Dietary Lecithin Decreases Skeletal Muscle COL1A1 and COL3A1 Gene Expression in Finisher Gilts

Abstract

Simple SummaryIn this study, the effect of dietary lecithin on skeletal muscle gene expression of collagen precursors and enzymes was investigated in gilts. Thirty-six finisher gilts were fed with diets containing either 0, 4, 20 or 80 g/kg soybean lecithin for six weeks. Then, rectus abdominis muscle was sampled and analyzed for eight genes involved in collagen synthesis and degradation (COL1A1, COL3A1, MMP-1, MMP-13, TIMP-1, TIMP-3, lysyl oxidase and α-subunit P4H) using quantitative real-time PCR. The results showed that lecithin down-regulated COL1A1 and COL3A1 as well as tended to down-regulate α-subunit P4H expression.AbstractThe purpose of this study was to investigate the effect of dietary lecithin on skeletal muscle gene expression of collagen precursors and enzymes involved in collagen synthesis and degradation. Finisher gilts with an average start weight of 55.9 ± 2.22 kg were fed diets containing either 0, 4, 20 or 80 g/kg soybean lecithin prior to harvest for six weeks and the rectus abdominis muscle gene expression profile was analyzed by quantitative real-time PCR. Lecithin treatment down-regulated Type I (α1) procollagen (COL1A1) and Type III (α1) procollagen (COL3A1) mRNA expression (p < 0.05, respectively), indicating a decrease in the precursors for collagen synthesis. The α-subunit of prolyl 4-hydroxylase (P4H) mRNA expression also tended to be down-regulated (p = 0.056), indicating a decrease in collagen synthesis. Decreased matrix metalloproteinase-1 (MMP-1) mRNA expression may reflect a positive regulatory response to the reduced collagen synthesis in muscle from the pigs fed lecithin (p = 0.035). Lecithin had no effect on tissue inhibitor metalloproteinase-1 (TIMP-1), matrix metalloproteinase-13 (MMP-13) and lysyl oxidase mRNA expression. In conclusion, lecithin down-regulated COL1A1 and COL3A1 as well as tended to down-regulate α-subunit P4H expression. However, determination of muscle collagen content and solubility are required to support the gene functions.

Plant-Based, Hydrogel-like Microfibers as an Antioxidant Platform for Skin Burn Healing

“…Moreover, the stimulation of collagen seems to be dependent exclusively on the VitC since the expression of col-1a was null for ZPC0/ZPC0 CL compared to the other samples bearing the bioactive molecule. This result is even more significant considering that pectin and soy lecithin (the two water-soluble microfibers components) were observed to be involved in a decrease of collagen mRNA levels in normal human dermal fibroblast cells and skeletal muscle cells , Furthermore, ZPC3 and ZPC3 CL have shown a significant 25-fold and 5-fold increase, respectively, in col-1 relative gene expression compared to the control (Figure c,d).…”

Transcriptomic Profiling of Subcutaneous Backfat in Castrated and Intact Alentejano Pigs Finished Outdoors with Commercial and Fiber-Rich Diets

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Genome-Wide Selection Signal Analysis to Investigate Wide Genomic Heredity Divergence between Eurasian Wild Boar and Domestic Pig

“…The present study also identified CDGs that are associated with excellent meat quality in Chinese local pigs, such as the SNP variant at CACNA2D1 intron, which was found to be significantly correlated with economic phenotypes, including leg gluteus muscle conductivity and eye muscle area (EMA) [ 33 ]. In addition, DECR1 expression was found to be related to pork quality [ 12 ], and COL3A1 was confirmed to be involved in the formation of collagen in the muscles [ 34 ].…”