Myosin Binding Protein C, Cardiac (MYBPC3) ELISA Kits

Cow (Bovine) Myosin Binding Protein C, Cardiac (MYBPC3) Interaktionspartner

1. N terminus of cMyBP-C interacts with F-actin through multiple distinct binding sites and that binding at one or more sites is reduced by phosphorylation

Mouse (Murine) Myosin Binding Protein C, Cardiac (MYBPC3) Interaktionspartner

1. The ablation of MYBPC3 and muscle-LIM protein protected the mice from developing the dilated cardiomyopathy phenotype.

2. these findings suggest the possibility that Fhod3 contributes to the pathogenesis of cMyBP-C-related cardiomyopathy and that Fhod3 is critically involved in cMyBP-C-mediated regulation of cardiac function via direct interaction.

3. Diltiazem recently showed promising beneficial effects in pre-clinical HCM, particularly in patients carrying MYBPC3 mutations.

4. the widely observed phenomenon of slowed force development in the presence of cMyBP-C may actually be a manifestation of cooperative binding of this protein to the thin filament.

5. autophagy is impaired in Mybpc3-targeted knockin mice

6. cMyBP-C lacking the S2 binding site is incorporated normally into the sarcomere, although systolic function is compromised.

7. these data indicate a robust proinflammatory response in DCM hearts, likely in response to cellular damage triggered by MYBPC3 mutation and resultant contractile dysfunction.

8. We provide evidence that haploinsufficiency and poison polypeptide hypotheses are disease mechanisms and that EHTs can be used as a platform to evaluate the direct impact of (newly identified) MYBPC3 gene variants.

9. These results support the proposal that cMyBP-C stabilises the thick filament and that the loss of cMyBP-C results in an untethering of myosin heads.

10. Crypts are a normal part of cardiac development but, along with the mitral valve and trabeculae, their developmental trajectory is altered by the presence of HCM truncating Mybpc3 gene mutation

11. that in the homozygous hypertrophic cardiomyopathy mouse model, beta-AR stimulation leads to preferential PKA phosphorylation of phospholamban over cardiac troponin I, resulting in an impaired inotropic and lusitropic response

12. Phosphorylation of MYBPC3 contributes to the genesis of ventricular wall geometry, linking myofilament biology with multiscale cardiac mechanics and myoarchitecture.

13. The cMyBP-C hypertrophic cardiomyopathy variant L348P enhances thin filament activation through an increased shift in tropomyosin position.

14. The contributions of cardiac myosin binding protein C and troponin I phosphorylation to beta-adrenergic enhancement of in vivo cardiac function

15. calcium levels at the peak of contraction would allow cMyBP-C to remain a potent contractile modulator, regardless of cMyBP-C's phosphorylation state

16. Phosphorylation reduced the level of molecular disorder and the distribution of C0C2 intramolecular distances became more compact, with probes flanking either the motif between C1 and C2 or the Pro/Ala-rich linker (PAL) between C0 and C1

17. the phosphorylation pattern of sMyBP-C is differentially regulated following reversible (i.e. fatigue) and non-reversible (i.e. age and disease) (patho)physiological stressors.

18. The proline/alanine-rich region and the C1 domain of cMyBP-C are not critical for normal cardiac contraction in mice.

19. the phosphorylation pattern of sMyBP-C is differentially regulated in response to age and disease, suggesting that phosphorylation plays important roles in these processes.

20. MYBPC3 mutations is elevated oxidative stress that corresponded to severe cardiac dysfunction, myocyte damage, and myocardial remodeling.

Human Myosin Binding Protein C, Cardiac (MYBPC3) Interaktionspartner

1. Compound heterozygous mutations in MYBPC3 were identified as a cause of severe familial hypertrophic cardiomyopathy.

2. The authors describe a pathogenic variant in MYBPC3 that shares with most truncating pathogenic variants in this gene 3 characteristics of : a late onset; a relatively benign clinical course in the young; and a high age-dependent penetrance.

3. Report age-at-death variations among MYBPC3 protein-truncating variant carriers in adult males.

4. Serum cMyC concentration is associated with myocardial hypertrophy, fibrosis and an increased risk of mortality in aortic stenosis.

5. A missense mutation in cardiac myosin-binding protein C linked to hypertrophic cardiomyopathy decreases stability of the fibronectin type III domain and results in substantially reduced mutant protein expression dissonant to transcript abundance.

6. Conflicting interpretations of pathogenicity have been reported for the Pro873His MYBPC3 variant described here. Our patient, presenting with two copies of the variant and devoid of a normal allele, progressed to end-stage heart failure, which supports the notion of a deleterious effect of this variant in the homozygous form.

7. Of the 52 hypertrophic cardiomyopathy patients 11 (21.2%) had MYBPC3 variants.

8. MYBPC3 does not seem to play a role in anthracycline induced cardiotoxicity.

9. Mutation in MYBPC3 was identified as Restrictive Cardiomyopathy - causing mutation.

10. pathogenic gene mutations in LMNA and MYBPC3 alter RNA splicing and may have a role in heart disease

11. MYBPC3 mutation carriers had a high frequency of ventricular arrhythmia and syncope. An absence of family history of sudden death (SD) and past history of syncope are useful prognostic factors in patients with hypertrophic cardiomyopathy. MYH7 and MYBPC3 mutations did not significantly influence prognosis compared to non-carriers. The patients with the MYBPC3 mutation should be closely followed for the possibility of SD.

12. Replacement Fibrosis was most abundantly present in the hearts with a MYBPC3 mutation that first presented with a Hypertrophic Cardiomyopathy.

13. Mutations in the gene MYBPC3 coding for cardiac myosin-binding protein-C (cMyBP-C), a multi-domain protein, are the most common cause of hypertrophic cardiomyopathy ..This molecular insight suggests that key HCM-causing mutations might significantly modify the native affinity required for the assembly of the domains in cMyBP-C, which is essential for normal cardiac function.

14. Our data demonstrate a critical role of the MLP/MyBP-C complex during early myoblast differentiation. Its absence in muscles with mutations or aberrant expression of MLP or MyBP-C could be directly implicated in the development of cardiac and skeletal myopathies.

15. Five of the 19 patients (26.3%) had either a pathogenic variant or a likely pathogenic variant in MYBPC3 (n=1), MYH7 (n=1), RYR2 (n=2), or TNNT2 (n=1). All five variants were missense variants that have been reported previously in patients with channelopathies or cardiomyopathies

16. Double heterozygotes for mutations in DSP and MYBPC3 showed a variable clinical presentation of arrhythmogenic cardiomyopathy and hypertrophic cardiomyopathy.

17. Data provide evidence that MYBPC3 mutations constitute the preeminent cause of hypertrophic cardiomyopathy (HCM) and that they are phenotypically indistinguishable from HCM caused by MYH7 mutations.

18. In children and young adults, a 2-parameter 12-lead A-ECG score is retrospectively significantly more sensitive and specific than pooled, age-specific conventional ECG criteria for detecting MYBPC3-HCM and in distinguishing such patients from healthy controls, including endurance-trained athletes.

19. mutations associated with a reduced super-relaxed state in hypertrophic cardiomyopathy

20. Study showed that CACNB2 is a possible candidate hypertrophy-modifying gene contributing to disease variability of MYBPC3-associated familial hypertrophic cardiomyopathy

Rabbit Myosin Binding Protein C, Cardiac (MYBPC3) Interaktionspartner

1. small es, CyrillicMyBP-C modulates interaction of myosin with actin