Glutamine transport by human intestinal basolateral membrane vesicle

Arab, Noushin; Bulus, Nada; Said, Hamid M.; Pietsch, John B.; Abumrad, Naji N.

doi:10.1093/ajcn/51.4.612

Cited by 15 publications

(6 citation statements)

References 14 publications

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“…Both Na+-dependent and Na+-independent carriermediated transport of glutamine has been identified in BBMV from a number of species [11][12][13][14]. Less information is available on amino acid uptake by the basolateral membrane surface [15][16][17]. Mircheff et al [15] and Ghishan et al [16] reported the presence of System L in rat BLMV after describing a Na+independent saturable system with broad substrate specificity.…”

Section: Introductionmentioning

confidence: 99%

Glutamine transport by basolateral plasma-membrane vesicles prepared from rabbit intestine

Wilde

Kilberg

1991

Biochemical Journal

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L-Glutamine, a major energy substrate for intestinal epithelial cells, can be extracted from intraluminal contents across the brush-border membrane and from arterial blood via the basolateral membrane. The purpose of the present study was to characterize glutamine transport by the basolateral membrane of rabbit epithelial cells. Transport of glutamine by isolated basolateral-membrane vesicles was mediated by both Na(+)-dependent and Na(+)-independent carriers. Tests were performed to distinguish glutamine uptake by likely transport agencies, including Systems A, ASC, N, IMINO, NBB, L and asc. The Na(+)-dependent glutamine uptake was strongly inhibited by an excess of 2-(methylamino)isobutyric acid (MeAIB), and glutamine was equally effective in inhibiting MeAIB transport. The reciprocal inhibition analysis, as well as a sensitivity to increased H+ concentration, indicates that Na(+)-dependent glutamine transport across the basolateral membrane is mediated by System A. The saturable Na(+)-independent glutamine transport was markedly inhibited by 2-aminobicyclo-[2,2,1]-heptane-2-carboxylic acid ('BCH') and insensitive to changes in assay pH, suggesting uptake via System L rather than System asc. The presence of a Na(+)-dependent carrier to mediate active transport of glutamine across the basolateral membrane is probably essential to ensure a continuous supply of this vital substrate to the enterocyte in the post-absorptive state.

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Section: Introductionmentioning

confidence: 99%

Glutamine transport by basolateral plasma-membrane vesicles prepared from rabbit intestine

Wilde

Kilberg

1991

Biochemical Journal

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“…The Na + -dependent mechanism has been described as electrogenic, sensitive to alanine, serine, cysteine, histidine and asparagine but insensitive to MeAIB and BCH and does not accept choline, Li + or K + [14,16,25,30,31,39]. Although it has been proposed that this mechanism is system B 0 , system B 0 accepts BCH [23].…”

Section: Glutamine Transport In Small Intestinal Villous and Crypt Cellsmentioning

confidence: 99%

“…Intestinal basolateral membrane vesicles also express Na + -dependent and -independent transport mechanisms [16,40]. The Na + -dependent mechanism is thought to be System A, due to its sensitivity to MeAIB, and the Na + -independent mechanism was identified as system L, mainly because of its sensitivity to BCH.…”

Section: Glutamine Transport In Small Intestinal Villous and Crypt Cellsmentioning

confidence: 99%

Glutamine transport in isolated epithelial intestinal cells. Identification of a Na + -dependent transport mechanism, highly specific for glutamine

Castillo

Sulbaran-Carrasco

Burguillos

2002

Pfl�gers Archiv European Journal of Physiology

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L-glutamine transport was evaluated in isolated cells from the guinea-pig small intestine by measuring [(3)H]- L-glutamine uptake. Villous and crypt cells expressed Na(+)-dependent and Na(+)-independent transport mechanisms. Glutamine transport systems were identified using various amino acids and analogues as inhibitors. In both villous and crypt cells, 2-(methylamino)-isobutyrate (MeAIB), a system A inhibitor, did not inhibit Na(+)-dependent glutamine influx. 2-Aminobicyclo(2,2,1)heptane-2-carboxylate (BCH), a system B(0) and B(0,+) substrate, had no effect on Na(+)-dependent influx. Serine, cysteine and threonine, system ASC inhibitors, reduced Na(+)-dependent influx by 50%. Asparagine, but not histidine, system N inhibitors, reduced Na(+)-dependent glutamine influx by 50%, however the effect of asparagine was not additive to that of threonine. The remaining Na(+)-dependent glutamine influx (50%) was only inhibited by glutamine itself, by Na(+) substitution ( N-methyl-glucamine, K(+), Li(+)) or by external pH reduction. Phenyl-acetyl-glutamine (PAG), a synthetic amino acid analogue, also inhibited this Na(+)-dependent, threonine-insensitive glutamine influx (IC(50) 2.45 mM). The Na(+)-independent uptake was partially inhibited by BCH, a system L inhibitor, and other neutral amino acids, but was not affect by PAG. Our results suggest that glutamine is transported in both villous and crypt cells by the Na(+)-independent system L, by the Na(+)-dependent system ASC and by an as yet undescribed Na(+)-dependent transport mechanism, highly specific for glutamine.

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“…The intestinal cells obtain glutamine through exogenous and endogenous routes. The exogenous glutamine comes from uptake of the amino acid itself or of glutamine‐containing peptides from the intestinal lumen via transporters in their apical brush border membranes [13], and from the bloodstream via their basolateral membranes [14]. The endogenous glutamine arises from conversion of glutamate and ammonia by glutamine synthetase [15].…”

mentioning

confidence: 99%

Differentiation stage‐dependent preferred uptake of basolateral (systemic) glutamine into Caco‐2 cells results in its accumulation in proteins with a role in cell–cell interaction

et al. 2005

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Glutamine has an important function in the small intestine with respect to maintaining the gut epithelial barrier in critically ill patients [1,2]. Several studies performed in different experimental settings reveal that it serves as an important metabolic fuel for enterocytes [3], and as a precursor for nucleotides, amino sugars, proteins and several other molecules such as glutathione [4,5]. In vitro cell culture studies demonstrate that glutamine specifically protects intestinal epithelial cells against apoptosis [6,7], has trophic effects on the intestinal mucosa [8] and prevents tumour necrosis factor (TNF)-alpha induced bacterial translocation [9]. In experimental models of critical illness, glutamine was able to attenuate Glutamine is an essential amino acid for enterocytes, especially in states of critical illness and injury. In several studies it has been speculated that the beneficial effects of glutamine are dependent on the route of supply (luminal or systemic). The aim of this study was to investigate the relevance of both routes of glutamine delivery to in vitro intestinal cells and to explore the molecular basis for proposed beneficial glutamine effects: (a) by determining the relative uptake of radiolabelled glutamine in Caco-2 cells; (b) by assessing the effect of glutamine on the proteome of Caco-2 cells using a 2D gel electrophoresis approach; and (c) by examining glutamine incorporation into cellular proteins using a new mass spectrometry-based method with stable isotope labelled glutamine. Results of this study show that exogenous glutamine is taken up by Caco-2 cells from both the apical and the basolateral side. Basolateral uptake consistently exceeds apical uptake and this phenomenon is more pronounced in 5-day-differentiated cells than in 15-day-differentiated cells. No effect of exogenous glutamine supply on the proteome was detected. However, we demonstrated that exogenous glutamine is incorporated into newly synthesized proteins and this occurred at a faster rate from basolateral glutamine, which is in line with the uptake rates. Interestingly, a large number of rapidly labelled proteins is involved in establishing cell-cell interactions. In this respect, our data may point to a molecular basis for observed beneficial effects of glutamine on intestinal cells and support results from studies with critically ill patients where parenteral glutamine supplementation is preferred over luminal supplementation.Abbreviations CBB, Coomassie brilliant blue; DMEM, Dulbecco's modified Eagle's medium; FBS, fetal bovine serum; IPG, immobilized pH gradient; LI-cadherin, liver-intestine cadherin; PTFE, polytetrafluoroethylene.

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Glutamine transport by human intestinal basolateral membrane vesicle

Cited by 15 publications

References 14 publications

Glutamine transport by basolateral plasma-membrane vesicles prepared from rabbit intestine

Glutamine transport by basolateral plasma-membrane vesicles prepared from rabbit intestine

Glutamine transport in isolated epithelial intestinal cells. Identification of a Na + -dependent transport mechanism, highly specific for glutamine

Differentiation stage‐dependent preferred uptake of basolateral (systemic) glutamine into Caco‐2 cells results in its accumulation in proteins with a role in cell–cell interaction

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