Fig 2: ATP Binding Cassette transporter C1 (ABCC1) and G protein-coupled receptor (GPR55) are expressed in prostate cancer cells. Expression of ABCC1 and GPR55 was assessed by Western blot analysis of lysates from the indicated prostate cancer cell lines. Membranes were stripped and re-incubated with anti-tubulin to confirm equal loading. The whole blot images can be found in Figure S13.

Fig 3: PPP1R13L was involved in the TMEM44‐AS1/miR‐2355‐5p‐dependent impacts on GC cell resistance to 5‐FU. A) Venn plot showing the four data sets. B) OS and DFS of GC patients (n = 112) with different PPP1R13L expression levels in their tumors. C) Linear regression analysis was done to each individual PPP1R13L and miR‐2355‐5p expression, r = −0.3222, p < 0.0001. D) RIP experiments were performed using the Ago2 antibody, and specific primers were used to detect the enrichment of PPP1R13L. E) Dual‐luciferase gene reporter assays were used to assess the binding sites of PPP1R13L and miR‐2355‐5p. The relative luciferase activities were restrained in the HEK‐293 T cells co‐transfected with PPP1R13L‐wt and miR‐2355‐5p. F) Transfection efficiency of si‐PPP1R13L and oe‐PPP1R13L was assessed by RT‐qPCR and WB assays. G) The proliferative abilities of HGC 27/R and MKN‐45/R cells subject to si‐NC, si‐PPP1R13L, oe‐NC, or oe‐PPP1R13L transfection were detected through EdU assay. Scale bar, 20 µm. H) The cell apoptosis rate was determined for the two GC cell lines with 5‐FU resistance through flow cytometry. I) ABCC1, ABCG2, Caspase3, cleaved caspase‐3, Survivin, and GAPDH protein expression was measured in HGC‐27/R and MKN‐45/R cells by western blotting. J) P53, AIFM2, Bcl‐2, Bax, and GAPDH protein levels within HGC‐27/R and MKN‐45/R cells. 5 µg mL−1 5‐FU was used to treat cells for a 48‐h period before EdU assays, flow cytometric analysis, and protein extraction. Data are mean ± SD, n = 3. *P < 0.05, **P < 0.01, ***P < 0.001.

Fig 4: Inhibition of RAGE reduced the CSC stemness. (A, B) The sphere formation abilities were shown and quantified with pretreatment with anti-RAGE antibody for 2 h in the presence or absence of CML (50 μM) treatment. *, p < 0.05 as compared to the Control group. #, p < 0.05 as compared to the CML group. (C-H) The protein expression of stemness markers, including MRP1, MDR1, CD44, ALDH1A1, and NANOG was determined and quantified in the indicated cells. *, p < 0.05 as compared to the Control group. #, p < 0.05 as compared to the CML group.

Fig 5: Adriamycin‐resistant profiles of SCLC cells. (A) The growth inhibition rate of H69 and H69AR cells was measured by MTT assay after Adriamycin treatment. **P < 0.01 vs. control. (B) Cell apoptosis was determined by flow cytometry after Adriamycin treatment. (C) Quantitative real‐time PCR analysis of MDR1 expression levels. (D) Western blot analysis of the expression levels of MRP1 and P‐gp; GAPDH was used as a loading control. This part of the results was provided by the contractor. (E) The activity of P‐gp was detected by rhodamine‐123 accumulation assay, sclae bar was 50 μm. Student’s unpaired t‐test and one‐way ANOVA were used for statistical analysis. **P < 0.01, vs. H69 group. All results were shown as mean ± SD. Data were obtained from at least three independent experiments.