These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: The isoforms of α-actin and myosin affect the Ca2+ regulation of the actin-myosin interaction in the heart.
    Author: Shchepkin DV, Nikitina LV, Bershitsky SY, Kopylova GV.
    Journal: Biochem Biophys Res Commun; 2017 Aug 19; 490(2):324-329. PubMed ID: 28623140.
    Abstract:
    Myocardium of mammals contains a wide range of isoforms of proteins that provides contractile function of the heart. These are two isoforms of ventricular and two of atrial myosin, α- and β-tropomyosin, and two isoforms of α-actin: cardiac and skeletal. We believe that the difference in the amino acid sequence of α-actin can affect the calcium regulation of the actin-myosin interaction. To test this hypothesis, we investigated effects of the isoforms of α-actin, cardiac and skeletal, and the isoforms of cardiac myosin on the calcium regulation of the actin-myosin interaction in an in vitro motility assay using reconstructed regulated thin filaments. The results show that isoforms of α-actin and the ratio of α/β-chains of Tpm differently affect the calcium regulation of the actin-myosin interaction in myocardium in dependence on cardiac myosin isoforms.
    [Abstract] [Full Text] [Related] [New Search]