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Macronutrients
Published in Chuong Pham-Huy, Bruno Pham Huy, Food and Lifestyle in Health and Disease, 2022
Chuong Pham-Huy, Bruno Pham Huy
Aspartate or aspartic acid is the precursor to several amino acids such as isoleucine, lysine, methionine, and threonine. It participates in gluconeogenesis and in the urea cycle. It is a neurotransmitter, but its activity is weaker than that of L-glutamate.
Synapses
Published in Nassir H. Sabah, Neuromuscular Fundamentals, 2020
Glutamate is the major excitatory neurotransmitter of the central nervous system. It is the monovalent cation that arises from the loss of an H+ from the terminal carboxyl group of glutamic acid – a non-essential amino acid. Glutamate is chemically related to glutamine. Aspartate, derived mainly from oxaloacetate, is also a major excitatory neurotransmitter.
Pyruvate carboxylase deficiency
Published in William L. Nyhan, Georg F. Hoffmann, Aida I. Al-Aqeel, Bruce A. Barshop, Atlas of Inherited Metabolic Diseases, 2020
William L. Nyhan, Georg F. Hoffmann, Aida I. Al-Aqeel, Bruce A. Barshop
The complex biochemical picture reminiscent of a defect in the urea cycle appears to result from depletion of intracellular oxaloacetate and aspartate [22, 23, 27]. Aspartate is a source of the second nitrogen of urea (Figure 48.1); its deficiency would lead to citrullinemia and hyperammonemia. Aspartate is also involved in the shuttle of reducing equivalents from cytosol to mitochondria [46] by which the NAD+/NADH ratio (nicotinamide adenine dinucleotide/reduced nicotinamide adenine dinucleotide) is very oxidized in the cytosol and reduced in mitochondria; its lack would make the cytosol more reduced and the mitochondria more oxidized, as occurs in this phenotype.
The low glutamate diet improves cognitive functioning in veterans with Gulf War Illness and resting-state EEG potentially predicts response
Published in Nutritional Neuroscience, 2022
Anna E. Kirkland, Michael Baron, John W. VanMeter, James N. Baraniuk, Kathleen F. Holton
The low glutamate diet is a healthy, whole food diet which restricts the intake of excitotoxins, which are amino acids in the diet that can over-excite glutamate receptors (e.g. free forms of glutamate and aspartate). Free forms of glutamate, such as monosodium glutamate (MSG), can be used as food additives to enhance the flavor of food [13]. Free glutamate can also be found in natural sources, like soy sauce, aged cheeses, seaweed, and tomato sauce. Aspartate is also restricted as it is an analog of glutamate. It is found most often in the diet as aspartame (a dipeptide of aspartate and phenylalanine), which is a commonly used artificial sweetener; and aspartate can also be found in hydrolyzed proteins and in gelatin. The low glutamate diet emphasizes consumption of foods which are protective against excitotoxicity and oxidative stress. More details on the low glutamate diet can be found elsewhere [12].
Recent developments in Phos-tag electrophoresis for the analysis of phosphoproteins in proteomics
Published in Expert Review of Proteomics, 2022
There are no reports on the relationship between the number of glutamates and the changes in mobility observed in Phos-tag SDS-PAGE or between the sequence localization of glutamate and the changes in mobility. Glutamate-containing proteins sometimes show a decrease in mobility like phosphorylated proteins do in Phos-tag SDS-PAGE. Aspartate is also an acidic amino acid similar to glutamate and used to mimic phosphorylation in studies on protein phosphorylation. However, there is also no report that the mobility of aspartate-rich proteins was reduced in Phos-tag SDS-PAGE. Furthermore, no study has reported why aspartate does not affect mobility. Therefore, it might be necessary to perform analyses such as phosphoprotein shotgun analysis, phosphoprotein detection using ProQ diamond, or Western blotting using an antibody specific to the phosphorylation sites to confirm whether the change in mobility observed in Phos-tag SDS-PAGE is due to protein phosphorylation or glutamate. In the future, the development of a novel method will be required to easily distinguish between glutamate-containing and phosphorylated proteins.
Common therapeutic advances for Duchenne muscular dystrophy (DMD)
Published in International Journal of Neuroscience, 2021
Arash Salmaninejad, Yousef Jafari Abarghan, Saeed Bozorg Qomi, Hadi Bayat, Meysam Yousefi, Sara Azhdari, Samaneh Talebi, Majid Mojarrad
Taurine (also called 2-aminoethane-sulfonic acid) is an amino acid that contains sulfur but it does not take part in protein synthesis. This amino acid is abundant in mammalian tissue except in liver, where aspartate is most abundant. Taurine is synthesized endogenously in the liver through cysteine sulfonic acid pathway and its intracellular concentration is relying on the presence of taurine transporter (TauT). Endogenous synthesis of taurine among individuals is highly variable. It is shown that skeletal muscles can accumulate the largest amount of taurine in body by TauT. High concentration of taurine is necessary to maintain appropriate calcium level in muscles [209]. It is demonstrated that taurine treatment led to improved strength and restored calcium homeostasis in mdx mice [210]. Based on these findings, taurine plays an important role in skeletal muscles by regulating the function of ion channel, calcium homeostasis and stability of membrane.