Properties of Cardiac Myosin with Cardiomyopathic Mutations in Essential Light Chains

The effects of cardiomyopathic mutations E56G, M149V, and E177G in the MYL3 gene encoding essential light chain of human ventricular myosin (ELCv), on the functional properties of cardiac myosin and its isolated head (myosin subfragment 1, S1) were investigated. Only the M149V mutation upregulated t...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2022-11, Vol.87 (11), p.1260-1267
Main Authors: Yampolskaya, Daria S., Kopylova, Galina V., Shchepkin, Daniil V., Bershitsky, Sergey Y., Matyushenko, Alexander M., Levitsky, Dmitrii I.
Format: Article
Language:English
Subjects:
Actin
Actin Cytoskeleton - metabolism
Actins - genetics
Actins - metabolism
Amino acids
Analysis
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Calcium ions
Cardiac Myosins - genetics
Cardiac Myosins - metabolism
Cardiomyopathy
Cardiomyopathy, Hypertrophic
Chains
Development and progression
Filaments
Gene mutations
Genetic aspects
Heart
Humans
Identification and classification
Life Sciences
Light
Light chains
Microbiology
Motility
Muscle contraction
Mutation
Myosin
Myosin Light Chains - genetics
Myosin Light Chains - metabolism
Myosins - genetics
Myosins - metabolism
Properties
Sliding
Velocity
Ventricle
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Summary:The effects of cardiomyopathic mutations E56G, M149V, and E177G in the MYL3 gene encoding essential light chain of human ventricular myosin (ELCv), on the functional properties of cardiac myosin and its isolated head (myosin subfragment 1, S1) were investigated. Only the M149V mutation upregulated the actin-activated ATPase activity of S1. All mutations significantly increased the Ca 2+ -sensitivity of the sliding velocity of thin filaments on the surface with immobilized myosin in the in vitro motility assay, while mutations E56G and M149V (but not E177G) reduced the sliding velocity of regulated thin filaments and F-actin filaments almost twice. Therefore, despite the fact that all studied mutations in ELCv are involved in the development of hypertrophic cardiomyopathy, the mechanisms of their influence on the actin–myosin interaction are different.
ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297922110050