TMT-based quantitative proteomics analysis reveals the key proteins related with the differentiation process of goat intramuscular adipocytes

Fig. 1. Differentiation of intramuscular preadipocytes induced in vitro. A Oil Red O staining and Bodipy staining of P_IMA and IMA. B The mRNA expression levels of key adipogenic regulatory genes detected by qRT-PCR. Data are shown as mean ± SD of four independent experiment. *P < 0.05; **P < 0.01

Fig. 2. Schematic diagram of the experimental flow. The P_IMA indicates the intramuscular preadipocytes and the IMA indicates the intramuscular adipocytes. The solid arrow shows the differentiation process from intramuscular preadipocytes to adipocytes, while the dotted arrows show the experimental flow. Diagram detailing the experiment including the principle, sample model establishment, data acquisition and data analysis

Fig. 3. Quality control results of the proteins. A The SDS-PAGE electrophoresis diagram. B Verification of the total protein quality, the abscissa represents the number of amino acid residues in the peptide, and the ordinate represents the number of peptides of this length. C Precursor ion tolerance, the abscissa represents the mass deviation, and the ordinate represents the precursor ion density distribution of the corresponding error. D Unique peptides number, slow increase of the curve means more unique peptides. E protein coverage, the abscissa represents the protein coverage interval, and the ordinate represents the number of proteins contained in the interval (F) Protein mass distribution, the abscissa represents the molecular weight of the identified protein, and the ordinate represents the number of the identified protein. A large molecular weight range indicates a wide range of identified proteins

Fig. 4. The analysis of identified proteins. A The volcano plot of identified proteins between P_IMA and IMA. B The distribution of up-regulated and down-regulated proteins in the DAPs that we obtained. C Hierarchical cluster analysis of relative protein content of the protein samples

Fig. 5. Annotations of the DAPs. A GO function enrichment analysis of the DAPs with the top 20 of biological processes. B Cellular components of the DAPs. C Molecular functions of the DAPs

Fig. 6. Enrichment analysis of the DAPs. A The DAPs were enriched in top 20 most significantly enriched KEGG pathways. B Cholesterol metabolism pathway. C Glucagon signaling pathway

Fig. 7. The protein-protein interactions network of DAPs. The bigger network nodes represent the higher the degree of protein interaction and the thickness of the connecting line between nodes represents different connectivity degree

Fig. 8. PRM protein expression quantities of the candidate proteins. Three biological replicates per protein. Data are shown as mean ± SD of three samples per protein. * P < 0.05; **P < 0.01