Department of Pharmacology, University of South Alabama College of Medicine, Mobile, Alabama, United States of America.
PLoS One. 2012;7(8):e41711. doi: 10.1371/journal.pone.0041711. Epub 2012 Aug 2.
Receptor desensitization is a ubiquitous regulatory mechanism that defines the activatable pool of receptors, and thus, the ability of cells to respond to environmental stimuli. In recent years, the molecular mechanisms controlling the desensitization of a variety of receptors have been established. However, little is known about the molecular mechanisms that underlie desensitization of natriuretic peptide receptors, including natriuretic peptide receptor-A (NPR-A). Here we report that calcineurin (protein phosphatase 2B, PP2B, PPP3C) regulates homologous desensitization of NPR-A in murine Leydig tumor (MA-10) cells. We demonstrate that both pharmacological inhibition of calcineurin activity and siRNA-mediated suppression of calcineurin expression potentiate atrial natriuretic peptide (ANP)-induced cGMP synthesis. Treatment of MA-10 cells with inhibitors of other phosphoprotein phosphatases had little or no effect on ANP-induced cGMP accumulation. In addition, overexpression of calcineurin blunts ANP-induced cGMP synthesis. We also present data indicating that the inhibition of calcineurin potentiates ANP-induced testosterone production. To better understand the contribution of calcineurin in the regulation of NPR-A activity, we examined the kinetics of ANP-induced cGMP signals. We observed transient ANP-induced cGMP signals, even in the presence of phosphodiesterase inhibitors. Inhibition of both calcineurin and phosphodiesterase dramatically slowed the decay in the response. These observations are consistent with a model in which calcineurin mediated dephosphorylation and desensitization of NPR-A is associated with significant inhibition of cGMP synthesis. PDE activity hydrolyzes cGMP, thus lowering intracellular cGMP toward the basal level. Taken together, these data suggest that calcineurin plays a previously unrecognized role in the desensitization of NPR-A and, thereby, inhibits ANP-mediated increases in testosterone production.
受体脱敏是一种普遍存在的调节机制,它决定了受体的可激活池,从而决定了细胞对环境刺激的反应能力。近年来,控制各种受体脱敏的分子机制已经建立。然而,对于包括利钠肽受体-A(NPR-A)在内的利钠肽受体脱敏的分子机制知之甚少。在这里,我们报告钙调神经磷酸酶(蛋白磷酸酶 2B,PP2B,PPP3C)调节鼠睾丸间质瘤(MA-10)细胞中 NPR-A 的同源脱敏。我们证明,钙调神经磷酸酶活性的药理学抑制和钙调神经磷酸酶表达的 siRNA 介导的抑制均增强了心钠肽(ANP)诱导的 cGMP 合成。用其他磷酸蛋白磷酸酶抑制剂处理 MA-10 细胞对 ANP 诱导的 cGMP 积累几乎没有影响。此外,钙调神经磷酸酶的过表达会减弱 ANP 诱导的 cGMP 合成。我们还提供了数据表明,钙调神经磷酸酶的抑制增强了 ANP 诱导的睾酮产生。为了更好地理解钙调神经磷酸酶在 NPR-A 活性调节中的作用,我们检查了 ANP 诱导的 cGMP 信号的动力学。我们观察到即使存在磷酸二酯酶抑制剂,ANP 也会引起短暂的 cGMP 信号。钙调神经磷酸酶和磷酸二酯酶的抑制均显著减慢了反应的衰减。这些观察结果与钙调神经磷酸酶介导的 NPR-A 去磷酸化和脱敏与 cGMP 合成的显著抑制相关的模型一致。PDE 活性水解 cGMP,从而使细胞内 cGMP 降低到基础水平。综上所述,这些数据表明钙调神经磷酸酶在 NPR-A 的脱敏中发挥了以前未被认识到的作用,从而抑制了 ANP 介导的睾酮产生增加。