Fig. 4: TGFBI promotes HSC activation in a PDGFRβ dependent manner.
A Heat map of differentially expressed genes drawn based on RNA sequencing data. Samples were obtained from oil-treated WT mice, CCl4-induced WT mice, and Tgfbi−/− mice liver tissue lysates. B GO gene analysis of the differential proteins. C IF staining and quantitative analysis of TGFBI and PDGFRβ in human fibrotic liver tissue. D Correlation analysis of expression between Tgfbi and Pdgfrb in the Human Chronic Liver Disease database (n = 58 independent samples). E Western blot analysis of PDGFRβ expression in WT and Tgfbi−/− mice livers of CCl4 and BDL models. F RT-qPCR analysis of PDGF-B in WT and Tgfbi−/− mice livers of CCl4 and BDL models. G Relative mRNA levels of PDGFRβ in primary liver parenchymal cells, HSCs, and macrophages isolated from mice livers of CCl4 and BDL models (n = 3 independent experiments). H Western blot and RT-qPCR analysis of PDGFRβ expression in HSC treated with rTGFBI (200 ng/mL) for 6 h (n = 3 independent experiments). I Western blot and RT-qPCR analysis of α-SMA and PDGFRβ in HSC treated with rTGFBI (200 ng/mL) alone or in combination with integrin αvβ3 or αvβ5 neutralizing antibody for 6 h (n = 3 independent experiments). J Western blot and RT-qPCR analyses of PDGFRβ in HSC treated with rTGFBI (200 ng/mL) alone or in combination with the indicated inhibitors for 6 h (n = 3 independent experiments). Mice samples (n = 4–6 per group). Data were presented as the mean ± SDs; scale bars, 50 µm; *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001; ns not significant (Student’s t test).
