Wehrens Xander H T, Lehnart Stephan E, Reiken Steven R, Marks Andrew R
Department of Physiology and Cellular Biophysics, Columbia University College of Physicians and Surgeons, 630 W 168th St, P&S 9-401, Box 65, New York, NY 10032, USA.
Circ Res. 2004 Apr 2;94(6):e61-70. doi: 10.1161/01.RES.0000125626.33738.E2. Epub 2004 Mar 11.
The cardiac ryanodine receptor (RyR2)/calcium release channel on the sarcoplasmic reticulum is required for muscle excitation-contraction coupling. Using site-directed mutagenesis, we identified the specific Ca2+/calmodulin-dependent protein kinase II (CaMKII) phosphorylation site on recombinant RyR2, distinct from the site for protein kinase A (PKA) that mediates the "fight-or-flight" stress response. CaMKII phosphorylation increased RyR2 Ca2+ sensitivity and open probability. CaMKII was activated at increased heart rates, which may contribute to enhanced Ca2+-induced Ca2+ release. Moreover, rate-dependent CaMKII phosphorylation of RyR2 was defective in heart failure. CaMKII-mediated phosphorylation of RyR2 may contribute to the enhanced contractility observed at higher heart rates. The full text of this article is available online at http://circres.ahajournals.org.
肌浆网上的心脏雷诺丁受体(RyR2)/钙释放通道是肌肉兴奋-收缩偶联所必需的。我们利用定点诱变技术,在重组RyR2上鉴定出了特定的Ca2+/钙调蛋白依赖性蛋白激酶II(CaMKII)磷酸化位点,该位点不同于介导“战斗或逃跑”应激反应的蛋白激酶A(PKA)的位点。CaMKII磷酸化增加了RyR2对Ca2+的敏感性和开放概率。CaMKII在心率增加时被激活,这可能有助于增强Ca2+诱导的Ca2+释放。此外,心力衰竭时RyR2的速率依赖性CaMKII磷酸化存在缺陷。CaMKII介导的RyR2磷酸化可能有助于解释在较高心率时观察到的收缩力增强现象。本文全文可在http://circres.ahajournals.org在线获取。