Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati Medical Center, 231 Albert Sabin Way, Cincinnati, OH, 45267-0524, USA.
J Muscle Res Cell Motil. 2013 Aug;34(3-4):239-46. doi: 10.1007/s10974-013-9348-7. Epub 2013 Jun 22.
The focus of this review is on the very recent work we have conducted that addresses the molecular, morphological, and physiological significance of cardiac tropomyosin phosphorylation in the heart. We employ transgenic mice to address questions of how cardiomyocytes and the whole heart respond when the tropomyosin phosphorylation site (Ser283) is converted to a non-phosphorylatable amino acid (Ala). We address the phenotype of these mice during normal development and in response to acute cardiac stress (transaortic coarctation). In addition, we also examined how transgenic mice encoding the altered tropomyosin phosphorylation site (Ser283Ala) would respond to chronic cardiac stress through an encoded hypertrophic cardiomyopathy mutation (Glu180Gly). These studies are the first to address the in vivo significance of tropomyosin phosphorylation in the heart. In this review manuscript, we report the recent findings of these investigations.
这篇综述的重点是我们最近开展的工作，这些工作涉及心脏中的肌球蛋白轻链磷酸化在分子、形态和生理方面的意义。我们利用转基因小鼠来解决以下问题：当肌球蛋白轻链磷酸化位点（Ser283）被转化为非磷酸化氨基酸（Ala）时，心肌细胞和整个心脏会如何反应。我们在正常发育和急性心脏应激（升主动脉缩窄）时研究这些小鼠的表型。此外，我们还研究了编码改变的肌球蛋白轻链磷酸化位点（Ser283Ala）的转基因小鼠如何通过编码的肥厚型心肌病突变（Glu180Gly）来应对慢性心脏应激。这些研究首次在体内探讨了肌球蛋白轻链磷酸化在心脏中的意义。在本综述手稿中，我们报告了这些研究的最新发现。
