hexokinase/نخر

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Reduced hexokinase II impairs muscle function 2 wk after ischemia-reperfusion through increased cell necrosis and fibrosis.

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We previously demonstrated that hexokinase (HK) II plays a key role in the pathophysiology of ischemia-reperfusion (I/R) injury of the heart (Smeele et al. Circ Res 108: 1165-1169, 2011; Wu et al. Circ Res 108: 60-69, 2011). However, it is unknown whether HKII also plays a key role in I/R injury and

Disruption of hexokinase II-mitochondrial binding blocks ischemic preconditioning and causes rapid cardiac necrosis.

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BACKGROUND Isoforms I and II of the glycolytic enzyme hexokinase (HKI and HKII) are known to associate with mitochondria. It is unknown whether mitochondria-bound hexokinase is mandatory for ischemic preconditioning and normal functioning of the intact, beating heart. OBJECTIVE We hypothesized that

T cell immunoglobulin and mucin domain protein 3 inhibits glycolysis in RAW 264.7 macrophages through Hexokinase 2

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T cell immunoglobulin and mucin domain-3 (Tim-3), an immune checkpoint molecule, plays critical roles in maintaining innate immune homeostasis; however, the mechanisms underlying these roles remain to be determined. Here, we determined that Tim-3 controls glycolysis in macrophages, and thus

Gene expression during liver regeneration after partial hepatectomy in mice lacking type 1 tumor necrosis factor receptor.

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BACKGROUND To investigate the function of tumor necrosis factor-alpha (TNF-alpha) during hepatocyte proliferation, we studied liver regeneration following partial hepatectomy in mice lacking type 1 TNF receptor (TNFR-1). METHODS TNFR-1 knockout (KO) and wild-type mice were subjected to partial

Metabolic adaptations in delayed skin flaps. Glucose utilization and hexokinase activity.

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The distribution of glucose and hexokinase activity was determined in the epithelial tissue of delayed bipedicled skin flaps in guinea pigs. The periods of "delay" were 1, 3, 7, 14, or 21 days. The flap survival was maximal (100% of the flap) when the flap elevation was performed either 7 or 14 days

Hexokinase and adenylate kinase activities in aorta, heart muscle and skeletal muscle from uraemic rats.

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The effect of parathyroidectomy and/or vitamin D on the development of arterial and myocardial lesions was studied in rats with moderate uraemia. The activities of hexokinase and adenylate kinase in the aorta, myocardium and skeletal muscle were measured and the incidence of aortic calcification and

Influence of alkaline ionized water on rat erythrocyte hexokinase activity and myocardium.

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Alkaline ionized water (AKW) produced by the electrolysis of tap water (TPW) was given to pregnant rats throughout gestation. AKW was subsequently given to infants as a test group until 15 weeks old to determine changes in body and organ weights, erythrocyte hexokinase (HK) activity and histological

Local toxicity of hepatic arterial infusion of hexokinase II inhibitor, 3-bromopyruvate: In vivo investigation in normal rabbit model.

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OBJECTIVE 3-Bromopyruvate (3-BrPA), an hexokinase II inhibitor, is known to have high necrotic rate in hyperglycolytic liver tumor models without apparent damage to the normal liver parenchyma. The toxicity of intra-arterial delivery of 3-BrPA in various concentrations has not been specifically

No relationship between 18F-fluorodeoxyglucose positron emission tomography and expression of Glut-1 and -3 and hexokinase I and II in high-grade glioma.

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The purpose of this study was to compare glucose metabolism, measured using 18F-fluorodeoxyglucose positron emission tomography ([18F]FDG-PET), with the expression of Glut-1 and -3 and hexokinase I (Hex I) and II in high-grade glioma. The retrospective study involved 27 patients with WHO

[Activity of the key glycolysis enzymes of the heart during emotional stress and myocardial necrosis induced after exposure to stress].

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Activities of hexokinase, phosphofructokinase and pyruvate kinase were studied in rat heart after emotional-painful stress and development of myocardium necrosis. The stress caused an activation of hexokinase and phosphofructokinase within 2 and 7 days, activity of pyruvate kinase was not altered.

[Activity of key enzymes of glycolysis in the rat liver during the development of experimental myocardial necrosis].

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Hexokinase, glucokinase, and phosphofructokinase activity in supernatant hepatic fluid obtained by centrifugation of the homogenate at 20,000 g for 20 minutes was studied during the development of experimental necrosis of the heart muscle. The activity of these enzymes was lowest in the 12th and

Effects of tumour necrosis factor-alpha on the enzymatic activities related to glucose metabolism.

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The effects of an intravenous administration of a single dose (100 micrograms/kg bw) of tumour necrosis factor-alpha (TNF, cachectin) on in vivo glucose oxidation and on several enzymatic activities related with glucose metabolism both in rat liver and skeletal muscle were studied. The treatment

Bcl-2 inhibits tumor necrosis factor-alpha-mediated increase of glycolytic enzyme activities and enhances pyruvate carboxylase activity.

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To understand the effects of bcl-2 on glucose metabolism and tumor necrosis factor-alpha (TNF-alpha) mediated cytotoxicity, the activities of glycolytic enzymes (hexokinase, 6-phosphofructo-1-kinase, and pyruvate kinase), lactate dehydrogenase, pyruvate carboxylase, and phosphoenolpyruvate

A functional RNAi screen identifies hexokinase 1 as a modifier of type II apoptosis.

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Tumor necrosis factor alpha (TNF-alpha) signals through NF-kappaB, JNK, and caspase modules to drive physiological responses that range from inflammation to apoptosis. The balance between the individual modules determines the nature of the response, and deregulated TNF signaling has been implicated

Metabolic effects of tumour necrosis factor-alpha on rat brown adipose tissue.

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Intravenous administration of a single dose (100 micrograms/kg bw) of recombinant tumour necrosis factor-alpha (TNF, cachectin) to rats increased the rate of in vitro fatty acid synthesis in interscapular brown adipose tissue (IBAT) from both glucose and alanine, without changes in the oxidation of

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