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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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Journal ArticleDOI
TL;DR: Data indicate that L-arginine is the physiological precursor for the formation of NO which mediates endothelium-dependent relaxation.

1,405 citations

Journal ArticleDOI
TL;DR: The unexpected discovery of pentose-mediated protein cross-linking raises new questions concerning the aging process and suggests ribose or ribonucleotide metabolites as precursors.

1,090 citations

Journal ArticleDOI
TL;DR: It is demonstrated that the guanidine headgroup of arginine was the critical structural component responsible for the biological activity, indicating that the process was energy dependent, but did not involve endocytosis.
Abstract: Homopolymers or peptides containing a high percentage of cationic amino acids have been shown to have a unique ability to cross the plasma membrane of cells, and consequently have been used to facilitate the uptake of a variety of biopolymers and small molecules. To investigate whether the polycationic character of these molecules, or some other structural feature, was the molecular basis for the effect, the ability of a variety of homopolymers to enter cells was assayed by confocal microscopy and flow cytometry. Polymers of L- or D-arginine containing six or more amino acids entered cells far more effectively than polymers of equal length composed of lysine, ornithine and histidine. Peptides of fewer than six amino acids were ineffective. The length of the arginine side-chain could be varied without significant loss of activity. These data combined with the inability of polymers of citrulline to enter cells demonstrated that the guanidine headgroup of arginine was the critical structural component responsible for the biological activity. Cellular uptake could be inhibited by preincubation of the cells with sodium azide, but not by low temperature (3 degrees C), indicating that the process was energy dependent, but did not involve endocytosis.

1,083 citations

Journal ArticleDOI
TL;DR: Endothelin is released from the intimal layer of intact blood vessels, both under basal conditions and after stimulation withThrombin and the calcium ionophore A23187, and endothelium-derived nitric oxide released during stimulation with thrombin inhibits the production of the peptide via a cyclic GMP-dependent pathway.
Abstract: This study was designed to examine whether endothelin is released from the intima of intact arteries, and whether endothelium-derived nitric oxide regulates its production. Endothelin was detected in the incubating medium of unstimulated pig aortae with, but not in those without endothelium. In preparations with endothelium, thrombin (2-6 U/ml) and the calcium ionophore A23187 (10(-6) M) stimulated the release of the peptide. The basal and thrombin-stimulated production of endothelin were prevented by the protein synthetase inhibitor cycloheximide (10(-6) M). The production of endothelin upon stimulation with thrombin (4 U/ml) was potentiated by L-NG-monomethyl arginine and methylene blue and reduced by superoxide dismutase and 8-bromo cyclic guanosine 5'-monophosphate (GMP), while the basal release of the peptide was unaffected. Thus, (a) endothelin is released from the intimal layer of intact blood vessels, both under basal conditions and after stimulation with thrombin and the calcium ionophore A23187, and (b) endothelium-derived nitric oxide released during stimulation with thrombin inhibits the production of the peptide via a cyclic GMP-dependent pathway.

1,078 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023492
2022765
2021351
2020381
2019332
2018357