Activation of the Ca2+-activated K+ channel via protein kinase A-dependent phosphorylation in human prostatic smooth muscle cells.
International Journal of Urology(1998)
摘要
BACKGROUND:We investigated the functional importance of the Ca2+-activated K+ channel (K(Ca)-channel) of human prostatic smooth muscle cells in cyclic adenosine 3',5'-monophosphate (cAMP)-induced relaxation, to clarify signal transduction pathways and intracellular mechanisms of relaxation in prostatic smooth muscle.
METHODS:Using the patch-clamp technique, we characterized the K(Ca)-channel of cultured human prostatic smooth muscle cells. We also investigated the effects on the K(Ca)-channels of forskolin, an activator of adenylate cyclase, amrinone, a phosphodiesterase inhibitor, and protein kinase A (A-kinase)-dependent phosphorylation.
RESULTS:Single-channel current recordings from cultured human prostatic smooth muscle cells revealed the presence of K(Ca)-channels (conductance 296.7 +/- 5.67 pS, n = 7). In cell-attached patch configurations, the K(Ca)-channel was activated by forskolin (10(-4) mol/L) and amrinone (10(-4) mol/L). In inside-out patch configurations, it was activated by catalytic subunits of A-kinase (10 U/mL).
CONCLUSIONS:We conclude that the K(Ca)-channel of human prostatic smooth muscle cells is regulated by intracellular cAMP levels and that A-kinase mediates the cAMP-induced activation of the K(Ca)-channel. This regulation of the K(Ca)-channel by cAMP may at least partially explain cAMP-induced prostatic smooth muscle relaxation and the effectiveness of certain drugs for treatment of obstruction in benign prostatic hyperplasia.
更多查看译文
关键词
relaxation,protein kinase a
AI 理解论文
溯源树
样例
生成溯源树,研究论文发展脉络
Chat Paper
正在生成论文摘要