Sahin-Erdemli I, Rashed S M, Songu-Mize E
Department of Pharmacology and Experimental Therapeutics, Louisiana State University Medical Center, New Orleans 70112.
Am J Physiol. 1994 Jan;266(1 Pt 2):H350-3. doi: 10.1152/ajpheart.1994.266.1.H350.
The catalytic alpha- and smaller glycosylated beta-subunits of the membrane transport enzyme Na(+)-K(+)-adenosinetriphosphatase (ATPase) occur in different molecular forms, alpha 1, alpha 2, alpha 3, beta 1, and beta 2. The catalytic alpha 1-, alpha 2-, and alpha 3-subunits of the enzyme have varying affinities for digitalis and exist in different tissues with unique distribution patterns. In this report we document for the first time the existence of alpha 1-, alpha 2-, alpha 3-subunit proteins (all approximately 97.5 kDa) in cultured rat aortic smooth muscle cells and rat tail arteries. In addition to the three molecular forms of the alpha-protein we detected a minor band at approximately 68-kDa position in aortic smooth muscle cells, which may correspond to the truncated alpha 1-protein reported earlier.
膜转运酶钠钾-三磷酸腺苷酶(ATP酶)的催化性α亚基和较小的糖基化β亚基以不同的分子形式存在,即α1、α2、α3、β1和β2。该酶的催化性α1、α2和α3亚基对洋地黄有不同的亲和力,并以独特的分布模式存在于不同组织中。在本报告中,我们首次记录了培养的大鼠主动脉平滑肌细胞和大鼠尾动脉中存在α1、α2、α3亚基蛋白(均约97.5 kDa)。除了α蛋白的三种分子形式外,我们在主动脉平滑肌细胞中约68 kDa位置检测到一条 minor 条带,它可能对应于先前报道的截短型α1蛋白。