Department of Pediatrics, Center for Neural Circuits and Behavior, University of California at San Diego School of Medicine, La Jolla, CA 92093, USA.
Proc Natl Acad Sci U S A. 2012 Feb 28;109(9):3377-82. doi: 10.1073/pnas.1118067109. Epub 2012 Feb 13.
Lesch-Nyhan disease (LND) is an X-linked genetic disorder caused by mutations of the hypoxanthine guanine phosphoribosyltransferase (HPRT) purine biosynthesis gene and characterized by aberrant purine metabolism, deficient basal ganglia dopamine levels, dystonia, and severe neurobehavioral manifestations, including compulsive self-injurious behavior. Although available evidence has identified important roles for purinergic signaling in brain development, the mechanisms linking HPRT deficiency, purinergic pathways, and neural dysfunction of LND are poorly understood. In these studies aimed at characterizing purinergic signaling in HPRT deficiency, we used a lentivirus vector stably expressing an shRNA targeted to the HPRT gene to produce HPRT-deficient human CVB induced pluripotent stem cells and human HUES11 embryonic stem cells. Both CVB and HUES11 cells show >99% HPRT knockdown and demonstrate markedly decreased expression of the purinergic P2Y1 receptor mRNA. In CVB cells, P2Y1 mRNA and protein down-regulation by HPRT knockdown is refractory to activation by the P2Y1 receptor agonist ATP and shows aberrant purinergic signaling, as reflected by marked deficiency of the transcription factor pCREB and constitutive activation of the MAP kinases phospho-ERK1/2. Moreover, HPRT-knockdown CVB cells also demonstrate marked reduction of phosphorylated β-catenin. These results indicate that the housekeeping gene HPRT regulates purinergic signaling in pluripotent human stem cells, and that this regulation occurs at least partly through aberrant P2Y1-mediated expression and signaling. We propose that such mechanisms may play a role in the neuropathology of HPRT-deficiency LND and may point to potential molecular targets for modulation of this intractable neurological phenotype.
Lesch-Nyhan 病(LND)是一种 X 连锁遗传疾病,由次黄嘌呤鸟嘌呤磷酸核糖转移酶(HPRT)嘌呤生物合成基因的突变引起,其特征为异常嘌呤代谢、基底神经节多巴胺水平不足、肌张力障碍和严重的神经行为表现,包括强迫性自残行为。尽管现有证据已确定嘌呤能信号在大脑发育中的重要作用,但 HPRT 缺乏、嘌呤能途径和 LND 神经功能障碍之间的机制仍知之甚少。在这些旨在表征 HPRT 缺乏症中嘌呤能信号的研究中,我们使用稳定表达靶向 HPRT 基因的 shRNA 的慢病毒载体来产生 HPRT 缺陷型人 CVB 诱导多能干细胞和人 HUES11 胚胎干细胞。CVB 和 HUES11 细胞均显示 >99%的 HPRT 敲低,并且明显降低嘌呤能 P2Y1 受体 mRNA 的表达。在 CVB 细胞中,HPRT 敲低导致 P2Y1 mRNA 和蛋白下调对 P2Y1 受体激动剂 ATP 的激活具有抗性,并表现出异常的嘌呤能信号,反映为转录因子 pCREB 的明显缺乏和 MAP 激酶磷酸化 ERK1/2 的组成性激活。此外,HPRT 敲低的 CVB 细胞还显示磷酸化 β-连环蛋白的明显减少。这些结果表明,管家基因 HPRT 调节多能人干细胞中的嘌呤能信号,并且这种调节至少部分通过异常的 P2Y1 介导的表达和信号传导发生。我们提出,这些机制可能在 HPRT 缺乏型 LND 的神经病理学中起作用,并且可能指向这种难治性神经表型的潜在分子靶标。