces an increase in acetylation levels of proteins which is concomitant to the perturbation of glucose transport. The purpose of the present review is to gather, in a synthetic model, the different evidences that demonstrate the role of acetylation in the inhibition of the insulin-stimulated glucose uptake in cardiac muscle.

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Protein acetylation

Cited by 15 publications

References 86 publications

On Acetyl-CoA as a Gauge of Cellular Metabolic State

On Acetyl-CoA as a Gauge of Cellular Metabolic State

Ghrelin accelerates the healing of cysteamine-induced duodenal ulcers in rats

The Regulation of Insulin-Stimulated Cardiac Glucose Transport via Protein Acetylation

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