Cardiovascular Research Center, Temple University School of Medicine, Philadelphia, PA, USA.
Mol Pharmacol. 2013 Aug;84(2):227-35. doi: 10.1124/mol.113.086322. Epub 2013 May 20.
Circulating levels of arginine vasopressin (AVP) are elevated during hypovolemia and during cardiac stress. AVP activates arginine vasopressin type 1A (V(1A))/Gα(q)-coupled receptors in the heart and vasculature and V(2)/Gα(s)-coupled receptors in the kidney. However, little is known regarding the signaling pathways that influence the effects of V(1A) receptor (V(1A)R) activation during cellular injury. Using hypoxia-reoxygenation (H/R) as a cell injury model, we evaluated cell survival and caspase 3/7 activity in H9c2 myoblasts after treatment with AVP. Pretreatment of H9c2 cells with AVP significantly reduced H/R-induced cell death and caspase 3/7 activity, effects that were blocked via both selective V(1A)R inhibition and mitogen-activated protein kinase (MEK1/2) inhibition. AVP increased extracellular-regulated kinase 1/2 (ERK1/2) phosphorylation in a concentration-dependent manner that was sensitive to MEK1/2 inhibition and V(1A)R inhibition, but not V(1B)R or V(2)R inhibition. Discrete elements of the V(1A)/Gα(q)-protein kinase C (PKC) and V(1A)/G protein-coupled receptor kinase (GRK)/β-arrestin signaling cascades were inhibited to dissect the pathways responsible for the protective effects of V(1A)R signaling: Gα(q) (overexpression of Gq-I-ires-green fluorescent protein), PKC (administration of Ro 31-82425; 2-[8-(aminomethyl)-6,7,8,9-tetrahydropyrido[1,2-a]indol-3-yl]-3-(1-methyl-1H-indol-3-yl)maleimide, HCl, bisindolylmaleimide X, HCl), GRK2 [C-terminal GRK2 peptide overexpression and small interfering RNA (siRNA) knockdown], GRK5 (siRNA knockdown), and β-arrestin1 (siRNA knockdown). These studies demonstrated that both Gα(q)/PKC- and GRK2/β-arrestin1-dependent V(1A)R signaling were capable of inducing ERK1/2 phosphorylation in response to AVP stimulation. However, AVP-mediated protection against H/R was elicited only via GRK2- and β-arrestin1-dependent signaling. These results suggest that activation of the V(1A)R in H9c2 cells mediates protective signaling via a GRK2/β-arrestin1/ERK1/2-dependent mechanism that leads to decreased caspase 3/7 activity and enhanced survival under conditions of ischemic stress.
血管加压素(AVP)在低血容量和心脏应激期间循环水平升高。AVP 在心脏和血管中激活精氨酸加压素 1A 型(V(1A)/Gα(q)偶联受体),在肾脏中激活 V(2)/Gα(s)偶联受体。然而,关于影响细胞损伤期间 V(1A)受体(V(1A)R)激活的信号通路知之甚少。使用缺氧再复氧(H/R)作为细胞损伤模型,我们评估了 AVP 处理后 H9c2 成肌细胞的细胞存活和 caspase 3/7 活性。H9c2 细胞的预处理用 AVP 显著降低了 H/R 诱导的细胞死亡和 caspase 3/7 活性,这些作用通过选择性 V(1A)R 抑制和丝裂原活化蛋白激酶(MEK1/2)抑制来阻断。AVP 以浓度依赖性方式增加细胞外调节激酶 1/2(ERK1/2)磷酸化,该作用对 MEK1/2 抑制和 V(1A)R 抑制敏感,但对 V(1B)R 或 V(2)R 抑制不敏感。通过抑制 V(1A)/Gα(q)-蛋白激酶 C(PKC)和 V(1A)/G 蛋白偶联受体激酶(GRK)/β-arrestin 信号级联的离散元件来剖析负责 V(1A)R 信号的保护作用的途径:Gα(q)(过表达 Gq-I-ires-绿色荧光蛋白),PKC(给予 Ro 31-82425;2-[8-(氨甲基)-6,7,8,9-四氢吡啶并[1,2-a]吲哚-3-基]-3-(1-甲基-1H-吲哚-3-基)马来酰亚胺盐酸盐,双吲哚基马来酰亚胺 X,HCl),GRK2[C 末端 GRK2 肽过表达和小干扰 RNA(siRNA)敲低],GRK5(siRNA 敲低)和β-arrestin1(siRNA 敲低)。这些研究表明,AVP 刺激后,Gα(q)/PKC-和 GRK2/β-arrestin1 依赖性 V(1A)R 信号均能够诱导 ERK1/2 磷酸化。然而,仅通过 GRK2 和β-arrestin1 依赖性信号,AVP 介导的对 H/R 的保护作用被诱发。这些结果表明,在 H9c2 细胞中激活 V(1A)R 通过一种依赖于 GRK2/β-arrestin1/ERK1/2 的机制介导保护信号,导致在缺血应激下 caspase 3/7 活性降低和存活增加。