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

Steven B. Marston*, O'Neal Copeland, Andrew E. Messer, Elyshia MacNamara, Kristen Nowak, Cleidiane G. Zampronio, Douglas G. Ward

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)189-197
Number of pages9
JournalJournal of Muscle Research and Cell Motility
Issue number3-4
Publication statusPublished - Aug 2013

Bibliographical note

Funding Information:
Acknowledgments We thank Jim Lin and Peter Gunning for advice with the isoform-specific antibodies and Robin Maytum for help with identifying tropomyosin isoforms. Human samples were provided by Prof William McKenna and Prof Cristobal Dos Remedios. This work was supported by grants from the British Heart Foundation. DGW and mass spectrometry equipment funded by Birmingham Science City.


  • Cardiac muscle
  • Cardiomyopathy
  • Heart failure
  • Isoforms
  • Phosphorylation
  • Tropomyosin

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Cell Biology


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