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. 2023 Mar 28;5(7):100746. doi: 10.1016/j.jhepr.2023.100746

Fig. 4.

Fig. 4

MSC-ex transport CAMKK1 into liver tissues and hepatocytes.

(A and B) Proteomic profiling of MSC-ex as compared with HFL1-Ex was analysed by LC-MS/MS. (A) Protein classification diagram and (B) Biological process enrichment analyses. (C) A partial list of proteins involved in metabolic biological processes. (D) CAMKK1 expression in MSC-ex was examined by immunoblotting. (E and F) Representative confocal microscopy images of CD81 (green) and CAMKK1 (red) colocalisation in L02 cells subjected to OPA stimulation (2.0 mM, 2:1 ratio) in combination with MSC-ex (800 μg/ml), deMSC-ex, or PBS treatment for 24 h (E) and liver sections of mice fed a normal chow diet (n = 10) or HFD and injected with PBS (n = 10), 5 mg/kg MSC-ex (n = 10), or 10 mg/kg MSC-ex (n = 10) (F); nuclei were labelled with DAPI (blue). Scale bars, 20 μm. CAMKK1, calcium/calmodulin-dependent protein kinase 1; de-MSC-ex, MSC-ex-free conditional medium supernatant; HFD, high-fat diet; HFL1-ex, foetal HFL1-derived exosomes; HFL1, human lung fibroblast 1; LC-MS/MS, liquid chromatography–tandem mass spectrometry; MSC-ex, MSC-derived exosomes; MSC, mesenchymal stem cell; OPA, oleate and palmitate.