ArticleJournal of biomedicine & biotechnology2011
Electrophoretic mobility of cardiac myosin heavy chain isoforms revisited: application of MALDI TOF/TOF analysis.
Article in Journal of biomedicine & biotechnology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Myosins and MyomiR Network in Patients with Obstructive Hypertrophic Cardiomyopathy.Biomedicines · 2022Article
- Effect of altered innervation and thyroid hormones on myosin heavy chain expression and fiber type transitions: a mini-review.Histochemistry and cell biology · 2015Review
- Remarkable heterogeneity in myosin heavy-chain composition of the human young masseter compared with young biceps brachii.Histochemistry and cell biology · 2012Article
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4 authors.
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Abstract
The expression of two cardiac myosin heavy chain (MyHC) isoforms in response to the thyroid status was studied in left ventricles (LVs) of Lewis rats. Major MyHC isoform in euthyroid and hyperthyroid LVs had a higher mobility on SDS-PAGE, whereas hypothyroid LVs predominantly contained a MyHC isoform with a lower mobility corresponding to that of the control soleus muscle. By comparing the MyHC profiles obtained under altered thyroid states together with the control soleus, we concluded that MyHCα was represented by the lower band with higher mobility and MyHCβ by the upper band. The identity of these two bands in SDS-PAGE gels was confirmed by western blot and mass spectrometry. Thus, in contrast to the literature data, we found that the MyHCα possessed a higher mobility rate than the MyHCβ isoform. Our data highlighted the importance of the careful identification of the MyHCα and MyHCβ isoforms analyzed by the SDS-PAGE.
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