Fig 2: Inhibition of lysosomal and NF-κB p65 signaling pathways led to proliferation and decrease in expression level of PLD2 in CRC cell lines. (A) Inhibition of the lysosomal pathway with CQ (50 mM); PLD2 first declined and then increased with the lowest point observed at 4 h. (B and C) Inhibition of the lysosomal pathway (CQ; 50 Mm, 4 h) and NF-κB signaling pathway (PDTC; 10 mM; 2 h) led to a significant reduction in the expression level of PLD2 compared with the control group. (D) Co-immunoprecipitation of NF-κB with PLD2, CD147, GST3, MLH1 in HCT116/DLD-1, HCT116-R/DLD-1-R and HCT116L2A/DLD-1L2A cells. The data represent the mean ± standard deviation from three independent experiments. *P<0.05. PLD2, phospholipase D2; R, resistance; CRC, colorectal cancer; CQ, clioquinol; PDTC, pyrrolidine dithiocarbamate; CD, cluster of differentiation; LRP1, lung resistance-related protein 1; PGP, P-glycoprotein 1; GST, glutathione S-transferase; MLH1, MutL homologue 1; IP, immunoprecipitation.

Fig 3: XG1LenRes demonstrated altered CD147 expression and impaired lenalidomide-mediated downregulation of IRF4 (truncated form).a Immunoblotting of XG1 and XG1LenRes demonstrated that XG1LenRes has normal CRBN expression and has an altered CD147 expression compared with XG1. b Introduction of exogenous CRBN into XG1LenRes did not restore its sensitivity. c In addition to a full-length (f) IRF4, a short (s) IRF4 protein was detected from both XG1 and XG1LenRes. Upon lenalidomide treatment, shorted IRF4 in XG1LenRes was not downregulated as well as in XG1. d Mate pair sequencing data suggested that the IRF4 gene in both XG1 and XG1LenRes has an inversion mutation, which is likely to produce a short C-terminal-truncated IRF4 protein

Fig 4: Immunohistochemistry staining pattern of EMMPRIN in glioma (×200). ANegative staining (−) of EMMPRIN, figure was taken from grade III glioma; B Weak positive staining (+) of EMMPRIN, figure was taken from grade II glioma; C Moderate positive staining (++) of EMMPRIN, figure was taken from grade II glioma; D Strong positive staining (+++) of EMMPRIN, figure was taken from grade IV glioma.

Fig 5: CD147 interacts with multiple transmembrane proteins beyond its interaction with MCTsA. Schematic representation of the cross-linking/pull-down strategy utilized here for the identification of CD147 interacting partners through MS analysis. B. Classification of CD147 interactions monitored via a cross-linking/MS approach. GO terms analysis for all 153 proteins identified. Only terms with a p-value < 0.05 are listed. Western blot analysis further validates CD147 interacting partners identified via cross-linking/MS. Arrows indicate the location of the correct molecular weight for each identified proteins. Cross-linked fractions are also marked. C. CD147 knockdown leads to downregulation of PMCA1. ß-actin provided a loading control. D. Western blot validation of CD147-specific interactions identified via cross-linking/pull-downs. Arrows indicate the location of the correct molecular weight bands for each identified proteins. Cross-linked fractions are also marked.