Department of Pharmacology and Toxicology, Virginia Commonwealth University School of Medicine, Richmond, Virginia, United States of America.
PLoS One. 2013 Aug 7;8(8):e71212. doi: 10.1371/journal.pone.0071212. Print 2013.
The CD38-ADP-ribosylcyclase-mediated Ca(2+) signaling pathway importantly contributes to the vasomotor response in different arteries. Although there is evidence indicating that the activation of CD38-ADP-ribosylcyclase is associated with CD38 internalization, the molecular mechanism mediating CD38 internalization and consequent activation in response to a variety of physiological and pathological stimuli remains poorly understood. Recent studies have shown that CD38 may sense redox signals and is thereby activated to produce cellular response and that the NADPH oxidase isoform, NOX1, is a major resource to produce superoxide (O2·-)) in coronary arterial myocytes (CAMs) in response to muscarinic receptor agonist, which uses CD38-ADP-ribosylcyclase signaling pathway to exert its action in these CAMs. These findings led us hypothesize that NOX1-derived O2·- serves in an autocrine fashion to enhance CD38 internalization, leading to redox activation of CD38-ADP-ribosylcyclase activity in mouse CAMs. To test this hypothesis, confocal microscopy, flow cytometry and a membrane protein biotinylation assay were used in the present study. We first demonstrated that CD38 internalization induced by endothelin-1 (ET-1) was inhibited by silencing of NOX1 gene, but not NOX4 gene. Correspondingly, NOX1 gene silencing abolished ET-1-induced O2·- production and increased CD38-ADP-ribosylcyclase activity in CAMs, while activation of NOX1 by overexpression of Rac1 or Vav2 or administration of exogenous O2·- significantly increased CD38 internalization in CAMs. Lastly, ET-1 was found to markedly increase membrane raft clustering as shown by increased colocalization of cholera toxin-B with CD38 and NOX1. Taken together, these results provide direct evidence that Rac1-NOX1-dependent O2·- production mediates CD38 internalization in CAMs, which may represent an important mechanism linking receptor activation with CD38 activity in these cells.
CD38-ADP-核糖基环化酶介导的 Ca(2+)信号通路对不同动脉的血管舒缩反应很重要。虽然有证据表明 CD38-ADP-核糖基环化酶的激活与 CD38 的内化有关,但介导 CD38 内化及其对各种生理和病理刺激的反应的分子机制仍知之甚少。最近的研究表明,CD38 可能感知氧化还原信号,从而被激活以产生细胞反应,并且 NADPH 氧化酶同工型 NOX1 是产生超氧阴离子(O2·-)的主要来源)在冠状动脉心肌细胞(CAMs)中,对毒蕈碱受体激动剂的反应,其使用 CD38-ADP-核糖基环化酶信号通路在这些 CAMs 中发挥作用。这些发现使我们假设,NOX1 衍生的 O2·- 以自分泌的方式增强 CD38 的内化,从而导致 CD38-ADP-核糖基环化酶活性在小鼠 CAMs 中的氧化还原激活。为了验证这一假设,本研究采用共聚焦显微镜、流式细胞术和膜蛋白生物素化测定法。我们首先证明,内皮素-1(ET-1)诱导的 CD38 内化被 NOX1 基因沉默抑制,但不是 NOX4 基因。相应地,NOX1 基因沉默消除了 ET-1 诱导的 O2·-产生和 CAMs 中 CD38-ADP-核糖基环化酶活性的增加,而 Rac1 或 Vav2 的过表达或外源性 O2·- 的给予激活 NOX1 显著增加了 CAMs 中的 CD38 内化。最后,发现 ET-1 明显增加了膜筏聚类,表现为霍乱毒素-B 与 CD38 和 NOX1 的共定位增加。总之,这些结果提供了直接证据,表明 Rac1-NOX1 依赖性 O2·- 产生介导了 CAMs 中的 CD38 内化,这可能代表了一种将受体激活与这些细胞中 CD38 活性联系起来的重要机制。