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首页> 外文期刊>Journal of Cellular Physiology >Link between high-affinity adenosine concentrative nucleoside transporter-2 (CNT2) and energy metabolism in intestinal and liver parenchymal cells.
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Link between high-affinity adenosine concentrative nucleoside transporter-2 (CNT2) and energy metabolism in intestinal and liver parenchymal cells.

机译：高亲和性腺苷集中之间的联系核苷transporter-2 (CNT2)和能量代谢在肠道和肝实质细胞。

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摘要

Concentrative nucleoside transporter 2 (CNT2) is a high-affinity adenosine transporter that may play physiological roles beyond nucleoside salvage. Previous reports relate CNT2 function to modulation of purinergic signaling and energy metabolism in intestinal and liver parenchymal cells (Duflot et al., 2004, Mol Cell Biol 24:2710-2719; Aymerich et al., 2006, J Cell Sci 119:1612-1621). In the present study, to further examine the link between CNT2 and energy metabolism, CNT2 protein partners were identified using the bacterial two-hybrid and GST pull-down approaches. The N-terminal segment of CNT2 was used as bait, since proteins lacking this domain display impaired plasma membrane insertion and intracellular retention. Glucose-regulated protein 58 (GRP58) was identified as a potential rCNT2 partner in pull-down experiments. Two-hybrid screening performed against a liver human cDNA library led to the identification of aldolase B as another hCNT2 partner. Aldolase B-RFP and endogenous GRP58 separately co-localized with CNT2 in HeLa cells transfected with YFPrCNT2. CNT2 interaction with GRP58 was validated using co-immunoprecipitation experiments. In HeLa cells, fluorescence resonance energy transfer (FRET) efficiency increased upon fructose addition, consistent with a transient interaction between aldolase B and the transporter. The physiological basis for in vivo interactions was derived from experiments in which GRP58 was inhibited or overexpressed and aldolase B activity stimulated towards glycolysis. GRP58 appeared to be a negative effector of CNT2 function, whereas aldolase B flux modulated CNT2 activity via a mechanism involving acquisition of higher affinity for its substrates. These findings support the theory that CNT2 plays roles other than salvage and establishes links with energy metabolism.
机译：浓缩的核苷转运蛋白2 (CNT2)可能玩的高亲和性腺苷运输车生理作用超出了核苷打捞。先前的报道CNT2函数联系起来purinergic调制的信号和能量代谢在肠道和肝实质细胞(Duflot et al ., 2004年,摩尔细胞杂志24:2710-2719;119:1612 - 1621)。检查CNT2和能量之间的联系蛋白质代谢,CNT2伙伴被确定使用细菌二者混合和销售税下拉方法。作为诱饵,因为蛋白质缺乏这一领域显示等离子体膜插入和受损细胞内潴留。蛋白58 (GRP58)被确认为一个潜在的rCNT2伙伴拉实验。二者混合筛选对肝脏执行人类cDNA库识别了醛缩酶B作为另一个hCNT2伙伴。B-RFP和内源性GRP58分开硝唑与CNT2海拉细胞转染YFPrCNT2。验证使用co-immunoprecipitation实验。共振能量转移(FRET)效率增加对果糖,一致瞬态醛缩酶B和之间的相互作用运输机。体内相互作用是来自实验GRP58被抑制或过表达吗醛缩酶B对刺激的活动糖酵解。CNT2功能的效应,而醛缩酶B通量调制CNT2活动通过一个机制涉及收购的高亲和力基板。除了打捞,CNT2扮演角色建立与能量代谢的关系。

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