Amino acids and gut function

Wang, W. W.; Qiao, Shiyan; Li, D. F.

doi:10.1007/s00726-008-0152-4

Cited by 238 publications

(173 citation statements)

References 54 publications

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“…Glycine, lysine, threonine and glutamate help to maintain intestinal integrity and health [17,18]. Jutuki plant is used to treat stomach infections [19] sample, and it showed low amino acid concentration, some of which are related to bowel function, which somehow may explain the medicinal properties of the plant.…”

Section: Discussionmentioning

confidence: 99%

Determination of Amino Acids in Medicinal Plants from Southern Sonora, Mexico

Moran-Palacio¹,

Tortoledo‐Ortiz²,

Yañez-Farias³

et al. 2014

Trop. J. Pharm Res

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Section: Discussionmentioning

confidence: 99%

Determination of Amino Acids in Medicinal Plants from Southern Sonora, Mexico

Moran-Palacio¹,

Tortoledo‐Ortiz²,

Yañez-Farias³

et al. 2014

Trop. J. Pharm Res

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“…124 Although, their distinct contribution remains to be explored, it is likely that altered activities of L-Arg catabolizing enzyme families, Arg as well as NOS all contribute to the observed intestinal immunopathologies. It therefore can be postulated that Arg activity through conversion of L-Arg into L-Orn enhances intestinal epithelial barrier function, 125 while iNOS activity confers an antiinflammatory state through regulation of energy metabolism. 126 Indeed, iNOS activity dampens inflammation through regulation of myeloid and lymphoid cell activation.…”

Section: Ly6gmentioning

confidence: 99%

Re-thinking the functions of IgA⁺plasma cells

Gommerman

Rojas

Fritz³

2014

Gut Microbes

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“…Although, their distinct contribution remains to be explored, it is likely that altered activities of L-Arg-catabolizing enzyme families, arginase(s), and NOS contribute to the observed immunopathology. It can be postulated that the activity of arginase through conversion of L-Arg into L-Orn enhances epithelial barrier function (29), while NOS activity confers an anti-inflammatory state through regulation of energy metabolism (30).…”

Section: Regulation Of Intestinal Barrier Function and Inflammation Bmentioning

confidence: 99%

Arginine Cools the Inflamed Gut

Fritz

2013

Infect Immun

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Maintenance of immunophysiological homeostasis and regulation of gut barrier function are essential for the defense of the host. Severe alterations, including infections and chronic inflammation, have been associated with increased intestinal permeability, leading to deregulation of gut function and homeostasis. To establish and reinforce this crucial balance, the intestinal metabolism plays a key role and has to be tightly regulated since in the human intestinal mucosa, the protein fractional synthesis rate is approximately 50% per day. This value is higher than that of other major metabolically active tissues, such as liver and muscle, and depends on the accessibility of the metabolic precursor pool (1). The amino acid L-arginine (L-Arg) is a central intestinal metabolite, both as a constituent of protein synthesis and as a regulatory molecule limiting intestinal alterations and maintaining immunophysiological functions (1, 2). Infection-associated L-Arg deficiency has been shown to contribute to immunopathology, and clinical trials involving L-Arg administration have shown substantial decreases in inflammation and infectious complications (3). In this issue, Chau and colleagues demonstrate that malariaassociated hypoargininemia impairs intestinal barrier function and predisposes the host to coinfection with Salmonella. Increasing bioavailability of L-Arg through oral supplementation ameliorates intestinal inflammation and pathology, demonstrating that pharmacological intervention at the metabolic-precursor level can be utilized to regulate mucosal immunohomeostasis (4). METABOLISM AND CATABOLISM OF L-ARGININEL-Arg is derived from the diet, turnover of proteins, and endogenous production through synthesis from L-citrulline (L-Cit) and successive actions of argininosuccinate synthetase (AS) and argininosuccinate lyase (AL), the third and fourth enzymes of the urea cycle. The major site of L-Arg metabolism is the liver, where L-Arg generated in the urea cycle is rapidly converted to urea and ornithine by arginases, however, with no net synthesis of L-Arg. Although synthesis of L-Arg from L-Cit can occur in many cell types, a major part of endogenous synthesis occurs via "the intestinal-renal axis," a postnatally established collaboration between epithelial cells of the small intestine and proximal tubule cells of the kidney. In adult animals, L-Cit is produced primarily by intestinal epithelial cells from NH 3 , CO 2 , and ornithine by carbamylphosphate synthetase I and ornithine transcarbamylase, the first two enzymes of the urea cycle, and is supplied to the kidney and probably to other tissues for synthesis of L-Arg (2,5,6).L-Arg is a crucial amino acid that serves to modulate immune responses through conversion by several intracellular classes of enzymes, with isoforms of arginase and nitric oxide synthase (NOS) being the two major enzyme families exerting key immunological functions (7). However, catabolism of extracellular LArg requires active and regulated uptake via specific cationic amino acid transport...

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Amino acids and gut function

Cited by 238 publications

References 54 publications

Determination of Amino Acids in Medicinal Plants from Southern Sonora, Mexico

Determination of Amino Acids in Medicinal Plants from Southern Sonora, Mexico

Re-thinking the functions of IgA⁺plasma cells

Arginine Cools the Inflamed Gut

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Amino acids and gut function

Cited by 238 publications

References 54 publications

Determination of Amino Acids in Medicinal Plants from Southern Sonora, Mexico

Determination of Amino Acids in Medicinal Plants from Southern Sonora, Mexico

Re-thinking the functions of IgA+plasma cells

Arginine Cools the Inflamed Gut

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Product

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Re-thinking the functions of IgA⁺plasma cells