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Additional file 2: Figure S7. The original figure of western blots of Fig. 1b. The red box indicated the representative bands of protein levels in Fig. 1b. Protein expression of HIF-1α in normal and OSCC patient tissues by western blotting. GAPDH was used as the internal control. Additional file 2: Figure S8. The original figure of western blots of Figure 1e. The red box indicated the representative bands of protein levels in Figure 1e. Protein expression of HIF-1α and p53 in OSCC cell lines by western blotting. GAPDH was used as the internal control. Additional file 2: Figure S9. The original figure of western blots of Figure 2a. The red box indicated the representative bands of protein levels in Fig. 2a. Protein expression of HIF-1α, E-cad, Snail, Par3, TJP1 and claudin in HSC-2 cell line under normoxia or hypoxic conditions by western blotting. GAPDH was used as the internal control. Additional file 2: Figure S10. The original figure of western blots of Figure 2a. The red box indicated the representative bands of protein levels in Fig. 2a. Protein expression of HIF-1α, E-cad, Snail, Par3, TJP1 and claudin in SCC-9 cell line under normoxia or hypoxic conditions by western blotting. GAPDH was used as the internal control. Additional file 2: Figure S11. The original figure of western blots of Figure 2a. The red box indicated the representative bands of protein levels in Fig. 2a. Protein expression of HIF-1α, E-cad, Snail, Par3, TJP1 and claudin in SCC-25 cell line under normoxia or hypoxic conditions by western blotting. GAPDH was used as the internal control. Additional file 2: Figure S12. The original figure of western blots of Figure 3a. The red box indicated the representative bands of protein levels in Fig. 3a. Protein expression of HIF-1α, Par3, TJP1 and Par6b in HSC-2 cell line treated with siRNA-HIF-1α or control siRNA by western blotting. GAPDH was used as the internal control. Additional file 2: Figure S13. The original figure of western blots of Figure 3a. The red box indicated the representative bands of protein levels in Fig. 3a. Protein expression of HIF-1α, Par3, TJP1 and Par6b in SCC-9 cell line treated with siRNA-HIF-1α or control siRNA by western blotting. GAPDH was used as the internal control. Additional file 2: Figure S14. The original figure of western blots of Figure 3a. The red box indicated the representative bands of protein levels in Fig. 3a. Protein expression of HIF-1α, Par3, TJP1 and Par6b in SCC-25 cell line treated with siRNA-HIF-1α or control siRNA by western blotting. GAPDH was used as the internal control. Additional file 2: Figure S15. The original figure of western blots of Figure 4a. The red box indicated the representative bands of protein levels in Fig. 4a. Protein expression of Par3, TJP1 Par6b and aPKC in HSC-2 cell line treated with siRNA-Par3 or control siRNA by western blotting. GAPDH was used as the internal control. Additional file 2: Figure S16. The original figure of western blots of Figure 4a. The red box indicated the representative bands of protein levels in Fig. 4a. Protein expression of Par3, TJP1 Par6b and aPKC in SCC-9 cell line treated with siRNA-Par3 or control siRNA by western blotting. GAPDH was used as the internal control. Additional file 2: Figure S17. The original figure of western blots of Figure 4a. The red box indicated the representative bands of protein levels in Fig. 4a. Protein expression of Par3, TJP1 Par6b and aPKC in SCC-25 cell line treated with siRNA-Par3 or control siRNA by western blotting. GAPDH was used as the internal control.

Additional file 1: Table S1. Clinicopathological features of 29 patients with OSCC, and association between Par3 expression these variables. Additional file 1: Fig. S1. The expression pattern of HIF-1α in OSCC. The IHC scores were classified as negative, low and high expression. Additional file 1: Fig. S2. The expression of HIF-1α has nothing to do with tumor growth in vivo. HSC-2 cells treated with or without hypoxic conditions and siRNA-HIF-1α were subcutaneously injected into the BALB/c nude mice. a The image and b growth curve of tumor volume was measured in mice xenografts. Additional file 1: Fig. S3. The expression of Par3 is negatively correlated with metastatic properties of OSCC. The mRNA expression of Par3 were significantly increased in patient cohort with a HNSC and b OSCC, compared with paired normal tissue. Results were retrieved from TCGA and GSE37991, respectively. Each lines represented paired adjacent normal tissues. * indicates significance differences between tumor and normal tissues (P < 0.05). c The mRNA and d protein expression of Par3 were decreased in metastatic patient cohort and tissues of OSCC, compared with non-metastatic OSCC tissues. Patient cohort was retrieved from GSE2880 (n = 14). The black box indicates cropped fields of original images. * indicates significance differences between metastatic and non-metastatic OSCC (P < 0.05). Additional file 1: Fig. S4. The expression of Par3 has nothing to do with tumor growth in vivo. HSC-2 cells treated with or without siRNA-Par3 were subcutaneously injected into the BALB/c nude mice. c The image and d growth curve of tumor volume was measured in mice xenografts. Additional file 1: Fig. S5. Morphologic changes are reflected in invasion ability of the OSCC cell lines. a The image represents the phase-contrast images of cell morphology of HSC-2, SCC-9 and SCC-25 cell lines. Scale bar, 100 μm. b the image represents the invaded number of HSC-2, SCC-9 and SCC-25 cells from upper chamber by matrigel invasion assay. Additional file 1: Fig. S6. A graphic model for the role of hypoxic conditions in OSCC. Hypoxic conditions are involved with disruption of tight junctions and promotes the metastatic properties of OSCC by Par3.

Additional file 1. Supplementary Table 1. Primer sequences using quantitative real time polymerase chain reaction. Supplementary Table 2. Comparison of follicle counts after transplantation in vivo. Supplementary Fig. 1. The level of PDGF in PRL-1 compared to Na��ve. (a-b) The intensity of PDGF-BB was expressed dot blot by cytokine array and Image J program. The data were representative of three independent experiments and expressed as means S.D. Significant indicates * p < 0.05, Na��ve vs. PRL-1. Supplementary Fig. 2. Effect of PRL-1 on PDGF downstream in ovary of OVX rats. (a) The mRNA expression of PKC�� in ovary was analyzed by qRT-PCR. (b) The gene expression and localization of p-Src in ovary were analyzed by IF staining. (c) The mRNA expression of VEGF and (d) VEGFR2 in ovary were analyzed by qRT-PCR. (e) The gene expression of VEGFR in ovary was analyzed by western blot. The data were representative of three independent experiments and expressed as means S.D. Significant indicates * p < 0.05, Normal vs. NTx, NTx vs. Tx (Naive and PRL-1), Naive vs. PRL-1 in each time point. Supplementary Fig. 3. Effect of PRL-1 on angiogenesis in ovary of OVX rats. (a) The mRNA expression of HIF1�� and (b) Endoglin in ovary were analyzed by qRT-PCR. (c) The gene expression of HIF1�� and (d) Endoglin in ovary were analyzed by western blot. The data were representative of three independent experiments and expressed as means S.D. Significant indicates * p < 0.05, Normal vs. NTx, NTx vs. Tx (Naive and PRL-1), Naive vs. PRL-1 in each time point.

Additional file 1. Supplementary Fig. 1 Optimal concentration of thapsigargin (TG) in WB-F344. a TG was treated with each concentration (100, 500, and 1000 nM) for 6, 12, 24, and 48 h in WB-F344. XBP1 splice form was transformed upon TG 24 h treatment. GAPDH was used as loading control. GAPDH, glycraldehyde-3-phosphate dehydrogenase; TG, tapsigargin. Supplementary Fig. 2 PD-MSCsPRL-1 regulated calcium channels in a rat BDL and hepatocyte treated with TG. a–d mRNA levels of calcium channels (e.g., IP3R, GRP75, VDAC1, and MCU) in a rat model with BDL. e-i mRNA levels of calcium channels (e.g., IP3R, GRP75, VDAC1, MCU, and CaM) exposed to TG (500 nM) for 24 h in WB-F344 by qRT-PCR. Data from each group are shown as the means ± SD and were assessed using Student’s t-test. *p < 0.05 vs. NTx, #p < 0.05 vs. PD-MSCs. BDL, bile duct ligation; CaM, calmodulin; GRP75, glucose regulated protein 75; IP3R, inositol trisphosphate receptor; MCU, mitochondria calcium uniporter; NTx, nontransplantation; PRL-1, phosphatase of regenerating liver-1; TG, thapsigargin; VDAC1, voltage dependent anion channel 1. Supplementary Fig. 3 Increased expression of SERCA2b and STIM1 in PD-MSCsPRL-1 groups in a rat model with BDL. a, b mRNA levels of ER-specific Ca2+ channel factor SERCA2b and Ca2+ sensor factor STIM1 in a rat model with BDL. Data from each group are shown as the means ± SD and were assessed using Student’s t-test. *p < 0.05 vs. NTx, #p < 0.05 vs. PD-MSCs. BDL, bile duct ligation; NTx, nontransplantation; SERCA2b, sarco/endoplasmic reticulum Ca2+ ATPase; PRL-1, phosphatase of regenerating liver-1; STIM1, stromal interaction molecule 1. Supplementary Fig. 4 PRL-1 regulates EGFR-PI3K-CaM calcium signaling in a BDL-injured rat liver and rat hepatocyte treated LCA. a mRNA levels of CaM and b PI3K-p85 in a rat model with BDL. c-e mRNA levels of intracellular calcium signaling (e.g., EGFR, PI3K, and CaM) induced LCA (100 μM) and treated recombinant PRL-1 (rePRL-1; 500 pg) in WB-F344. Data from each group are shown as the means ± SD and were assessed using Student’s t-test. *p < 0.05 vs. NTx, #p < 0.05 vs. PD-MSCs. BDL, bile duct ligation; CaM, calmodulin; EGFR, epidermal growth factor receptor; NTx, nontransplantation; PI3K, phosphatidylinositol-3-kinase. Supplementary Fig. 5 PD-MSCsPRL-1 modulated calcium channels in a rat hepatocyte treated with LCA by qRT-PCR. a-g mRNA levels related to intracellular calcium transport channels factors (e.g., SERCA2b, IP3R, VDAC1, MCU, GRP75, CaM, and STIM1) induced LCA (100 μM) and co-cultivation with naïve PD-MSCs or PD-MSCsPRL-1 in WB-F344. Data from each group are shown as the means ± SD and were assessed using Student’s t-test. *p < 0.05 vs. LCA (100 μM), #p < 0.05 vs. PD-MSCs. CaM, calmodulin; GRP75, glucose regulated protein 75; IP3R, inositol trisphosphate receptor; LCA, lithocholic acid; MCU, mitochondria calcium uniporter; PRL-1, phosphatase of regenerating liver-1; SERCA2b, sarco/endoplasmic reticulum Ca2+ ATPase; STIM1, stromal interaction molecule 1; VDAC1, voltage dependent anion channel 1. Supplementary Fig. 6 PD-MSCsPRL-1 regulated calcium channels in a rat hepatocyte treated with LCA and TG by western blotting. a Protein expression and b-f their intensities of intracellular calcium transport channels factors (e.g., SERCA2b, IP3R, VDAC1, MCU, and GRP75) induced LCA (100 μM) and co-cultivation with naïve PD-MSCs or PD-MSCsPRL-1 in WB-F344. g Protein expression and h-j their intensities of intracellular calcium transport channels factors (e.g., SERCA2b, and MCU) and liver regeneration factor induced LCA (100 μM) and co-cultivation with naïve PD-MSCs or PD-MSCsPRL-1 and Pentamidine (10 μg) treated in rat primary hepatocytes. GAPDH and α-tubulin was used as loading control. Data from each group are shown as the means ± SD and assessed using Student’s t-test. *p < 0.05 vs. LCA (100 μM), #p < 0.05 vs. PD-MSCs, $p < 0.05 vs. PD-MSCs or PD-MSCsPRL-1. ALB, Albumin; GAPDH, glycraldehyde-3-phosphate dehydrogenase; GRP75, glucose regulated protein 75; IP3R, inositol trisphosphate receptor; LCA, lithocholic acid; MCU, mitochondria calcium uniporter; PRL-1, phosphatase of regenerating liver-1; SERCA2b, sarco/endoplasmic reticulum Ca2+ ATPase; TG, Thapsigargin; VDAC1, voltage dependent anion channel 1. Supplementary Fig. 7 Recombinant PRL-1 increased calcium channels in a rat hepatocyte treated with LCA. a-g mRNA levels of intracellular calcium transport channels factors (e.g., SERCA2b, IP3R, VDAC1, MCU, GRP75, CaM, and STIM1) induced LCA (100 μM) and treated recombinant PRL-1 (rePRL-1; 500 pg) in WB-F344. Data from each group are shown as the means ± SD and assessed using Student’s t-test. *p < 0.05 vs. LCA (100 μM). CaM, calmodulin; GRP75, glucose regulated protein 75; IP3R, inositol trisphosphate receptor; LCA, lithocholic acid; MCU, mitochondria calcium uniporter; PRL-1, phosphatase of regenerating liver-1; SERCA2b, sarco/endoplasmic reticulum Ca2+ ATPase; VDAC1, voltage dependent anion channel 1.