Can arginine and ornithine support gut functions?

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Can arginine and ornithine support gut functions?

Arginine and ornithine are precursors of nitric oxide and polyamines, respectively. These metabolites intimately participate in permeability and adaptive responses of the gut. The liver possesses high arginase activity as an intrinsic part of urea synthesis and would consume most of the portal supply of dietary arginine. The gut reduces this possibility by converting dietary arginine to citrull...

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5 Arginine , Citrulline , and Ornithine

Metabolism as well as function of the three amino acids, L-arginine, L-citrulline, and Lornithine, are closely intertwined and related to the homeostasis of nitric oxide at the tissue and cellular levels. For the three compounds data on neural tissue and CSF levels are summarized and localization in brain mainly derived from immunohistochemical experiments is reported. A complex pattern of diff...

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Enzymatic transamination reactions involving arginine and ornithine.

Recent research has resulted in considerable modification of the earlier concept that enzymatic transamination was limited to reactions between alanine, aspartate, glutamate, and their or-keto analogues. Reactions leading to the reversible amination of the cY-keto analogues of many of the natural amino acids have been described (l-5), and there is also evidence that aldehyde groups may particip...

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Delayed separation and the plasma amino acids arginine and ornithine.

When collecting blood for amino acid testing, leaving plasma in contact with cells at room temperature lowers the concentration of arginine and raises that of ornithine. This is presumably due to the arginase content of red blood cells. In contrast, the sum of arginine and ornithine is constant over the first hour, and defines a reference interval of 74-148 mumol/L (mean +/- 2 SD, n = 20) which...

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Mouse ornithine decarboxylase-like gene encodes an antizyme inhibitor devoid of ornithine and arginine decarboxylating activity.

Ornithine decarboxylase (ODC), a key enzyme in the biosynthesis of polyamines, is a labile protein that is regulated by interacting with antizymes (AZs), a family of polyamine-induced proteins. Recently, a novel human gene highly homologous to ODC, termed ODC-like or ODC-paralogue (ODCp), was cloned, but the studies aimed to determine its function rendered contradictory results. We have cloned ...

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ژورنال

عنوان ژورنال: Gut

سال: 1994

ISSN: 0017-5749

DOI: 10.1136/gut.35.1_suppl.s42