Topic
Arginine
About: Arginine is a research topic. Over the lifetime, 16677 publications have been published within this topic receiving 579791 citations. The topic is also known as: L-Arg & (2S)-2-amino-5-guanidinopentanoic acid.
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TL;DR: The chapter discusses the physiological importance of protein oxidation, and increases in carbonyl levels are examined in several diseases, such as rheumatoid arthritis, ischemia-reperfusion injury to heart muscles, and muscle damage caused by exhaustive exercise.
Abstract: Publisher Summary Oxygen radicals are implicated as an important cause of oxidative modification of proteins which may lead to their rapid degradation. Among the various oxidative modifications of amino acids in proteins, carbonyl formation may be an early marker for protein oxidation. This type of alteration is characterized as metal-catalyzed oxidation of proteins. The molecular mechanisms of this type of protein oxidation are discussed in this chapter. Redox cycling cations, such as Fe 2+ or Cu 2+ can bind to cation binding locations on proteins and with the aid of further attack by H 2 O 2 or O 2 can transform side-chain amine groups on several amino acids into carbonyls. The most likely amino acid residues to form carbonyl derivatives are lysine, arginine, proline, and histidine. Metal-catalyzed oxidation of proteins is not necessarily the only mechanism by which carbonyls are introduced into proteins. The chapter discusses the physiological importance of protein oxidation. Increases in carbonyl levels are examined in several diseases, such as rheumatoid arthritis, ischemia-reperfusion injury to heart muscles, and muscle damage caused by exhaustive exercise.
2,248 citations
TL;DR: It is established that NO mediates the neurotoxicity of glutamate and Hemoglobin, which complexes NO, prevents neurotoxic effects of both N-methyl-D-aspartate and sodium nitroprusside.
Abstract: Nitric oxide (NO) mediates several biological actions, including relaxation of blood vessels, cytotoxicity of activated macrophages, and formation of cGMP by activation of glutamate receptors in cerebellar slices. Nitric oxide synthase (EC 1.14.23.-) immunoreactivity is colocalized with nicotinamide adenine di-nucleotide phosphate diaphorase in neurons that are uniquely resistant to toxic insults. We show that the nitric oxide synthase inhibitors, N omega-nitro-L-arginine (EC50 = 20 microM) and N omega-monomethyl-L-arginine (EC50 = 170 microM), prevent neurotoxicity elicited by N-methyl-D-aspartate and related excitatory amino acids. This effect is competitively reversed by L-arginine. Depletion of the culture medium of arginine by arginase or arginine-free growth medium completely attenuates N-methyl-D-aspartate toxicity. Sodium nitroprusside, which spontaneously releases NO, produces dose-dependent cell death that parallels cGMP formation. Hemoglobin, which complexes NO, prevents neurotoxic effects of both N-methyl-D-aspartate and sodium nitroprusside. These data establish that NO mediates the neurotoxicity of glutamate.
2,229 citations
TL;DR: Dietary supplementation with one or a mixture of these functional AA, which include arginine, cysteine, glutamine, leucine, proline, and tryptophan, may be beneficial for ameliorating health problems at various stages of the life cycle and optimizing efficiency of metabolic transformations to enhance muscle growth, milk production, egg and meat quality and athletic performance.
Abstract: Recent years have witnessed the discovery that amino acids (AA) are not only cell signaling molecules but are also regulators of gene expression and the protein phosphorylation cascade. Additionally, AA are key precursors for syntheses of hormones and low-molecular weight nitrogenous substances with each having enormous biological importance. Physiological concentrations of AA and their metabolites (e.g., nitric oxide, polyamines, glutathione, taurine, thyroid hormones, and serotonin) are required for the functions. However, elevated levels of AA and their products (e.g., ammonia, homocysteine, and asymmetric dimethylarginine) are pathogenic factors for neurological disorders, oxidative stress, and cardiovascular disease. Thus, an optimal balance among AA in the diet and circulation is crucial for whole body homeostasis. There is growing recognition that besides their role as building blocks of proteins and polypeptides, some AA regulate key metabolic pathways that are necessary for maintenance, growth, reproduction, and immunity. They are called functional AA, which include arginine, cysteine, glutamine, leucine, proline, and tryptophan. Dietary supplementation with one or a mixture of these AA may be beneficial for (1) ameliorating health problems at various stages of the life cycle (e.g., fetal growth restriction, neonatal morbidity and mortality, weaning-associated intestinal dysfunction and wasting syndrome, obesity, diabetes, cardiovascular disease, the metabolic syndrome, and infertility); (2) optimizing efficiency of metabolic transformations to enhance muscle growth, milk production, egg and meat quality and athletic performance, while preventing excess fat deposition and reducing adiposity. Thus, AA have important functions in both nutrition and health.
2,047 citations
TL;DR: It is established that nitric oxide mediates the stimulation by glutamate of cGMP formation, which mediates influences of numerous neurotransmitters and modulators on vascular smooth muscle and leukocytes.
Abstract: Nitric oxide, which mediates influences of numerous neurotransmitters and modulators on vascular smooth muscle and leukocytes, can be formed in the brain from arginine by an enzymatic activity that stoichiometrically generates citrulline. We show that glutamate and related amino acids, such as N-methyl-D-aspartate, markedly stimulate arginine--citrulline transformation in cerebellar slices stoichiometrically with enhancement of cGMP levels. N omega-monomethyl-L-arginine blocks the augmentation both of citrulline and cGMP with identical potencies. Arginine competitively reverses both effects of N omega-monomethyl-L-arginine with the same potencies. Hemoglobin, which complexes nitric oxide, prevents the stimulation by N-methyl-D-aspartate of cGMP levels, and superoxide dismutase, which elevates nitric oxide levels, increases cGMP formation. These data establish that nitric oxide mediates the stimulation by glutamate of cGMP formation.
1,854 citations
TL;DR: Based on the fluorescence microscopic observations of mouse macrophage RAW264.7 cells, it is found that various arginine-rich peptides have a translocation activity very similar to Tat-(48–60), and the results strongly suggested the possible existence of a common internalization mechanism ubiquitous to arkinine- rich peptides.
1,665 citations