蛋白激酶C介导的肌节蛋白磷酸化在心脏中起有害还是有益作用？
The role of protein kinase C-mediated phosphorylation of sarcomeric proteins in the heart-detrimental or beneficial?
作者信息
Kooij Viola, Stienen Ger J M, van der Velden Jolanda
机构信息
Division of Cardiology, Johns Hopkins Bayview Proteomics Center, Johns Hopkins University, 5200 Eastern Avenue, MFL Bldg, Center Tower, Rm 601, Baltimore, MD, 21224, USA.
Laboratory for Physiology, Institute for Cardiovascular Research, VU University Medical Center, Amsterdam, The Netherlands.
出版信息
Biophys Rev. 2011 Sep;3(3):107. doi: 10.1007/s12551-011-0050-y. Epub 2011 Jun 28.
Protein kinase C (PKC) is a family of serine/threonine protein kinases, and alterations have been found in PKC isoform expression and localization in the failing heart. These alterations in PKC activation levels influence the PKC-mediated phosphorylation status of cellular target proteins involved in Ca-handling and sarcomeric contraction. The differences observed in the effects due to PKC-mediated phosphorylation may underlie part of the contractile dysfunction observed in the failing heart. It is therefore important to establish the beneficial and detrimental effects of this kinase in the healthy and failing heart. The function of PKC has been studied intensively; however, the complexity of the regulation of this kinase makes the interpretation of the different effects difficult. The main focus of this review is the (patho)physiological impact of phosphorylation of sarcomeric proteins, myosin light chain-2, troponin I and T, desmin, myosin binding protein-C, and titin by PKC.
蛋白激酶C（PKC）是丝氨酸/苏氨酸蛋白激酶家族，在衰竭心脏中已发现PKC亚型的表达和定位存在改变。PKC激活水平的这些改变会影响PKC介导的参与钙处理和肌节收缩的细胞靶蛋白的磷酸化状态。PKC介导的磷酸化作用所观察到的效应差异可能是衰竭心脏中观察到的部分收缩功能障碍的基础。因此，确定这种激酶在健康心脏和衰竭心脏中的有益和有害作用非常重要。PKC的功能已得到深入研究；然而，这种激酶调节的复杂性使得对不同效应的解释变得困难。本综述的主要重点是PKC对肌节蛋白、肌球蛋白轻链-2、肌钙蛋白I和T、结蛋白、肌球蛋白结合蛋白-C和肌联蛋白磷酸化的（病理）生理影响。
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