Abstract
As the master regulator of adipogenesis, peroxisome proliferator-activated receptor gamma (PPARG) is required for the accumulation of adipose tissue and hence contributes to obesity. A previous study showed that the substitution of +20A>G in PPARG changed the 7th amino acid from Asp to Gly, creating a mutant referred to as PPARG Asp7Gly. In this study, association analysis indicated that PPARG Asp7Gly was associated with lower body height, body weight and heart girth in cattle (P<0.05). Overexpression of PPARG in NIH3T3-L1 cells showed that the Asp7Gly substitution may cause a decrease in its adipogenic ability and the mRNA levels of CIDEC (cell death-inducing DFFA-like effector c) and aP2, which are all transcriptionally activated by PPARG during adipocyte differentiation. A dual-luciferase reporter assay was used to analyze the promoter activity of CIDEC. The results confirmed that the mutant PPARG exhibited weaker transcriptional activation activity than the wild type (P<0.05). These findings likely explain the associations between the Asp7Gly substitution and the body measurements. Additionally, the Asp7Gly mutation may be used in molecular marker assisted selection (MAS) of cattle breeding in the future.
Highlights
Adipose tissue is essential for whole body energy homeostasis
The results proved that the mutant peroxisome proliferator-activated receptor gamma (PPARG) was less capable of inducing adipogenesis under both growth conditions (Figure 1a) and differentiation conditions (Figure 1b) (P,0.05)
The PPARG1 isoform is expressed in most tissues, whereas PPARG2 is specific for adipose tissue, where it plays a key role in regulating adipogenic differentiation [17]
Summary
Adipose tissue is essential for whole body energy homeostasis. This tissue serves as a safe place for storing excess energy to avoid lipid buildup in other tissues, and it releases energy when other tissues are in need [1]. Three mutations under linkage disequilibrium were detected in the PPARG gene that were associated with lower body measurements in cattle [8]. In these three mutations, a substitution of +20A.G changed the 7th amino acid of PPARG from Asp to Gly, creating a mutant referred to as PPARG Asp7Gly. Sequence analysis showed that Asp7Gly in bovine PPARG and Pro12Ala in human PPARG were located within the same structural domain, which suggested that an understanding of the biological effects of Asp7Gly could help to explain the variability in cattle body measurements. This study may enhance our understanding of PPARG regulation and help animal scientists to develop genetic markers
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