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

被引:0
|
作者
Steven B. Marston
O’Neal Copeland
Andrew E. Messer
Elyshia MacNamara
Kristen Nowak
Cleidiane G. Zampronio
Douglas G. Ward
机构
[1] Imperial College London,Myocardial Function, NHLI
[2] University of Western Australia,Centre for Medical Research, WA Institute for Medical Research
[3] University of Birmingham,School of Biosciences
[4] University of Birmingham,School of Cancer Sciences
来源
Journal of Muscle Research and Cell Motility | 2013年 / 34卷
关键词
Cardiac muscle; Tropomyosin; Phosphorylation; Isoforms; Cardiomyopathy; Heart failure;
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学科分类号
摘要
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 α-tropomyosin was the only significant isoform expressed and that tropomyosin was 25–30 % phosphorylated at serine 283. Mass spectrometry confirmed directly that α-tropomyosin made up over 95 % of tropomyosin but also indicated the presence of up to 4 % κ-tropomyosin and much smaller amounts of β-, γ- and smooth β-tropomyosin and about 26 % phosphorylation. Neither the isoform distribution nor the level of phosphorylation changed significantly in the pathological heart muscle samples.
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页码:189 / 197
页数:8
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