The Experts below are selected from a list of 231 Experts worldwide ranked by ideXlab platform
Dany Muller - One of the best experts on this subject based on the ideXlab platform.
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Calcium/calmodulin-dependent kinase IV controls glucose-induced Irs2 expression in mouse beta cells via activation of cAMP response element-binding protein
Diabetologia, 2011Co-Authors: Shanta J. Persaud, Bo Liu, H. Barbosa Sampaio, Peter M. Jones, Dany MullerAbstract:Aims/hypothesis Irs2, which is upregulated by glucose, is important for beta cell plasticity. Cyclic AMP response element-binding protein (CREB) stimulates beta cell Irs2 expression and is a major calcium/calmodulin-dependent kinase (CaMK)IV target in neurons. We therefore hypothesised that CaMKIV mediates glucose-induced Irs2 expression in beta cells via CREB activation.
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calcium calmodulin dependent kinase iv controls glucose induced irs2 expression in mouse beta cells via activation of camp response element binding protein
Diabetologia, 2011Co-Authors: Shanta J. Persaud, Bo Liu, Peter M. Jones, Barbosa H Sampaio, Dany MullerAbstract:Aims/hypothesis Irs2, which is upregulated by glucose, is important for beta cell plasticity. Cyclic AMP response element-binding protein (CREB) stimulates beta cell Irs2 expression and is a major calcium/calmodulin-dependent kinase (CaMK)IV target in neurons. We therefore hypothesised that CaMKIV mediates glucose-induced Irs2 expression in beta cells via CREB activation.
Willy Malaisse - One of the best experts on this subject based on the ideXlab platform.
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Dissimilar effects of D-mannoheptulose on the phosphorylation of α- versus β-D-glucose by either hexokinase or glucokinase
International journal of molecular medicine, 2004Co-Authors: Ying Zhang, Philippe Courtois, Abdullah Sener, Willy MalaisseAbstract:D-mannoheptulose inhibits D-glucose phosphorylation by hexokinase isoenzymes. The present study aims at investigating whether the pattern of such an inhibition differs in the case of alpha- versus Beta-D-Glucose. The phosphorylation of alpha- and beta-D-[U-14C]glucose was measured over 60-min incubation at 4 degrees C in the presence of bovine heart hexokinase and over 10 min at 24 degrees C in the presence of human liver glucokinase. The relative extent of the inhibitory action of D-mannoheptulose (0.02-10.0 mM) was always less marked with alpha- than Beta-D-Glucose. In the case of hexokinase, the experiments conducted at the high concentration of the D-glucose anomers (1.0 mM) revealed that D-mannoheptulose, at low concentrations (0.2-0.5 mM), may unexpectedly increase the phosphorylation of alpha-D-glucose. These findings thus document anomeric specificity in terms of the inhibitory action of D-mannoheptulose upon alpha- versus Beta-D-Glucose phosphorylation by either hexokinase or glucokinase.
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Metabolism of D-glucose anomers in rat pancreatic islets exposed to equilibrated D-glucose.
Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et metabolisme, 2004Co-Authors: Willy Malaisse, Ying Zhang, Hassan Jijakli, Philippe Courtois, Abdullah SenerAbstract:This study aims at establishing the contribution of alpha- and Beta-D-Glucose to the total generation of (3)HOH by rat pancreatic islets exposed to D-[2 - (3)H]glucose or D-[5 - (3)H] glucose at anomeric equilibrium. The islets were incubated for 60 min at 4 degrees C in the presence of equilibrated D-glucose (2.8 and 8.3 mM) mixed with tracer amounts of either alpha- or Beta-D-Glucose labelled with tritium on either the C (2) or C (5) of the hexose. Relative to their respective concentrations, (3)HOH generation from the anomers labelled with tritium on the C (2) or C (5) of the hexose provided beta/alpha ratios comparable to those previously found at both 2.8 and 8.3 mM, when the islets were exposed to each anomer separately. The relative contributions of each anomer to the total generation of (3)HOH was also close to the theoretical values derived from mathematical models for the catabolism of D-glucose at anomeric equilibrium in rat islets at both 2.8 and 8.3 mM and in the case of both D-[2 - (3)H]glucose and D-[5 - (3)H]glucose. Thus, even in islets exposed to D-glucose at anomeric equilibrium, the metabolic fate of alpha-D-glucose differs vastly from that of Beta-D-Glucose, the enzyme-to-enzyme channelling between hexokinase isoenzymes, especially glucokinase, and phosphoglucoisomerase being restricted to alpha-D-glucose 6-phosphate.
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Metabolism of tritiated D-glucose anomers in rat erythrocytes.
Molecular and cellular biochemistry, 2004Co-Authors: Ying Zhang, Hassan Jijakli, Philippe Courtois, Abdullah Sener, Willy MalaisseAbstract:It was recently proposed that alpha-D-glucose 6-phosphate may undergo enzyme-to-enzyme channelling between glucokinase and phosphoglucoisomerase in rat pancreatic islets. The present study aims at exploring whether a different situation prevails in cells deprived of glucokinase, namely in erythrocytes. At anomeric equilibrium, the ratio between D-[2-3H]glucose and D-[5-3H]glucose conversion to 3HOH was lower in rat erythrocytes incubated for 60 min at 4 degrees C in the presence of 2.8 mM, rather than 8.3 mM, D-glucose. This coincided with both a greater relative increase in beta-D-[5-3H]glucose, as compared to alpha-D-[5-3H]glucose, conversion to 3HOH and an increase in the beta/alpha ratio for 3HOH generation from D-[5-3H]glucose in response to an increase in the anomeric concentration from 2.8 to 8.3 mM, the suppression of the difference between the beta/alpha ratios for 3HOH generation from D-[2-3H]glucose and D-[5-3H]glucose in the erythrocytes incubated at 8.3 mM, as distinct from 2.8 mM, alpha- and Beta-D-Glucose, and a [2-3H]/[5-3H] ratio for 3HOH generation lower than unity in erythrocytes exposed to alpha-D-glucose but not significantly different from unity in the presence of Beta-D-Glucose. These findings emphasize the relevance of alpha-D-glucose 6-phosphate channelling between hexokinase and phosphoglucoisomerase as a determinant of the difference between D-[2-3H]glucose and D-[5-3H]glucose conversion to 3HOH, and reveal that the regulation of such a tunnelling process by the concentration of the D-glucose represents, in rat erythrocytes, a mirror image of that observed in rat pancreatic islets. The regulation of this process thus tightly depends on the identity of the hexokinase enzyme mainly responsible for the phosphorylation of D-glucose in distinct cell types.
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Metabolism of tritiated D-glucose anomers in rat erythrocytes
Molecular and Cellular Biochemistry, 2004Co-Authors: Ying Zhang, Hassan Jijakli, Philippe Courtois, Abdullah Sener, Willy MalaisseAbstract:It was recently proposed that alpha-D-glucose 6-phosphate may undergo enzyme-to-enzyme channelling between glucokinase and phosphoglucoisomerase in rat pancreatic islets. The present study aims at exploring whether a different situation prevails in cells deprived of glucokinase, namely in erythrocytes. At anomeric equilibrium, the ratio between D-[2-3H]glucose and D-[5-3H]glucose conversion to 3HOH was lower in rat erythrocytes incubated for 60 min at 4 degrees C in the presence of 2.8 mM, rather than 8.3 mM, D-glucose. This coincided with both a greater relative increase in beta-D-[5-3H]glucose, as compared to alpha-D-[5-3H]glucose, conversion to 3HOH and an increase in the beta/alpha ratio for 3HOH generation from D-[5-3H]glucose in response to an increase in the anomeric concentration from 2.8 to 8.3 mM, the suppression of the difference between the beta/alpha ratios for 3HOH generation from D-[2-3H]glucose and D-[5-3H]glucose in the erythrocytes incubated at 8.3 mM, as distinct from 2.8 mM, alpha- and Beta-D-Glucose, and a [2-3H]/[5-3H] ratio for 3HOH generation lower than unity in erythrocytes exposed to alpha-D-glucose but not significantly different from unity in the presence of Beta-D-Glucose. These findings emphasize the relevance of alpha-D-glucose 6-phosphate channelling between hexokinase and phosphoglucoisomerase as a determinant of the difference between D-[2-3H]glucose and D-[5-3H]glucose conversion to 3HOH, and reveal that the regulation of such a tunnelling process by the concentration of the D-glucose represents, in rat erythrocytes, a mirror image of that observed in rat pancreatic islets. The regulation of this process thus tightly depends on the identity of the hexokinase enzyme mainly responsible for the phosphorylation of D-glucose in distinct cell types.Journal ArticleResearch Support, Non-U.S. Gov'tinfo:eu-repo/semantics/publishe
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Modulation by D-glucose anomers of the effect of D-fructose upon 45Ca efflux from prelabelled rat pancreatic islets.
International journal of molecular medicine, 2003Co-Authors: Hassan Jijakli, Abdullah Sener, Hai-xia Zhang, Willy MalaisseAbstract:It was recently reported that alpha-D-glucose is more potent than Beta-D-Glucose in conferring to glucokinase positive cooperativity towards D-fructose. We have now extended pilot experiments to investigate whether a comparable situation prevails in intact rat pancreatic islets in terms of the modulation by the D-glucose anomers of the effect of D-fructose upon 45Ca efflux from prelabelled perifused islets. As expected from the effect of increasing concentrations of equilibrated D-glucose upon 45Ca efflux from the prelabelled islets, D-fructose either decreased or increased 45Ca outflow from islets perifused in the presence of either alpha- or Beta-D-Glucose. In all cases, the alpha-anomer of D-glucose affected more markedly than Beta-D-Glucose the cationic response to D-fructose. These findings indicate that the anomeric specificity of the effect of D-glucose upon D-fructose phosphorylation by glucokinase is also operative in intact islets.
Shanta J. Persaud - One of the best experts on this subject based on the ideXlab platform.
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Calcium/calmodulin-dependent kinase IV controls glucose-induced Irs2 expression in mouse beta cells via activation of cAMP response element-binding protein
Diabetologia, 2011Co-Authors: Shanta J. Persaud, Bo Liu, H. Barbosa Sampaio, Peter M. Jones, Dany MullerAbstract:Aims/hypothesis Irs2, which is upregulated by glucose, is important for beta cell plasticity. Cyclic AMP response element-binding protein (CREB) stimulates beta cell Irs2 expression and is a major calcium/calmodulin-dependent kinase (CaMK)IV target in neurons. We therefore hypothesised that CaMKIV mediates glucose-induced Irs2 expression in beta cells via CREB activation.
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calcium calmodulin dependent kinase iv controls glucose induced irs2 expression in mouse beta cells via activation of camp response element binding protein
Diabetologia, 2011Co-Authors: Shanta J. Persaud, Bo Liu, Peter M. Jones, Barbosa H Sampaio, Dany MullerAbstract:Aims/hypothesis Irs2, which is upregulated by glucose, is important for beta cell plasticity. Cyclic AMP response element-binding protein (CREB) stimulates beta cell Irs2 expression and is a major calcium/calmodulin-dependent kinase (CaMK)IV target in neurons. We therefore hypothesised that CaMKIV mediates glucose-induced Irs2 expression in beta cells via CREB activation.
Bo Liu - One of the best experts on this subject based on the ideXlab platform.
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Calcium/calmodulin-dependent kinase IV controls glucose-induced Irs2 expression in mouse beta cells via activation of cAMP response element-binding protein
Diabetologia, 2011Co-Authors: Shanta J. Persaud, Bo Liu, H. Barbosa Sampaio, Peter M. Jones, Dany MullerAbstract:Aims/hypothesis Irs2, which is upregulated by glucose, is important for beta cell plasticity. Cyclic AMP response element-binding protein (CREB) stimulates beta cell Irs2 expression and is a major calcium/calmodulin-dependent kinase (CaMK)IV target in neurons. We therefore hypothesised that CaMKIV mediates glucose-induced Irs2 expression in beta cells via CREB activation.
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calcium calmodulin dependent kinase iv controls glucose induced irs2 expression in mouse beta cells via activation of camp response element binding protein
Diabetologia, 2011Co-Authors: Shanta J. Persaud, Bo Liu, Peter M. Jones, Barbosa H Sampaio, Dany MullerAbstract:Aims/hypothesis Irs2, which is upregulated by glucose, is important for beta cell plasticity. Cyclic AMP response element-binding protein (CREB) stimulates beta cell Irs2 expression and is a major calcium/calmodulin-dependent kinase (CaMK)IV target in neurons. We therefore hypothesised that CaMKIV mediates glucose-induced Irs2 expression in beta cells via CREB activation.
Peter M. Jones - One of the best experts on this subject based on the ideXlab platform.
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Calcium/calmodulin-dependent kinase IV controls glucose-induced Irs2 expression in mouse beta cells via activation of cAMP response element-binding protein
Diabetologia, 2011Co-Authors: Shanta J. Persaud, Bo Liu, H. Barbosa Sampaio, Peter M. Jones, Dany MullerAbstract:Aims/hypothesis Irs2, which is upregulated by glucose, is important for beta cell plasticity. Cyclic AMP response element-binding protein (CREB) stimulates beta cell Irs2 expression and is a major calcium/calmodulin-dependent kinase (CaMK)IV target in neurons. We therefore hypothesised that CaMKIV mediates glucose-induced Irs2 expression in beta cells via CREB activation.
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calcium calmodulin dependent kinase iv controls glucose induced irs2 expression in mouse beta cells via activation of camp response element binding protein
Diabetologia, 2011Co-Authors: Shanta J. Persaud, Bo Liu, Peter M. Jones, Barbosa H Sampaio, Dany MullerAbstract:Aims/hypothesis Irs2, which is upregulated by glucose, is important for beta cell plasticity. Cyclic AMP response element-binding protein (CREB) stimulates beta cell Irs2 expression and is a major calcium/calmodulin-dependent kinase (CaMK)IV target in neurons. We therefore hypothesised that CaMKIV mediates glucose-induced Irs2 expression in beta cells via CREB activation.