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首页> 外文期刊>The Journal of Nutritional Biochemistry >Regulation of protein turnover by l-glutamine in porcine intestinal epithelial cells.
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Regulation of protein turnover by l-glutamine in porcine intestinal epithelial cells.

机译：猪肠上皮细胞中谷氨酰胺对蛋白质更新的调节。

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摘要

L-Glutamine (Gln) plays an important role in sustaining the intestinal mucosal mass of humans and animals. However, the underlying mechanisms are largely unknown. This study tested the hypothesis that Gln regulates protein turnover in intestinal epithelial cells. Intestinal porcine epithelial cells (IPEC-1) were cultured for 3 h (short-term study) or 96 h (long-term study) in Gln-free Dulbecco's modified Eagle-F12 Ham medium containing 0, 0.5 or 2.0 mM Gln. To determine effects of ammonia (a metabolite of Gln, i.e., 0.18 mM ammonia produced from 2 mM Gln in 3 h) on protein turnover, additional experiments were conducted in which medium contained 0.5 mM Gln and 0, 0.2, 0.5 or 2.0 mM NH4Cl. Variables of analysis included cell growth, protein synthesis, proteolysis and mammalian target of rapamycin (mTOR) signaling. IPEC-1 cell growth increased with extracellular Gln concentrations. Compared with 0 mM Gln, the addition of 0.5 and 2 mM Gln to medium stimulated protein synthesis and inhibited protein degradation in those cells in both the short- and long-term studies. Ammonia (0.05 to 2.0 mM) did not affect protein synthesis, although higher levels of ammonia (0.5 and 2.0 mM) reduced protein degradation in IPEC-1 cells. Consistent with the data on protein turnover, 0.5 and 2 mM Gln increased abundance of phosphorylated eIF4E-binding protein-1 and phosphorylated S6 kinase-1 proteins. Collectively, these results demonstrate that physiological levels of Gln regulate protein turnover independent of ammonia production in intestinal cells through the mTOR signaling pathway.
机译：L-谷氨酰胺（Gln）在维持人类和动物的肠道粘膜质量中起着重要作用。但是，基本机制尚不清楚。这项研究检验了Gln调节肠上皮细胞蛋白质更新的假设。在不含Gln的Dulbecco改良的Eagle-F12 Ham培养基（含0、0.5或2.0 mM Gln）中，将肠道猪上皮细胞（IPEC-1）培养3 h（短期研究）或96 h（长期研究）。为了确定氨（Gln的代谢产物，即2 mM Gln在3小时内产生的0.18 mM氨）对蛋白质更新的影响，还进行了另外的实验，其中培养基中含有0.5 mM Gln和0、0.2、0.5或2.0 mM NH 4 Cl。分析变量包括细胞生长，蛋白质合成，蛋白水解和雷帕霉素（mTOR）信号转导的哺乳动物靶点。 IPEC-1细胞的生长随细胞外Gln浓度的增加而增加。与0 mM Gln相比，在短期和长期研究中，向培养基中添加0.5和2 mM Gln可以刺激这些细胞的蛋白质合成并抑制蛋白质降解。氨水（0.05至2.0 mM）不会影响蛋白质合成，尽管较高水平的氨水（0.5和2.0 mM）减少了IPEC-1细胞中的蛋白质降解。与蛋白质更新数据一致，0.5和2 mM Gln可增加磷酸化eIF4E结合蛋白1和磷酸化S6激酶1蛋白的丰度。总体而言，这些结果表明，Gln的生理水平通过mTOR信号传导途径独立于肠细胞中氨的产生而调节蛋白质的更新。

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