La Jolla Bioengineering Institute, 505 Coast Blvd. S., La Jolla, CA 92037, USA.
Am J Physiol Heart Circ Physiol. 2010 Jul;299(1):H225-35. doi: 10.1152/ajpheart.01073.2009. Epub 2010 May 7.
We studied hypoxia-induced dynamic changes in the balance between PKA and PKA-counteracting phosphatases in the microfluidic environment in single cells using picosecond fluorescence spectroscopy and intramolecular fluorescence resonance energy transfer (FRET)-based sensors of PKA activity. First, we found that the apparent PKA activity in bone cells (MC3T3-E1 cells) and endothelial cells (bovine aortic endothelial cells) is rapidly and sensitively modulated by the level of O(2) in the media. When the O(2) concentration in the glucose-containing media was lowered due to O(2) consumption by the cells in the microfluidic chamber, the apparent PKA activity increases; the reoxygenation of cells under hypoxia leads to a rapid ( approximately 2 min) decrease of the apparent PKA activity. Second, lack of glucose in the media led to a lower apparent PKA activity and to a reversal of the response of the apparent PKA activity to hypoxia and reoxygenation. Third, the apparent PKA activity in cells under hypoxia was predominantly regulated via a cAMP-independent pathway since 1) changes in the cAMP level in the cells were not detected using a cAMP FRET sensor, 2) the decay of cAMP levels was too slow to account for the fast decrease in PKA activity levels in response to reoxygenation, and 3) the response of the apparent PKA activity due to hypoxia/reoxygenation was not affected by an adenylate cyclase inhibitor (MDL-12,330A) at 1 mM concentration. Fourth, the immediate onset of ROS accumulation in MC3T3-E1 cells subjected to hypoxia and the sensitivity of the apparent PKA activity to redox levels suggest that the apparent PKA activity change during hypoxia and reoxygenation in this study can be linked to a redox potential change in response to intermittent hypoxia through the regulation of activities of PKA-counteracting phosphatases such as protein phosphatase 1. Finally, our results suggest that the detection of PKA activity could be used to monitor responses of cells to hypoxia in real time.
我们使用皮秒荧光光谱法和基于 PKA 活性的分子内荧光共振能量转移(FRET)传感器,在微流控环境中单细胞中研究了缺氧诱导的 PKA 与 PKA 拮抗磷酸酶之间平衡的动态变化。首先,我们发现骨细胞(MC3T3-E1 细胞)和内皮细胞(牛主动脉内皮细胞)中的 PKA 活性的表观水平可以被培养基中 O(2)的水平快速而敏感地调节。当微流控室中的细胞消耗 O(2)导致培养基中的 O(2)浓度降低时,表观 PKA 活性增加;缺氧条件下细胞复氧会导致表观 PKA 活性的快速(约 2 分钟)下降。其次,培养基中缺乏葡萄糖会导致表观 PKA 活性降低,并使表观 PKA 活性对缺氧和复氧的反应发生逆转。第三,缺氧细胞中的表观 PKA 活性主要通过 cAMP 非依赖性途径进行调节,原因如下:1)使用 cAMP FRET 传感器未检测到细胞内 cAMP 水平的变化,2)cAMP 水平的衰减太慢,无法解释复氧时 PKA 活性水平的快速下降,3)由于缺氧/复氧引起的表观 PKA 活性的反应不受 1mM 浓度的腺苷酸环化酶抑制剂(MDL-12,330A)的影响。第四,MC3T3-E1 细胞缺氧时 ROS 积累的即刻发生以及表观 PKA 活性对氧化还原水平的敏感性表明,在本研究中,缺氧和复氧过程中表观 PKA 活性的变化可能与通过调节 PKA 拮抗磷酸酶(如蛋白磷酸酶 1)的活性来响应间歇性缺氧的氧化还原电位变化有关。最后,我们的结果表明,PKA 活性的检测可用于实时监测细胞对缺氧的反应。