Regulation of cardiac contractile proteins. Correlations between physiology and biochemistry.
Regulation of cardiac contractile proteins. Correlations between physiology and biochemistry.
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心脏收缩蛋白的调节。
DOI：
10.1161/01.res.55.5.565
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发表时间：
1984
影响因子：
20.1
通讯作者：
Winegrad,S
中科院分区：
文献类型：
--
作者：
Winegrad,S
哺乳动物心肌收缩蛋白功能特性的调节在心脏对β-肾上腺素能刺激的反应中起重要作用。最好理解的修饰是激活收缩系统所需的钙离子浓度的变化。通过肌钙蛋白（TNI）抑制亚基的cAMP敏感性磷酸化，激活的阈值浓度可以增加多达5倍，而不改变最大钙激活力。参与这种调节的蛋白激酶位于肌膜中。胆碱能刺激通过cGMP敏感性磷酸酶引起TNI去磷酸化。随着肌肉长度的增加，激活收缩所需的钙离子浓度也会降低。收缩蛋白的这种反应不涉及TNI的磷酸化。最大钙激活力的调节可以通过涉及位于细胞内的不同蛋白激酶的cAMP敏感性反应发生。该机制涉及至少两个连续反应，一个是cAMP控制的结合于细胞内膜的蛋白质的磷酸化以释放活性因子，第二个是活性因子与收缩蛋白质之间的相互作用以增强在钙存在下产生力的能力。肌球蛋白轻链的磷酸化由钙调蛋白调节激酶产生。肌球蛋白的轻链在完整心脏中部分磷酸化，但心脏的β-肾上腺素能刺激不会增加磷酸化的减少，同时增加收缩力。
Modulation of the functional properties of the contractile proteins of mammalian heart muscle plays a significant role in the response of the heart to beta-adrenergic stimulation. The most well understood modification is a change in the concentration of calcium ions that is required to activate the contractile system. By means of a cAMP-sensitive phosphorylation of the inhibitory subunit of troponin (TNI), the threshold concentration for activation can be increased as much as 5-fold without changing the maximum calcium-activated force. The protein kinase involved in this regulation is located in the sarcolemma. Cholinergic stimulation causes a dephosphorylation of TNI by a cGMP-sensitive phosphatase. The concentration of calcium ions required to activate contraction also decreases as muscle length increases. This response of the contractile proteins does not involve phosphorylation of TNI. Regulation of the maximum calcium-activated force can take place by a cAMP-sensitive reaction involving a different protein kinase that is located inside the cell. This mechanism involves at least two sequential reactions, one a cAMP-controlled phosphorylation of a protein bound to an intracellular membrane to release an active factor, and the second, an interaction between the active factor and the contractile proteins to enhance the capacity for generating force in the presence of calcium. Phosphorylation of the light chain of myosin is produced by a calmodulin-regulated kinase. The light chain of myosin is partially phosphorylated in the intact heart, but beta-adrenergic stimulation of the heart does not increase the decrease of phosphorylation in parallel with the increase in contractility.
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DOI：
--
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