Regulation of insulin release by factors that also modify glutamate dehydrogenase.

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Regulation of insulin release by factors that also modify glutamate dehydrogenase.

Leucine and monomethyl succinate initiate insulin release, and glutamine potentiates leucine-induced insulin release. Alanine enhances and malate inhibits leucine plus glutamine-induced insulin release. The insulinotropic effect of leucine is at least in part secondary to its ability to activate glutamate oxidation by glutamate dehydrogenase (Sener, A., Malaisse-Lagae, F., and Malaisse, W. J. (...

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Regulation of Bovine Glutamate Dehydrogenase

The activity of bovine liver glutamate dehydrogenase is affected in several ways depending on substrate concentrations and pH. At pH 6.5 and below, both oxidative deamination and reductive amination reactions are inhibited by ADP. At pH 7.0 and above both activatory and inhibitory effects can be observed depending on substrate concentrations. The effects are explicable in terms of a model with ...

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Evaluation of Glutamate Dehydrogenase Activity and Insulin Secretion in Mice Exposed to Dexamethasone

Background and Aims: Diabetes is one of the most important endocrine disrupters and is associated with various hormones, including those that can lead to diabetes. Glucocorticoid use may lead to insulin resistance. Dexamethasone is one of these glucocorticoid compounds. Glutamate dehydrogenase plays a key role in the production of glutamate in the secretion of insulin. Based on these hormonal i...

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Green tea polyphenols modulate insulin secretion by inhibiting glutamate dehydrogenase.

Insulin secretion by pancreatic beta-cells is stimulated by glucose, amino acids, and other metabolic fuels. Glutamate dehydrogenase (GDH) has been shown to play a regulatory role in this process. The importance of GDH was underscored by features of hyperinsulinemia/hyperammonemia syndrome, where a dominant mutation causes the loss of inhibition by GTP and ATP. Here we report the effects of gre...

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Regulation of glutamate dehydrogenase in Bacillus subtilis.

The activity of the nicotinamide adenine dinucleotide-dependent glutamate dehydrogenase in Bacillus subtilis was influenced by the carbon source, but not the nitrogen source, in the growth medium. The highest specific activity for this enzyme was found when B. subtilis was grown in a minimal or rich medium that contained glutamate as the carbon source. It is proposed that glutamate dehydrogenas...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1988

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)68285-7