Tropomyosin isoform expression and phosphorylation in the human heart in health and disease

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• 作者：Steven B. Marston (1) <br> Oeal Copeland (1) <br> Andrew E. Messer (1) <br> Elyshia MacNamara (2) <br> Kristen Nowak (2) <br> Cleidiane G. Zampronio (3) <br> Douglas G. Ward (4) <br>
• 关键词：Cardiac muscle ; Tropomyosin ; Phosphorylation ; Isoforms ; Cardiomyopathy ; Heart failure
• 刊名：Journal of Muscle Research and Cell Motility
• 出版年：2013
• 出版时间：August 2013
• 年：2013
• 卷：34
• 期：3-4
• 页码：189-197
• 全文大小：
• 作者单位：Steven B. Marston (1) <br> Oeal Copeland (1) <br> Andrew E. Messer (1) <br> Elyshia MacNamara (2) <br> Kristen Nowak (2) <br> Cleidiane G. Zampronio (3) <br> Douglas G. Ward (4) <br><br>1. Myocardial Function, NHLI, Imperial College London, London, W12 0NN, UK <br> 2. Centre for Medical Research, WA Institute for Medical Research, University of Western Australia, Nedlands, WA, Australia <br> 3. School of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK <br> 4. School of Cancer Sciences, University of Birmingham, Birmingham, B15 2TT, UK <br>
• ISSN：1573-2657

文摘

We determined the isoforms of tropomyosin expressed and the level of tropomyosin phosphorylation in donor, end-stage failing and hypertrophic obstructive cardiomyopathy samples of human heart muscle. Western blots and isoform-specific antibodies showed that tropomyosin was the only significant isoform expressed and that tropomyosin was 250% phosphorylated at serine 283. Mass spectrometry confirmed directly that tropomyosin made up over 95% of tropomyosin but also indicated the presence of up to 4% tropomyosin and much smaller amounts of , and smooth tropomyosin and about 26% phosphorylation. Neither the isoform distribution nor the level of phosphorylation changed significantly in the pathological heart muscle samples.