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Cardiac Myosin Binding Protein - DOAJ

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Last Updated: 16 August 2022

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Cardiac myosin binding protein-C phosphorylation modulates myofilament length-dependent activation

Following an increase in SL in 3SA skinned myocardium, relative to WT skinned myocardium, a decrease in myofilament Ca2+-sensitivity of force generation was revealed by a decrease in the length-dependent increase in myofilament Ca2+-sensitivity of force generation in the myofilament Ca2+-sensitivity of force generation, which led to a reduction in the longevity of myocardium, relative to myocardium In 3SA skinned myocardium and short and long SL, and before and after PKA treatment, the incidence and rate of XB detachment following stretch was dramatically reduced in 3SA skinned myocardium revealed in 3SA skinned myocardium was significantly reduced in 3SA skinned myocardium and saaed myocardium were significantly reduced in 3SA skinned myocardium following stretch In addition, the length-dependent acceleration of krel caused by lower SL that was seen in WT skinned myocardium was cut off in 3SA skinned myocardium. However, the magnitude of the entire delayed force phase, which can fall below initial pre-stretch stable-state levels, was significantly lower in 3SA skinned myocardium under all circumstances, due in large part to a reduced XB detachment in 3SA skinned myocardium relative to WT skinned myocardium.

Source link: https://doi.org/10.3389/fphys.2016.00038


Cardiac myosin binding protein C and MAP-kinase activating death domain-containing gene polymorphisms and diastolic heart failure.

In a human case-control study, the aim of the research was to determine the relationship between cardiac myosin binding protein C gene polymorphisms and diastolic heart failure. METHODS: The National Taiwan University Hospital and its affiliated hospital were enrolled in a total of 352 patients from 1752 consecutive patients. According to HapMap Han Chinese Beijing's China databank, we genotyped 12 single nucleotide polymorphisms to determine 100% of haplotype variation in all SNPs with minor allele frequencies of u2265 percent. According to a population attributable risk percentage of 12. 02%, the SNP with a minor allele frequency of 9. 4% had an odds ratio 2. 14 for the additive model and 2. 06 for the autosomal dominant model. CONCLUSION: We found a SNP among the tagging SNP set that was closely associated with early DHF in a Chinese population.

Source link: https://doi.org/10.1371/journal.pone.0035242


Cardiac Myosin‐Binding Protein C to Diagnose Acute Myocardial Infarction in the Pre‐Hospital Setting

Background The early triage is a key component of improved outcomes in patients with a suspected acute myocardial infarction. Methods and Results In a prospective, epidemiological cohort study, cMyC and high-sensitivity cardiac troponin T were retrospectively measured in blood samples obtained by ambulance-u2010-based paramedics. 98 [43;855] versus 17 [9;42] ng/L in patients with AMI was significantly higher than in patients with AMI than in other diagnoses. AMI's discrimination power for AMI was greater with cMyC than with high-sensitivity cardiac troponin T, according to T. After 2 hours of symptoms, cMyC hits 100% sensitivity and negative predictive value in patients, surpassing the previously published rule u2010out threshold. Conclusions: cMyC demonstrates improved diagnostic discrimination of AMI in patients undergoing blood draws as early as symptoms develop, which may lead to a significant reduction in the early triage of patients with suspected AMI.

Source link: https://doi.org/10.1161/JAHA.119.013152


Myomegalin is a novel A-kinase anchoring protein involved in the phosphorylation of cardiac myosin binding protein C

Cardiac Myosin Binding Protein-C and cardiac troponin I are hypertrophic cardiomyopathy-causing sarcomeric proteins that regulate contractility in response to PKA phosphorylation. We found isoform 4 of myomegalin as an interactor of this N-terminal cMyBPC region on a yeast 2-hybrid library screen using a trisphosphorylation mimic of cMyBPC's C1-C2 region. Using Y2H-based direct protein-protein interaction assays, we investigated this possibility and determined whether MMGL isoform 4 can interact with PKA regulatory subunits R1A and R2A. Under u03b2-adrenergic strain, we also found that quantitatively greater interaction between MMGL and cTNI occurs quantitatively more interaction occurs. Conclusions MMGL isoform 4's latest research identifies a novel function as an AKAP, and we find that it participates in the phosphorylation of cMyBPC and cTNI, as well as cTNI, making MMGL a key regulator of cardiac contractility.

Source link: https://doi.org/10.1186/1471-2121-12-18


Length-dependent changes in contractile dynamics are blunted due to cardiac myosin binding protein-C ablation

In part, a decrease in the radial distance between myosin heads and actin helps with increased cardiac contractile function with longer sarcomere length. Myosin heads relative to actin's pH is modulated by cardiac myosin binding protein-C, indicating that cMyBP-C plays a role in myocardium's length-dependent activation. Our results show that maximal force was not significantly different between KO and WT preparations, but that a length-dependent increase in pCa50 was attenuated in the KO preparations. pCa50 was not significantly different between WT and KO preparations at long SL, despite the fact that pCa50 was not significantly different between WT and KO preparations at long SL, whereas pCa50 was not significantly different between WT and KO preparations at short SL, whereas pCa50 was significantly different between WT and KO preparations at short SL, whereas pCa50 was not significantly different between WT and pCa50 was not significantly different between WT and KO plans at long SL, SL KO s at long SL, SL versus compared to SL vs SL, KO preparations compared KO preparations versus t KO, KO a50, KO plans at short SL vs t KO SL KO & KO SL, KO despite t KO SL a50, t KO SL & In the same way, KO preparations did not exhibit length-dependent changes in krel and kdf.

Source link: https://doi.org/10.3389/fphys.2014.00461


Cardiac Myosin Binding Protein-C Autoantibodies Are Potential Early Indicators of Cardiac Dysfunction and Patient Outcome in Acute Coronary Syndrome

Summary: The deposition and release of cardiac myosin binding protein-C can lead to an inflammatory reaction and autoantibody production. We figured out whether the presence of cMyBP-C-AAbs in cardiovascular disease patients was correlated with poor cardiac function. We conclude that cMyBP-C-AAbs may be early warning signs of deteriorating cardiac function and patient outcome in acute coronary syndrome patients prior to the infarction.

Source link: https://doi.org/10.1016/j.jacbts.2016.12.001


Cardiac Myosin Binding Protein-C Phosphorylation Mitigates Age-Related Cardiac Dysfunction

Summary: Cardiac's myosin binding protein-C phosphorylation prevents aging-related cardiac dysfunction. The phosphorylation of cMyBP-C decreased with ageing cardiac function and hypertrophy mimicking those found in hypophosphorylated cMyBP-C mice in hypophosphorylated cMyBP-C mice. Intact papillary muscle tests showed that cMyBP-C phosphorylation raised cross-bridge detachment rates as the underlying mechanism.

Source link: https://doi.org/10.1016/j.jacbts.2019.06.003


MMI‐0100 Inhibits Cardiac Fibrosis in a Mouse Model Overexpressing Cardiac Myosin Binding Protein C

BackgroundCardiac stress, as well as cMyBPu2010C mutations, can lead to the production of 1 such truncated protein fragment, a 40-kDa peptide fragment derived from the amino terminus of the cMyBP fragment derived from the amino terminus of cMyBP/u2010C peptide fragment derived from the amino terminus of cMyBP's 40-KDa peptide fragment peptide fragment peptide fragment peptide a c vy a u2010C c a peptide fragment peptide fragment peptide fragment peptide fragment peptide fragment peptide fragment peptide fragment derivington peptide fragment peptide fragment peptide fragment derivus derivu2010C peptide fragment peptide fragment derivers of peptide fragment peptide fragment peptide fragment peptide fragment peptide fragment peptide fragment peptide fragment peptide fragment peptide fragment peptide fragment peptid Fibrosis can be present in several cardiovascular disorders, and mitogen-u2013-activated protein kinase, u2013-activated protein kinase u2013 signaling has been implicated in a variety of fibrotic processes. U2013-activated protein kinase inhibition using the cell-u2010permeant peptide inhibitor MMI 20100100 is helpful in the case of acute myocardial infarction. Methods and ResultsNontransgenic and cMyBP>u20100100100 or PBS infused transgenic mice were given MMIu20100100 or PBS every 30 weeks for 30 weeks. U2013-activated protein kinase signaling by MMI-u20100100 treatment is helpful in the context of fibrotic cMyBPC40k disease.

Source link: https://doi.org/10.1161/JAHA.117.006590


Modulation of myosin by cardiac myosin binding protein-C peptides improves cardiac contractility in ex-vivo experimental heart failure models

In heart failure patients, reduced phosphorylation of cMyBP-C has been attributed to reduced contractility. Here, we used previously published cMyBP-C peptides 302A and 302S, surrogates of the federal phosphorylation site serine 302, as a way to determine the effects of modulating the dephosphorylation state of cMyBP-C on cardiac contraction and relaxation in experimental heart failure models in vitro. In particular, Peptide 302A may also raise the force redevelopment rate in papillary muscle fibers from cMyBP-CAAA mice. Both peptides elevated ATPase rates in myofibrils isolated from rats with myocardial infarction mice, but not from sham rats, according to the above findings. These findings, taken together, show that modulation of cMyBP-C dephosphorylation state can be a therapeutic strategy to increase myosin function, sarcomere contractility, and relaxation following an adverse cardiac event. Hence, targeting cMyBP-C could potentially boost overall cardiac function as a complement to standard-care drugs in HF patients.

Source link: https://doi.org/10.1038/s41598-022-08169-1


Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility

Myosin binding protein C was a perplexing yet integral part of the sarcomeric thick filament until it was discovered that genetic abnormalities in its corresponding gene is a frequent cause of hypertrophic cardiomyopathy in the sarcomeric thick filament. Deficiency or inadequacy in cMyBPC leads to severe cardiac arrest and tissue degeneration, culminating in cardiac hypertrophy and dilation, as well as reduced cardiac function and reduced cardiac output as a result of cystolic function and reduced cardiac output, as a result of impaired cardiac function and structural changes.

Source link: https://doi.org/10.24170/7-1-1966

* 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