Polyamine metabolism in enterocytes isolated from newborn pigs

Blachier, François; M'Rabet-Touil, Hamida; Posho, Leta; Morel, Marie-Thérèse; Bernard, Françoise; Darcy‐Vrillon, Béatrice; Duée, Pierre‐Henri

doi:10.1016/0167-4889(92)90005-v

Cited by 45 publications

(16 citation statements)

References 25 publications

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“…The fact that the basal production of L-ornithine from L-arginine was similar to the production of urea at all stages of development that were studied indicates that L-ornithine metabolism is limited in enterocytes. This is in agreement with the reported low production of polyamines from L-arginine in newborn pig enterocytes [15] and low oxidative catabolism in rat enterocytes [ 2 ] . In the present study, the production of 14C0, from radioactive L-arginine was negligible compared to I4CO, production from L-glutamine [29] at all stages of development, indicating that the increased catabolism of L-arginine into L-ornithine during development is not accompanied by an increased oxidation of the amino acid.…”

Section: Discussionsupporting

confidence: 82%

“…Since a constant amount of L-arginine from L-ornithine or L-citrulline was produced during the first two days after birth and since L-glutamine was utilized in similar amounts [29], it is likely that the step between L-glutamate and L-ornithine was affected in L-glutamine metabolism between birth and 2 days of age. Indeed, in enterocytes isolated from pigs at birth, exogenous L-glutamine produces a low but measurable net amount of L-ornithine [15] confirming that this pathway is operative in these cells. Moreover this production of L-ornithine is decreased in enterocytes from 2-day-old suckling pigs [ 151.…”

Section: Discussionmentioning

confidence: 76%

“…These spaces were determined by centrifugation through an oil layer after incubation of enterocytes for 10 rnin at 37°C in the presence of 2 m M ~-[l-'~C]glucose or 0.5 pM ['Hlinulin as recently described [15].…”

Section: Measurement Of Intracellular Volume Of Enterocytesmentioning

confidence: 99%

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Intestinal arginine metabolism during development

Blachier

M'Rabet-Touil

Posho

et al. 1993

European Journal of Biochemistry

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The capacity for L-arginine metabolism was studied in villus enterocytes isolated from pigs at birth, after 2-8 days suckling and after weaning. Immediately after birth, enterocytes were able to convert 1 mM L-citrulline, 2 mM ~-glutamine or 1 mM L-ornithine to L-arginine. In 2-8-day-old animals, the net production of L-arginine from L-citrulline (2.00 f 0.45 nmol . lo6 cells-' . 30 min-'), or from L-ornithine (0.29 -+ 0.06 nmol . 10' cells-' . 30 min-') was similar to the values obtained at birth. Furthermore, 40% of L-arginine synthetized de novo from L-citrulline were released into the incubation medium. In 2 -8-day-old animals, the production of L-arginine from L-glutamine represented only 5% of the production at birth (the latter being 0.73 f 0.15 nmol . lo6 cells-' . 30 min-').In enterocytes isolated from post-weaned pigs, no significant production of L-arginine from either L-glutamine or L-ornithine was detected. In contrast, although the L-arginine production from Lcitrulline was very low in post-weaned animals, it was significantly enhanced in the presence of Lglutamine, representing 23% of the production measured in suckling animals. The capacity of enterocytes to cleave L-arginine to L-ornithine and urea was very limited at birth, but was increased more than threefold in 2-day-old animals. This was concomitant with a marked increase in arginase activity. In post-weaned animals, the flux through arginase in intact enterocytes, and the arginase activity were both threefold higher than in 2 -8-day-old animals. It is concluded that enterocytes isolated from neonatal pigs exhibit the capacity for a net production of L-arginine since the metabolism of this amino acid is oriented to anabolism rather than catabolism. The results are discussed in relation to L-arginine metabolism in the neonatal liver.Apart from their well-identified function of nutrient translocation, including that of amino acids, from the intestinal lumen to the bloodstream, enterocytes are able to partially metabolize these amino acids during their transcellular journey. L-Glutamine is highly utilized by intestinal absorptive cells where it plays the role of a respiratory fuel [l]. In contrast, the oxidative catabolism of L-arginine in enterocytes is negligible relative to its conversion to L-ornithine and L-citrulline [2]. The adult intestine intensively degrades absorbed L-arginine resulting in a high L-ornithine, urea and L-citrulline release into blood [3]. Intestinal arginase cleaves L-arginine into L-ornithine and urea, and L-ornithine is considered as an important contributor to urea synthesis from excess ammonia in liver [4-61. Further metabolism of L-ornithine in adult intestine is limited to L-citrulline generation since a complete urea cycle does not operate in adult intestinal mucosa (71, the two enzymes responsible for the conversion of L-citrulline to L-arginine [argininosuccinate

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Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 76%

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Intestinal arginine metabolism during development

Blachier

M'Rabet-Touil

Posho

et al. 1993

European Journal of Biochemistry

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“…There is also evidence for a link between arginase activity and polyamine synthesis in the small intestine. The synthesis of polyamines from arginine is negligible in enterocytes of newborn and suckling animals [245,246], due, at least in part, to low arginase activity. Polyamine synthesis increases in enterocytes of post-weaning animals, concurrent with the induction of both arginase and ODC [193].…”

Section: Figure 6 Developmental Changes In Arginine Catabolism By Pigmentioning

confidence: 99%

Arginine metabolism: nitric oxide and beyond

Morris

1998

Biochemical Journal

2,452

2,036

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Arginine is one of the most versatile amino acids in animal cells, serving as a precursor for the synthesis not only of proteins but also of nitric oxide, urea, polyamines, proline, glutamate, creatine and agmatine. Of the enzymes that catalyse rate-controlling steps in arginine synthesis and catabolism, argininosuccinate synthase, the two arginase isoenzymes, the three nitric oxide synthase isoenzymes and arginine decarboxylase have been recognized in recent years as key factors in regulating newly identified aspects of arginine metabolism. In particular, changes in the activities of argininosuccinate synthase, the arginases, the inducible isoenzyme of nitric oxide synthase and also cationic amino acid transporters play major roles in determining the metabolic fates of arginine in health and disease, and recent studies have identified

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“…Indeed, during the high-rate postnatal growth of the pig intestinal mucosa, villus-crypt enterocytes (i.e. undifferentiated dividing stem cells of the enterocyte cell lineage) showed a very low ODC activity (Blachier et al 1992). In agreement with this observation, orally fed radiolabelled putrescine is accumulated and further metabolised to spermidine in normal growing pancreas, liver and small intestine of rat pups (L oser et al 1997).…”

Section: Discussionmentioning

confidence: 99%

Pancreatic Exocrine Secretions as a Source of Luminal Polyamines in Pigs

Loret

Brolet

Pierzynowski

et al. 2000

Experimental Physiology

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The goal of the present study was twofold: (1) to detect the possible storage of dietary polyamines (PAs) in various tissues and (2) to investigate the role of dietary PAs in the differentiation of the pig intestinal epithelium. A first experimental series was designed to assess the accumulation of either milk PAs (mostly spermidine) or orally administered spermine (SPM) in piglet red blood cells (RBCs) and plasma, a preliminary stage in their distribution to growing and storage organs. Though PA concentrations of piglet RBCs and plasma were generally significantly higher than their sow counterparts, our experimental conditions failed to demonstrate that this increase could stem from ingested PAs. A second experimental series dealt with the determination of disaccharidase specific activities in proximal and distal parts of piglet gut on the 26th and 29th days after birth (preweaning time). In agreement with observations made previously on rat pups, we observed an increase in maltase specific activity (SA) at the end of the suckling period (the observed increase in sucrase SA was not significant). However, orally administered SPM did not affect this activity. Compared to the constant protein concentrations observed in both parts of the gut, the pancreatic protein content decreased sharply between the 26th and 29th postnatal days. At the same time pancreatic concentrations of spermidine (SPD) also decreased, suggesting that some pancreatic PAs were released as the organ secreted its proteins. In accordance with this hypothesis, we recorded SPM and SPD in pancreatic juice. The increases in PA concentrations seemed to follow the protein secretion pattern (i.e. PA concentrations reached a maximal value when the protein concentration was highest). The presence of PAs in pancreatic juice could be indicative of a control mechanism exerted by the pancreas on PA‐induced growth and differentiation of porcine intestinal epithelium.

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Polyamine metabolism in enterocytes isolated from newborn pigs

Cited by 45 publications

References 25 publications

Intestinal arginine metabolism during development

Intestinal arginine metabolism during development

Arginine metabolism: nitric oxide and beyond

Pancreatic Exocrine Secretions as a Source of Luminal Polyamines in Pigs

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