Fig. 2
From: The SF3B1R625H mutation promotes prolactinoma tumor progression through aberrant splicing of DLG1
Mutant SF3B1 promoted EMT phenotypes in prolactinoma. A GO functional enrichment analysis of DEGs in Sf3b1 mutant vs. wild-type GH3 cells. B Scanning electron microscopy (SEM; upper) and confocal images of the actin cytoskeleton stained with rhodamine–phalloidin (lower) of Sf3b1 wild-type and mutant GH3 cells; scale bar: 10 μm. C Scratch wound healing assays were performed using Sf3b1 wild-type and mutant GH3 cells; scale bar: 200 μm. Relative scratch widths are shown over time (n = 3; mean ± SD shown below; P values by Student’s test). D Kinetics of wound confluence over 96 h were analyzed using IncuCyte 2018B software (Essen Bioscience). The results are expressed as mean ± SD, n = 3. P values by two-way ANOVA; ****P < 0.0001. E DLG1, E-cadherin, N-cadherin, Vimentin, and Snail levels in Sf3b1 wild-type and mutant GH3 cells transduced with or without Dlg1-FLAG cDNA. G Immunofluorescence staining of E-cadherin and Vimentin in rat prolactinoma tumors stereotactically injected with Ad-null, Ad-SF3B1WT, and Ad-SF3B1R625H; scale bar: 50 μm. F Representative immunohistochemical staining for E-cadherin, N-cadherin, and Snail in SF3B1 mutant and wild-type human prolactinoma tumors; scale bar: 50 μm. H Venn diagram of the numbers of differentially spliced (q < 0.05; t test) and differentially expressed genes (q < 0.05; DESeq2) in SF3B1 mutant human prolactinoma and GH3 samples