Lee S W, Schwartz A, Adams R J, Yamori Y, Whitmer K, Lane L K, Wallick E T
Hypertension. 1983 Sep-Oct;5(5):682-8. doi: 10.1161/01.hyp.5.5.682.
Na+,K+-ATPase activity, phosphorylation, and [3H]ouabain binding in sarcolemma isolated from spontaneously hypertensive rat (SHR) hearts were compared to the same parameters in sarcolemma from normotensive rat (WKY) hearts. Sarcolemma prepared from SHR heart contained significantly less ouabain-inhibitable ATPase activity than sarcolemma from WKY heart. No significant differences in sarcolemmal protein content or recovery were noted between the two groups. The numbers of phosphorylation sites and ouabain binding sites were lower for SHR hearts than for WKY hearts. The KD values for ouabain binding were the same (0.30 muM) in cardiac sarcolemma of SHR and WKY. The I50 values for inhibition by ouabain of Na+,K+-ATPase were also the same for both groups (SHR = 49 microM; WKY = 44 microM). These data suggest that the decrease of cardiac sarcolemmal Na+,K+-ATPase activity in SHR hearts is due to a decrease in the number of active sites.
将自发性高血压大鼠(SHR)心脏分离出的肌膜中的钠钾ATP酶活性、磷酸化作用及[3H]哇巴因结合情况,与正常血压大鼠(WKY)心脏肌膜中的相同参数进行了比较。SHR心脏制备的肌膜中哇巴因抑制的ATP酶活性明显低于WKY心脏的肌膜。两组之间肌膜蛋白含量或回收率无显著差异。SHR心脏的磷酸化位点和哇巴因结合位点数量低于WKY心脏。SHR和WKY心脏肌膜中哇巴因结合的KD值相同(0.30μM)。两组中哇巴因抑制钠钾ATP酶的I50值也相同(SHR = 49μM;WKY = 44μM)。这些数据表明,SHR心脏中心肌肌膜钠钾ATP酶活性的降低是由于活性位点数量减少所致。