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Expression of cardiac myosin light chain 2 during embryonic heart development in medaka fish, Oryzias latipes, and phylogenetic relationship with other myosin light chains
Author(s) -
Shimada Eriko,
Kinoshita Masato,
Murata Kenji
Publication year - 2009
Publication title -
development, growth and differentiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.864
H-Index - 66
eISSN - 1440-169X
pISSN - 0012-1592
DOI - 10.1111/j.1440-169x.2008.01074.x
Subject(s) - sinus venosus , biology , oryzias , heart development , zebrafish , cardiac function curve , atrium (architecture) , myh7 , myh6 , myosin , mesoderm , embryonic heart , anatomy , gene , myosin light chain kinase , medicine , microbiology and biotechnology , genetics , embryonic stem cell , heart failure , atrial fibrillation
Cardiac myosin light chain 2 (MLC‐2) plays a key role in heart development, contraction, and embryo and adult heart maintenance. In some animals, defects in the function of cardiac MLC‐2 cause hypertrophic cardiomyopathy. To illuminate the functions of cardiac MLC‐2 in embryonic heart formation and contraction, and into the evolution of MLC‐2, we characterized the expression and requirement for medaka cardiac MLC‐2 gene in the developing heart. Medaka cardiac MLC‐2 cDNA ( mcmlc2 ) was isolated and its gene expression pattern was determined. The mcmlc2 was found to be expressed in the bilateral cardiac mesoderm, the formed heart tube, and in both the differentiated ventricle and atrium. Knockdown of mcmlc2 function caused severe cardiac disorders, including edema in the atrium and sinus venosus. Using phylogenetic analysis, we found that physiological variations in the MLC‐2 molecules evolved due to amino acid changes in the Ca 2+ binding domain during molecular evolution. Our findings concerning the function and expression of mcmlc2 are nearly identical with those of other MLC‐2 genes, and our phylogenetic analysis suggests that during evolution, the variations in physiological function within the MLC‐2 gene family have arisen from a change in the amino acids in the Ca 2+ binding domain in the MLC‐2 molecule.