Ziskoven Christoph, Grafweg Sabrina, Bölck Birgit, Wiesner Rudolf J, Jimenez Maria, Giacobino Jean-Paul, Bloch W, Schwinger Robert H G, Brixius Klara
Laboratory of Muscle Research and Molecular Cardiology, Department of Internal Medicine III, University of Cologne, Cologne, Germany.
Pflugers Arch. 2007 Jan;453(4):443-53. doi: 10.1007/s00424-006-0137-7. Epub 2006 Sep 22.
This study investigated the influence of chronic beta(3)-adrenoceptor deficiency on myocardial function. Therefore, we investigated Ca(2+)-regulatory proteins, SERCA 2a activity, and myofibrillar and mitochondrial function in hearts of wild-type (WT, n=7) and beta(3)-adrenoceptor knockout mice (beta(3)-KNO, n=7). Morphometric heart analysis showed no difference between WT and beta(3)-KNO. No alterations were observed for the protein expression of the ryanodine receptor or phospholamban. However, in beta(3)-KNO mice, protein expression of SERCA 2a and phospholamban phosphorylation were significantly increased. These changes were accompanied by an increased SERCA 2a activity in beta(3)-KNO. Alterations in phospholamban phosphorylation were independent of alterations in beta(1)/beta(2)-adrenoceptor distribution and protein expression of G proteins in beta(3)-KNO. Measurement of myofibrillar Ca(2+) sensitivity showed no difference in the Ca(2+)/force relation for WT and beta(3)-KNO. The same seems to hold true for mitochondrial function since the protein expressions of cytochrome c, uncoupling protein 3 and cytochrome c oxidase subunit IV were similar in WT and beta(3)-KNO. The conclusion is that depression of beta(3)-adrenergic stimulation may modulate the protein expression of SERCA 2a and phospholamban phosphorylation, thereby improving sarcoplasmic reticulum Ca(2+) uptake. Thus, beta(3)-adrenergic depression may be a therapeutic aim in situations of impaired SERCA 2a activity, e.g. for the treatment of heart failure.
本研究调查了慢性β3 -肾上腺素能受体缺陷对心肌功能的影响。因此,我们研究了野生型(WT,n = 7)和β3 -肾上腺素能受体基因敲除小鼠(β3 - KNO,n = 7)心脏中的钙调节蛋白、肌浆网Ca2 + -ATP酶(SERCA)2a活性以及肌原纤维和线粒体功能。形态学心脏分析显示WT和β3 - KNO之间无差异。未观察到兰尼碱受体或受磷蛋白的蛋白表达有改变。然而,在β3 - KNO小鼠中,SERCA 2a的蛋白表达和受磷蛋白磷酸化显著增加。这些变化伴随着β3 - KNO中SERCA 2a活性的增加。受磷蛋白磷酸化的改变与β3 - KNO中β1/β2 -肾上腺素能受体分布的改变以及G蛋白的蛋白表达无关。肌原纤维Ca2 +敏感性的测量显示WT和β3 - KNO的Ca2 + /力关系无差异。线粒体功能似乎也是如此,因为细胞色素c、解偶联蛋白3和细胞色素c氧化酶亚基IV的蛋白表达在WT和β3 - KNO中相似。结论是β3 -肾上腺素能刺激的抑制可能调节SERCA 2a的蛋白表达和受磷蛋白磷酸化,从而改善肌浆网Ca2 +摄取。因此,β3 -肾上腺素能抑制可能是SERCA 2a活性受损情况下的一个治疗靶点,例如用于治疗心力衰竭。