Open AccessEffects of Total Replacement of Atrial Myosin Light Chain-2 With the Ventricular Isoform in Atrial Myocytes of Transgenic Mice
Author(s) -
Corinn M. Pawloski-Dahm,
Guojie Song,
Darryl L. Kirkpatrick,
Joe Palermo,
James Gulick,
Gerald W. Dorn,
Jeffrey Robbins,
Richard A. Walsh
Publication year - 1998
Publication title -
circulation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.795
H-Index - 607
eISSN - 1524-4539
pISSN - 0009-7322
DOI - 10.1161/01.cir.97.15.1508
Subject(s) - myosin light chain kinase , myosin , medicine , myocyte , contractility , transgene , myh7 , myh6 , calcium , genetically modified mouse , gene isoform , endocrinology , contraction (grammar) , biophysics , cardiology , microbiology and biotechnology , chemistry , biology , biochemistry , gene
In contrast to their well-known and critical role in excitation-contraction coupling of vascular smooth muscle, the effects of the myosin light chains on cardiomyocyte mechanics are poorly understood. Accordingly, we designed the present experiment to define the cardiac chamber-specific functional effects of the ventricular isoform of the regulatory myosin light chain (MLC2v).
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