Department of Clinical and Translational Sciences, Joan C Edwards School of Medicine, Marshall University, 1600 Medical Center Drive, Huntington, WV, 25701, USA.
Department of Clinical and Translational Sciences, Joan C Edwards School of Medicine, Marshall University, 1600 Medical Center Drive, Huntington, WV, 25701, USA.
Nitric Oxide. 2018 Sep 1;79:8-13. doi: 10.1016/j.niox.2018.04.007. Epub 2018 Apr 24.
Pharmacological manipulations of constitutive nitric oxide (cNO) levels have been shown to have variable effects on Na absorption in vivo and in vitro in different tissues. Species differences, untoward in vivo effects (e.g. ENS, blood flow) and pharmacological non-specificity may account for these confounding observations. Thus, to directly and specifically determine the effect of cNO on brush border membrane Na/H exchange (NHE3) and Na-dependent glucose co-transport (SGLT-1), we inhibited cNO synthase (NOS3) with its siRNA in rat small intestinal epithelial cells (IEC-18) in vitro. As expected, intracellular cNO levels were reduced in siRNA NOS3 transfected cells. In these cells, SGLT-1 was significantly reduced compared to control. In contrast, NHE3 was significantly increased in siRNA NOS3 transfected cells. To determine if SGLT-1 changes were secondary to altered Na/K-ATPase, its activity was measured and found to be increased in NOS3 silenced cells. The mechanism of inhibition of SGLT-1 was secondary to diminished affinity of the co-transporter for glucose in NOS3 silenced cells. In contrast, the mechanism of stimulation of NHE3 is by increasing BBM exchanger numbers in siRNA NOS3 cells while the affinity was unaffected. Western blot studies of immunoreactive BBM proteins also confirmed the kinetic studies. All these data indicates that direct and specific inhibition of NOS3 with its siRNA inhibits SGLT-1 while stimulating NHE3 in the BBM. Thus, cNO uniquely and compensatorily regulates BBM NHE3 and SGLT-1 to maintain cellular Na homeostasis and these unique alterations by cNO are mediated by its intracellular 2nd messenger cGMP.
药理学操纵组成型一氧化氮(cNO)水平已被证明在不同组织的体内和体外对 Na 吸收具有不同的影响。种属差异、体内不良反应(例如 ENS、血流)和药理学非特异性可能解释了这些混杂的观察结果。因此,为了直接和专门确定 cNO 对刷状缘膜 Na/H 交换(NHE3)和 Na 依赖性葡萄糖共转运(SGLT-1)的影响,我们在体外使用其 siRNA 抑制大鼠小肠上皮细胞(IEC-18)中的 cNO 合酶(NOS3)。如预期的那样,siRNA NOS3 转染细胞中的细胞内 cNO 水平降低。在这些细胞中,与对照相比,SGLT-1 显著减少。相比之下,siRNA NOS3 转染细胞中的 NHE3 显著增加。为了确定 SGLT-1 的变化是否继发于 Na/K-ATPase 的改变,测量了其活性,发现 NOS3 沉默细胞中的活性增加。SGLT-1 抑制的机制继发于 NOS3 沉默细胞中协同转运体对葡萄糖的亲和力降低。相比之下,NHE3 的刺激机制是通过增加 siRNA NOS3 细胞中 BBM 交换器的数量,而亲和力不受影响。免疫印迹研究也证实了 BBM 蛋白的动力学研究。所有这些数据表明,用其 siRNA 直接和专门抑制 NOS3 可抑制 SGLT-1,同时刺激 BBM 中的 NHE3。因此,cNO 独特地并补偿性地调节 BBM NHE3 和 SGLT-1 以维持细胞内 Na 稳态,而 cNO 引起的这些独特变化是由其细胞内第二信使 cGMP 介导的。