Restoration of uridine 5'-triphosphate-suppressed delayed rectifying K(+) currents by an NO activator KMUP-1 involves RhoA/Rho kinase signaling in pulmonary artery smooth muscle cells

NO激活剂KMUP-1通过激活肺动脉平滑肌细胞中的RhoA/Rho激酶信号通路,恢复尿苷5'-三磷酸抑制的延迟整流K(+)电流。

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Abstract

We have demonstrated that KMUP-1 (7-[2-[4-(2-chlorobenzene)piperazinyl]ethyl]-1,3-dimethylxanthine) blunts monocrotaline-induced pulmonary arterial hypertension by altering Ca(2+) sensitivity, K(+)-channel function, endothelial nitric oxide synthase activity, and RhoA/Rho kinase (ROCK) expression. This study further investigated whether KMUP-1 impedes uridine 5'-triphosphate (UTP)-inhibited delayed rectifying K(+) (K(DR)) current in rat pulmonary arteries involved the RhoA/ROCK signaling. Pulmonary artery smooth muscle cells (PASMCs) were enzymatically dissociated from rat pulmonary arteries. KMUP-1 (30μM) attenuated UTP (30μM)-mediated membrane depolarization and abolished UTP-enhanced cytosolic Ca(2+) concentration. Whole-cell patch-clamp electrophysiology was used to monitor K(DR) currents. A voltage-dependent K(DR) current was isolated and shown to consist of a 4-aminopyridine (5mM)-sensitive component and an insensitive component. The 4-aminopyridine sensitive K(DR) current was suppressed by UTP (30μM). The ROCK inhibitor Y27632 (30μM) abolished the ability of UTP to inhibit the K(DR) current. Like Y27632, KMUP-1 (30μM) similarly abolished UTP-inhibited K(DR) currents. Superfused protein kinase A and protein kinase G inhibitors (KT5720, 300nM and KT5823, 300nM) did not affect UTP-inhibited K(DR) currents, but the currents were restored by adding KMUP-1 (30μM) to the superfusate. KMUP-1 reversal of K(DR) current inhibition by UTP predominantly involves the ROCK inhibition. The results indicate that the RhoA/ROCK signaling pathway plays a key role in eliciting PASMCs depolarization caused by UTP, which would result in pulmonary artery constriction. KMUP-1 blocks UTP-mediated PASMCs depolarization, suggesting that it would prevent abnormal pulmonary vasoconstriction.

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