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Cardiac Myosin Binding Protein - Europe PMC

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Last Updated: 16 August 2022

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Investigation of Mutant Cardiac Myosin-Binding Protein C gene (MYBPC3) & Potential Cardiomyopathy Risks Among Indian Athletes

Hypertrophic Cardiomyopathy is one of the leading causes of sudden cardiac death in South Asia, and mutation in the MYBPC3 gene has been attributed to an elevated risk of HCM and other cardiomyopathies. The prevalence of MYBPC3 d25bp variant and its familial inheritance among Indian athletes, as well as the presence of HCM genotype carrier athletes among the MYBPC3 d25bp genotype carrier athletes was investigated. Methods Oral mouthwash samples were collected from a total of 149 athletes and tested for MYBPC3 d25bp genotype, as well as family members of 03 MYBPC3 d25bp heterozygous genotype carrier athletes. Results MYBPC3 d25bp homozygous genotype 7. 07 out of 149 athletes with deleterious MYBPC3 d25bp genotype analysis revealed 07 out of 149 athletes with deleterious MYBPC3 d25bp genotype mutations, according to a MYBPC3 d25bp heterozygous genotype.

Source link: https://europepmc.org/article/PPR/PPR529984


Cardiac myosin binding protein-C palmitoylation is associated with increased myofilament affinity, reduced myofilament Ca 2+ sensitivity and is increased in ischaemic heart failure

Cardiac myosin binding protein-C is a vital regulator of cardiac contractility by its interactions with the thick and thin filament. The palmitoylated version of cMyBP-C was more resistant to salt extraction from the myofilament lattice than the non-palmoylated variety. Measurements suggest that c-MyBP-C palmitoylation reduces myofilament Ca 2+ sensitivity, with no change to maximum force or passive tension, with no change to maximum force or passive tension. Importantly, cMyBP-C palmitoylation levels have been reduced at the site of injury in a rabbit model of heart disease, but they have increased in samples from patients with ischaemic heart failure. Both the cMyBP-C palmitoylation and C651 cysteines are required for cMyBP-C palmitoylation, according to a study at these locations, indicating an interplay between the two systems. We found that structural and contractile proteins within the myofilament lattice are palmitoylated, allowing for cardiac contractile function.

Source link: https://europepmc.org/article/PPR/PPR508246


A 0/1h-algorithm using cardiac myosin-binding protein C for early diagnosis of myocardial infarction.

The early detection of non-ST-elevation myocardial infarction by Aims Cardiac's myosin-binding protein C showed excellent diagnostic sensitivity. Methods and findings The research was conducted at presentation and after 1 h in a blinded fashion in a prospective international diagnostic research involving patients with suspected NSTEMI to the emergency department. cMyC 0 h cMyC concentrations below 18 ng/L or 0 h rise s as a result of increase 4 ng/L, the optimal derived 0/1h-algorithm determined-out NSTEMI with cMyC 0 h. The increase of u226515 ng/L was recorded in an adequate way. Negative predictive value for NSTEMI was 99. 6% [95% confidence interval 98. 9-100%]; positive predictive value 71. 1%] Conclusion The cMyC 0/1h-algorithm achieved excellent safety and determined a greater proportion of patients eligible for direct rule-out or rule-in based on a single measurement rather than the ESC 0/1h-algorithm using hs-CTnT/I.

Source link: https://europepmc.org/article/MED/35149868


Nanosurfer assay dissects β-cardiac myosin and cardiac myosin-binding protein C interactions.

By putative interactions with the myosin S2 tail and/or the thin filament, Cardiac's myosin-binding protein C modulates cardiac contractionality. Synthetic thick filaments were produced using recombinant human u03b2-cardiac myosin subfragments attached to DNA nanotubes, with 14- or 28-nm spacing in native thick filaments, corresponding to 14. 3-nm myosin spacing in native thick filaments. The nanosurfer assay contains DNA nanotubes that have been added to the in vitro motility assay, ensuring that myosins on the motility surface successfully deliver thin filaments to the DNA nanotubes, thus raising thin filament gliding probability on the DNA nanotubes. Every 14 nm, we investigated the effects of cMyBP-C on thin filament motility by alternating HMM and cMyBP-C N-terminal fragments on nanotubes. To communicate with cMyBP-C, similar inhibitions occurred using the myosin S1 model, but it lacks the myosin S2 region, which is unable to communicate with cMyBP-C, implying that the cMyBP-C N terminus must collaborate with other myosin head domains and/or actin to reduce thin filament velocity.

Source link: https://europepmc.org/article/MED/35591788

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions