CpG site DNA methylation of the CCAAT/enhancer‐binding protein,alpha promoter in chicken lines divergently selected for fatness

CCAAT/enhancer‐binding protein (C/EBP), alpha (CEBPA) is a master regulator of adipogenesis and, together with peroxisome proliferator‐activated receptor gamma (PPARG), plays a critical role in adipocyte differentiation. Previous studies have demonstrated that CEBPA is regulated by DNA methylation and involved in the osteogenesis and adipogenesis of mouse C3H10T1/2 and bone marrow stromal cells. However, it is unclear whether CEBPA is regulated by DNA methylation in adipose tissues. Thus, the objectives of the present study were to investigate CpG site methylation in a 357‐bp CEBPA promoter region and to assess the correlation between promoter CpG site methylation and CEBPA gene expression in the abdominal adipose tissues of Northeast Agricultural University broiler lines divergently selected for abdominal fat content. The results showed that the methylation percentage of the analyzed CEBPA promoter region was significantly higher in lean broilers than in fat broilers at 2 weeks (80.3% vs. 43.4%, P < 0.0001), 3 weeks (95.4% vs. 74.0%, P < 0.0001) and 7 weeks of age (82.6% vs. 57.2%, P < 0.0001). Real‐time quantitative RT‐PCR analysis showed that CEBPA expression was significantly higher in the fat vs. the lean line at 2 weeks of age (P = 0.0013) but not at 3 or 7 weeks of age. The correlation analysis showed that only at 2 weeks of age was the methylation percentage negatively correlated with CEBPA expression (Pearson's r = ?0.8312, P = 0.0029). Of all seven tested CpGs, only two, the CpGs at ?1494 and ?1478 bp, displayed a significantly negative correlation with CEBPA mRNA expression. These results suggest that the CEBPA is methylated in adipose tissue and may regulate chicken early adipose development.     

Review: Enhancing intramuscular fat development via targeting fibro-adipogenic progenitor cells in meat animals

In the livestock industry, subcutaneous and visceral fat pads are considered as wastes, while intramuscular fat or marbling fat is essential for improving flavor and palatability of meat. Thus, strategies for optimizing fat deposition are needed. Intramuscular adipocytes provide sites for lipid deposition and marbling formation. In the present article, we addressed the origin and markers of intramuscular adipocyte progenitors – fibro-adipogenic progenitors (FAPs), as well as the latest progresses in mechanisms regulating the proliferation and differentiation of intramuscular FAPs. Finally, by targeting intramuscular FAPs, possible nutritional manipulations to improve marbling fat deposition are discussed. Despite recent progresses, the properties and regulation of intramuscular FAPs in livestock remain poorly understood and deserve further investigation.     

Matrix remodeling controls a nuclear lamin A/C-emerin network that directs Wnt-regulated stem cell fate

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Culture on Tissue‐Specific Coatings Derived from α‐Amylase‐Digested Decellularized Adipose Tissue Enhances the Proliferation and Adipogenic Differentiation of Human Adipose‐Derived Stromal Cells

While extracellular matrix (ECM)‐derived coatings have the potential to direct the response of cell populations in culture, there is a need to investigate the effects of ECM sourcing and processing on substrate bioactivity. To develop improved cell culture models for studying adipogenesis, the current study examines the proliferation and adipogenic differentiation of human adipose‐derived stem/stromal cells (ASCs) on a range of ECM‐derived coatings. Human decellularized adipose tissue (DAT) and commercially available bovine tendon collagen (COL) are digested with α‐amylase or pepsin to prepare the coatings. Physical characterization demonstrates that α‐amylase digestion generates softer, thicker, and more stable coatings, with a fibrous tissue‐like ultrastructure that is lost in the pepsin‐digested thin films. ASCs cultured on the α‐amylase‐digested ECM have a more spindle‐shaped morphology, and proliferation is significantly enhanced on the α‐amylase‐digested DAT coatings. Further, the α‐amylase‐digested DAT provides a more pro‐adipogenic microenvironment, based on higher levels of adipogenic gene expression, glycerol‐3‐phosphate dehydrogenase (GPDH) enzyme activity, and perilipin staining. Overall, this study supports α‐amylase digestion as a new approach for generating bioactive ECM‐derived coatings, and demonstrates tissue‐specific bioactivity using adipose‐derived ECM to enhance ASC proliferation and adipogenic differentiation.