Fig. 1

G6PD upregulation promotes VSMC phenotypic switching, as determined by bioinformatics analysis of G6PD-interacting proteins. A Schematic diagram of the phenotypic switching of VSMCs induced by platelet-derived growth factor-BB (PDGF-BB) stimulation (20 ng/mL). Primary VSMCs were cultured from the thoracoabdominal aortas of male Sprague–Dawley rats, cultured for 3–5 generations and then stimulated with or without PDGF-BB. The whole-cell lysates were subjected to Western blot analysis. B Representative Western blot analysis and analysis of grayscale images of G6PD, PCNA, and VSMC contractile markers (α-actin and SM22α) in the lysates of VSMCs from A, which were treated with PDGF-BB for 0, 12, 24, 36 and 48 h, respectively. β-actin was used as an internal control. The data are presented as the relative fold change at 0 h (n = 3). C Representative Western blot analysis and analysis of grayscale images of G6PD, PCNA, α-actin, and SM22α in VSMCs stimulated with or without PDGF-BB in response to siG6PD. n = 3. D Venn diagrams displaying the number of unique and shared proteins identified by LC‒MS between control, PDGF-BB, and IgG VSMCs. E–G The functional categories based on gene ontology (GO) term enrichment and the signaling pathways based on KEGG enrichment analysis. biological process (E), cellular component (F), and molecular function (G). H Mass spectrometry analysis of G6PD and VDAC1 peptides after purification of G6PD-associated proteins. I, J Three peptides of VDAC1 identified by MS (I) and their positions in the 3D structure of VDAC1 (J). Statistical significance was determined using one-way ANOVA in (B) and two-tailed Student’s t tests in (C). *P < 0.05; **P < 0.01; ns, no significant difference