Department of Physiology and Pharmacology, Schulich School of Medicine and Dentistry, University of Western Ontario, London, ON, N6A 5C1, Canada.
Mol Cell Biochem. 2014 Jan;385(1-2):239-48. doi: 10.1007/s11010-013-1832-2. Epub 2013 Oct 6.
Adenosine receptor activation has been shown to be associated with diminution of cardiac hypertrophy and it has been suggested that endogenously produced adenosine may serve to blunt pro-hypertrophic processes. In the present study, we determined the effects of two pro-hypertrophic stimuli, angiotensin II (Ang II, 100 nM) and endothelin-1 (ET-1, 10 nM) on Ras homolog gene family, member A (RhoA)/Rho-associated, coiled-coil containing protein kinase (ROCK) activation in cultured neonatal rat ventricular myocytes and whether the latter serves as a target for the anti-hypertrophic effect of adenosine receptor activation. Both hypertrophic stimuli potently increased RhoA activity with peak activation occurring 15-30 min following agonist addition. These effects were associated with significantly increased phosphorylation (inactivation) of cofilin, a downstream mediator of RhoA, an increase in actin polymerization, and increased activation and nuclear import of p38 mitogen activated protein kinase. The ability of both Ang II and ET-1 to activate the RhoA pathway was completely prevented by the adenosine A1 receptor agonist N (6)-cyclopentyladenosine, the A2a receptor agonist 2-p-(2-carboxyethyl)-phenethylamino-5'-N-ethylcarboxamidoadenosine, the A3 receptor agonist N (6)-(3-iodobenzyl)adenosine-5'-methyluronamide as well as the nonspecific adenosine analog 2-chloro adenosine. All effects of specific receptor agonists were prevented by their respective receptor antagonists. Moreover, all adenosine agonists prevented either Ang II- or ET-1-induced hypertrophy, a property shared by the RhoA inhibitor Clostridium botulinum C3 exoenzyme, the ROCK inhibitor Y-27632 or the actin depolymerizing agent latrunculin B. Our study therefore demonstrates that both Ang II and ET-1 can activate the RhoA pathway and that prevention of the hypertrophic response to both agonists by adenosine receptor activation is mediated by prevention of RhoA stimulation and actin polymerization.
腺嘌呤核苷受体的激活已被证明与心肌肥厚的减轻有关,并且有人提出内源性产生的腺嘌呤核苷可能用于钝化促肥厚过程。在本研究中,我们确定了两种促肥厚刺激物,血管紧张素 II(Ang II,100 nM)和内皮素-1(ET-1,10 nM)对培养的新生大鼠心室肌细胞中 Ras 同源基因家族成员 A(RhoA)/Rho 相关卷曲螺旋蛋白激酶(ROCK)激活的影响,以及后者是否是腺嘌呤核苷受体激活的抗肥厚作用的靶标。两种肥厚刺激物均强烈增加 RhoA 活性,在激动剂添加后 15-30 分钟达到峰值激活。这些作用与下游 RhoA 介导物丝切蛋白的磷酸化(失活)显著增加、肌动蛋白聚合增加以及 p38 有丝分裂原激活蛋白激酶的激活和核内输入增加有关。腺嘌呤核苷 A1 受体激动剂 N(6)-环戊基腺嘌呤、A2a 受体激动剂 2-对-(2-羧乙基)-苯乙胺-5'-N-乙基羧酰胺腺嘌呤、A3 受体激动剂 N(6)-(3-碘苄基)腺苷-5'-甲基尿苷酰胺以及非特异性腺嘌呤类似物 2-氯腺嘌呤完全阻止了 Ang II 和 ET-1 激活 RhoA 途径的能力。所有特异性受体激动剂的作用均被其各自的受体拮抗剂所阻止。此外,所有的腺嘌呤核苷激动剂都能阻止 Ang II 或 ET-1 诱导的肥厚,这一特性与 RhoA 抑制剂肉毒梭菌 C3 外切酶、ROCK 抑制剂 Y-27632 或肌动蛋白解聚剂 latrunculin B 相同。因此,我们的研究表明,Ang II 和 ET-1 均可激活 RhoA 途径,并且腺嘌呤核苷受体激活对两种激动剂的肥厚反应的预防是通过阻止 RhoA 刺激和肌动蛋白聚合来介导的。