Ask about this productRelated genes to: MYBPC2 antibody
- Gene:
- MYBPC2 NIH gene
- Name:
- myosin binding protein C, fast type
- Previous symbol:
- -
- Synonyms:
- MYBPCF, MYBPC, MGC163408
- Chromosome:
- 19q13.33
- Locus Type:
- gene with protein product
- Date approved:
- 1993-12-15
- Date modifiied:
- 2014-11-19
Related products to: MYBPC2 antibody
Related articles to: MYBPC2 antibody
- BAG3 (Bcl-2 associated athanogene 3) is a multifunctional protein with pleiotropic effects in multiple cell types. Despite our knowledge of its role in cardiovascular disease, its specific role in endothelial cells (ECs) is unknown. The purpose of this study was to identify differences in the EC proteome of multiple tissues before and after cell specific deletion of Bag3. We hypothesized that BAG3 loss would uniquely alter the baseline proteome landscape of ECs in each tissue. Cdh5(PAC)-CreERT2;Bag3f/f mice received tamoxifen (KO; n=18) or vehicle (WT; n=18) and tissues (brain, heart, lung, and peripheral skeletal muscle-SkM) were collected for FACS of ECs from equal numbers of male and female mice at >22 weeks of age, followed by LC-MS/MS label-free proteomics. Initial comparisons of the WT proteomes between tissues revealed differential abundance of EC proteins (p<0.05), including: 367 brain v heart; 338 brain v lung; 570 brain v SkM; 400 heart v lung; 104 heart v SkM; and 489 lung v SkM. Additionally, the EC mitochondrial proteome was unique to each tissue of origin, with significantly (p<0.05) higher proportions dedicated to complexes I, III, IV and V, in heart compared to the other tissues. KO demonstrated the largest effect on SkM ECs, increasing 31 proteins (Mybpc2 Log2FC=4.81; PFKM Log2FC=3.02) and decreasing 65 (CDC42 Log2FC=-2.44; Prpf8 Log2FC=-2.24). Overall, these results demonstrate that the EC proteome of different tissues is unique and that the loss of BAG3 in these cells differentially alters a small proportion of the EC specific proteome. - Source: PubMed
Publication date: 2026/05/09
Terwilliger Zoë SLi FeifeiPentakota AnanyaZeczycki Tonya NGreen Thomas DKolasa MakenzieEdwards Nancy CGoldman Matthew PFisher-Wellman Kelsey HMcClung Joseph M - This study used proteomic analysis to evaluate how four cooking methods impact the quality of beef from Rikaze humped cattle. Conventional boiling, high-pressure boiling, roasting and frying produced varying numbers of differentially abundant proteins (DAPs) in and hind leg beef samples compared to the raw meat. Principal component analysis, hierarchical clustering and correlation analysis revealed 11 and 18 proteins significantly associated with meat tenderness and colour, respectively. Myosin heavy chain 7 (MYH7), myosin light chain 2 (MYL2) and myosin light chain 6B (MYL6B), involved in the sarcomere (GO:0030017) and cardiac muscle contraction (map04260) pathways were negatively correlated with tenderness, indicating that their decreased abundance contributes to improved tenderness after cooking. The cytoskeletal protein α-crystallin B chain (CRYAB) showed a positive correlation with shear force, suggesting a role in toughness. PGAM2, ALDOA and PKM, participating in ADP metabolism (GO:0046031) and glycolysis (map00010), influenced meat texture, while glycolytic enzymes ALDOA, CKM and PKM promoted changes in lightness (*). MYBPC2 and VDAC2 were negatively correlated with *. EEF1G, PGP, PPIA and PRDX2 were negatively correlated with redness (*), and DES was positively correlated with yellowness (*). Overall, wet-heat cooking altered mainly skeletal, heat-shock and cytoskeletal proteins and enhanced tenderness, while proteins related to energy metabolism and oxidative stress were closely linked to colour development. These key proteins could serve as potential biomarkers for predicting the eating quality of humped cattle beef and provide a basis for the development of high-value beef products. - Source: PubMed
Publication date: 2026/04/15
Zheng HaoZhao XiaolongLi JingWang PingLi SiminLi LiangLiu Zhendong - Neuregulin-1β (NRG1) improves cardiac output in heart failure patients, yet concerns remain that erythroblastic oncogene B (ErbB) activation may promote maladaptive hypertrophy, particularly during hemodynamic stress. We investigated how NRG1 influences structural, functional, and molecular remodeling during pressure overload. Male and female C57BL/6NRj mice underwent transverse aortic constriction (TAC) or sham surgery and received saline or recombinant NRG1 via osmotic minipumps or daily injection. In male mice, NRG1 increased ejection fraction at 1 and 4 wk after TAC. NRG1 accentuated TAC-induced concentric remodeling without increasing left ventricular weight or cardiomyocyte cross-sectional area. It markedly reduced fibrosis and macrophage infiltration and prevented progression toward early cardiac decompensation. NRG1 amplified TAC-induced and expression and also shifted toward their fetal profile. Transcriptomic analysis identified two novel NRG1-regulated genes: NRG1 reversed TAC-induced upregulation of the skeletal muscle gene myosin binding protein C () and induced the expression of Popeye domain-containing protein 2 (). Furthermore, NRG1 increased expression of and localization of connexin 43 at the intercalated disc, consistent with enhanced electrical coupling. In female mice, NRG1 increased systolic function and regulated similar molecular targets yet did not reduce the modest increase in fibrosis that was observed. In conclusion, our findings show that NRG1 promotes adaptive molecular and structural remodeling under pressure overload and enhances contractile performance without exacerbating hypertrophy. The identification of NRG1-responsive genes linked to contraction and conduction highlights potential mechanisms and supports further exploration of NRG1-based strategies for cardiac disease. Our study demonstrates that neuregulin-1β (NRG1) enhances systolic function during pressure overload while promoting adaptive remodeling without exacerbating hypertrophy. NRG1 regulates fetal gene programs in both sexes and reduces fibrosis in male mice. The identification of myosin binding protein C () and Popeye domain-containing protein 2 () as novel NRG1-responsive genes reveals previously unrecognized mechanisms underlying its cardioprotective effects. These findings support further investigation of NRG1-based therapeutic strategies and highlight potential sex-specific responses. - Source: PubMed
Publication date: 2026/02/03
Xu LifenAghagolzadeh ParisaMorandi ChristianWagner JasminLépine Lilia MSegers Vincent F Mde Keulenaer Gilles WBrink Marijke - Skeletal muscle plays a vital role in voluntary movement and locomotion. Fast-twitch muscle fibres are characterized by their rapid contraction kinetics, high-force generation and a distinct gene expression profile compared to slow-twitch fibres. These fibres have a predominant expression of fast skeletal myosin binding protein-C (fMyBP-C). The role of fMyBP-C in skeletal muscle disease and aging remains poorly understood. To address this, our study employs mouse models with fMyBP-C ablation to investigate its significance in skeletal muscle physiology. - Source: PubMed
Baby AkhilAnanthamohan KalyaniMcIntyre Brenna NNatesan SankarSong Taejeong - RBM20 is one of the genes predisposing to dilated cardiomyopathy (DCM). Several dozen variants associated with DCM have been reported so far. Variants in the arginine/serine-rich domain and the RNA recognition motif domain have been well studied, but the pathogenicity of variants outside of these areas remains unknown. A patient with the Q373fs-RBM20 variant without a typical DCM phenotype was identified in a sudden death cohort. The Q374fs-Rbm20 mouse model was generated to determine the significance of this variant. In mouse experiments, cardiac dysfunction, such as reduced fractional shortening and an extended duration of QRS and the corrected QT interval, were observed in Q374fs-Rbm20 mice by ultrasound echocardiography and electrocardiography. RNA sequencing analysis showed that Q374fs-Rbm20 mice had different splicing patterns, such as Ttn, Ldb3, Camk2d, Obscn, and Ryr2. Casq1, Mybpc2, and Myot expression was also upregulated in Q374fs-Rbm20 mice. A pathway analysis indicated the involvement of some of the 1770 differentially expressed genes in cytoplasmic ribosomal proteins, calcium regulation in cardiac cells, and striated muscle contraction. Our findings suggest that the Q374fs-Rbm20 variant changes gene splicing, affects genes involved in sarcomere structure and calcium handling genes, and presents with cardiac dysfunction. - Source: PubMed
Miura AyaYamamoto TakumaImasaka MaiSugimoto MichihikoNaito YoshiroNishiura HiroshiNishiguchi MinoriFunayama KazuhisaYamasu YuriKoyama AkihideTakatsuka HisakazuKuroyanagi HidehitoOhmuraya MasakiNishio Hajime