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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Farman, Gerrie P. Muthu, Priya Kazmierczak, Katarzyna Szczesna-Cordary, Danuta Moore, Jeffrey R. |
| Description | Author Affiliation: Farman GP ( Department of Physiology and Biophysics, Boston University, Boston, Massachusetts); Muthu P ( Department of Molecular and Cellular Pharmacology, University of Miami, Miami, Florida.); Kazmierczak K ( Department of Molecular and Cellular Pharmacology, University of Miami, Miami, Florida.); Szczesna-Cordary D ( Department of Molecular and Cellular Pharmacology, University of Miami, Miami, Florida.); Moore JR ( Department of Physiology and Biophysics, Boston University, Boston, Massachusetts) |
| Abstract | Familial hypertrophic cardiomyopathy (HCM) is associated with mutations in sarcomeric proteins, including the myosin regulatory light chain (RLC). Here we studied the impact of three HCM mutations located in the NH2 terminus of the RLC on the molecular mechanism of ß-myosin heavy chain (MHC) cross-bridge mechanics using the in vitro motility assay. To generate mutant ß-myosin, native RLC was depleted from porcine cardiac MHC and reconstituted with mutant (A13T, F18L, and E22K) or wild-type (WT) human cardiac RLC. We characterized the mutant myosin force and motion generation capability in the presence of a frictional load. Compared with WT, all three mutants exhibited reductions in maximal actin filament velocity when tested under low or no frictional load. The actin-activated ATPase showed no significant difference between WT and HCM-mutant-reconstituted myosins. The decrease in velocity has been attributed to a significantly increased duty cycle, as was measured by the dependence of actin sliding velocity on myosin surface density, for all three mutant myosins. These results demonstrate a mutation-induced alteration in acto-myosin interactions that may contribute to the pathogenesis of HCM. |
| File Format | HTM / HTML |
| ISSN | 87507587 |
| e-ISSN | 15221601 |
| DOI | 10.1152/japplphysiol.00798.2014 |
| Journal | Journal of Applied Physiology |
| Issue Number | 12 |
| Volume Number | 117 |
| Language | English |
| Publisher | American Physiological Society |
| Publisher Date | 2014-12-15 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Discipline Physiology Cardiac Myosins Metabolism Cardiomyopathy, Hypertrophic, Familial Genetics Mutation Myocardial Contraction Myocytes, Cardiac Myosin Heavy Chains Myosin Light Chains Animals Physiopathology Genetic Predisposition To Disease Kinetics Phenotype Protein Binding Protein Interaction Domains And Motifs Recombinant Proteins Swine Research Support, N.i.h., Extramural |
| Content Type | Text |
| Resource Type | Article |
| Subject | Physiology Physiology (medical) Sports Science |
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