Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini", Universidad de Buenos Aires (UBA), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Facultad de Farmacia y Bioquímica, Buenos Aires, Argentina.
Universidad de Buenos Aires (UBA), Facultad de Farmacia y Bioquímica, Departamento de Química Biológica, Cátedra de Química Biológica, Buenos Aires, Argentina.
PLoS Comput Biol. 2023 Jun 29;19(6):e1011196. doi: 10.1371/journal.pcbi.1011196. eCollection 2023 Jun.
Intestinal epithelial cells play important roles in the absorption of nutrients, secretion of electrolytes and food digestion. The function of these cells is strongly influenced by purinergic signalling activated by extracellular ATP (eATP) and other nucleotides. The activity of several ecto-enzymes determines the dynamic regulation of eATP. In pathological contexts, eATP may act as a danger signal controlling a variety of purinergic responses aimed at defending the organism from pathogens present in the intestinal lumen. In this study, we characterized the dynamics of eATP on polarized and non-polarized Caco-2 cells. eATP was quantified by luminometry using the luciferin-luciferase reaction. Results show that non-polarized Caco-2 cells triggered a strong but transient release of intracellular ATP after hypotonic stimuli, leading to low micromolar eATP accumulation. Subsequent eATP hydrolysis mainly determined eATP decay, though this effect could be counterbalanced by eATP synthesis by ecto-kinases kinetically characterized in this study. In polarized Caco-2 cells, eATP showed a faster turnover at the apical vs the basolateral side. To quantify the extent to which different processes contribute to eATP regulation, we created a data-driven mathematical model of the metabolism of extracellular nucleotides. Model simulations showed that eATP recycling by ecto-AK is more efficient a low micromolar eADP concentrations and is favored by the low eADPase activity of Caco-2 cells. Simulations also indicated that a transient eATP increase could be observed upon the addition of non-adenine nucleotides due the high ecto-NDPK activity in these cells. Model parameters showed that ecto-kinases are asymmetrically distributed upon polarization, with the apical side having activity levels generally greater in comparison with the basolateral side or the non-polarized cells. Finally, experiments using human intestinal epithelial cells confirmed the presence of functional ecto-kinases promoting eATP synthesis. The adaptive value of eATP regulation and purinergic signalling in the intestine is discussed.
肠上皮细胞在营养物质吸收、电解质分泌和食物消化中发挥重要作用。这些细胞的功能受到细胞外 ATP(eATP)和其他核苷酸激活的嘌呤能信号的强烈影响。几种外切酶的活性决定了 eATP 的动态调节。在病理情况下,eATP 可能作为一种危险信号,控制各种嘌呤能反应,旨在保护肠道腔中存在的病原体免受机体侵害。在这项研究中,我们对极化和非极化 Caco-2 细胞中的 eATP 动力学进行了表征。通过使用荧光素-荧光素酶反应的发光法对 eATP 进行定量。结果表明,非极化 Caco-2 细胞在低渗刺激后会引发强烈但短暂的细胞内 ATP 释放,导致低微摩尔 eATP 积累。随后,eATP 水解主要决定 eATP 的衰减,尽管这种效应可以通过本研究中动力学特征化的外切激酶来合成 eATP 来抵消。在极化的 Caco-2 细胞中,eATP 在顶端侧比基底外侧具有更快的周转率。为了量化不同过程对 eATP 调节的贡献程度,我们创建了一个外核苷酸代谢的基于数据的数学模型。模型模拟表明,外切 AK 对 eATP 的循环利用在低微摩尔 eADP 浓度下效率更高,并且受到 Caco-2 细胞中低 eADP 酶活性的青睐。模拟还表明,由于这些细胞中外切 NDPK 的高活性,在添加非腺嘌呤核苷酸时可能会观察到短暂的 eATP 增加。模型参数表明,在外极化过程中外切酶呈不对称分布,顶端侧的活性水平通常比基底外侧或非极化细胞的活性水平高。最后,使用人肠道上皮细胞的实验证实了具有促进 eATP 合成功能的功能性外切酶的存在。讨论了 eATP 调节和嘌呤能信号在肠道中的适应价值。