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Integration of Cardiac Actin Mutants Causing Hypertrophic (p.A295S) and Dilated Cardiomyopathy (p.R312H and p.E361G) into Cellular Structures. | LitMetric

AI Article Synopsis

  • - The study focuses on three human mutant cardiac α-actin variants (p.A295S, p.R312H, p.E361G) associated with different types of cardiomyopathy, which were produced and purified using an insect cell system to study their properties and interactions with proteins involved in heart cell development.
  • - These cardiac actin variants exhibited varying sensitivities to calcium stimulation and interacted differently with actin-binding proteins like Arp2/3 complex and mDia3, influencing their polymerization rates and overall behavior.
  • - The research also explored how the MICAL-1 enzyme affected these actins by modifying their structure, leading to varied rates of de-polymerization, and examined how these actin variants incorporated into

Article Abstract

The human mutant cardiac α-actins p.A295S or p.R312H and p.E361G, correlated with hypertrophic or dilated cardiomyopathy, respectively, were expressed by the insect cell system and purified to homogeneity. The purified cardiac actins maintained their native state but showed differences in Ca-sensitivity to stimulate the myosin-subfragment1 ATPase. Here we analyzed the interactions of these c-actins with actin-binding and -modifying proteins implicated in cardiomyocyte differentiation. We demonstrate that Arp2/3 complex and the formin mDia3 stimulated the polymerization rate and extent of the c-actins, albeit to different degrees. In addition, we tested the effect of the MICAL-1 monooxygenase, which modifies the supramolecular actin organization during development and adaptive processes. MICAL-1 oxidized these c-actin variants and induced their de-polymerization, albeit at different rates. Transfection experiments using MDCK cells demonstrated the preferable incorporation of wild type and p.A295S c-actins into their microfilament system but of p.R312H and p.E361G actins into the submembranous actin network. Transduction of neonatal rat cardiomyocytes with adenoviral constructs coding HA-tagged c-actin variants showed their incorporation into microfilaments after one day in culture and thereafter into thin filaments of nascent sarcomeric structures at their plus ends (Z-lines) except the p.E361G mutant, which preferentially incorporated at the minus ends.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8301065PMC
http://dx.doi.org/10.3390/antiox10071082DOI Listing

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