Fig 1: BCL11A inhibition in natural killer/T-cell lymphoma (NKTL) cells. BCL11A silenced NKTL cells (siBCL11A) showed deregulated cell proliferation and upregulated apoptosis. (A) NKTL cells were transiently transfected with lipo2000, control siRNA (siControl), and siRNA against BCL11A (si-BCL11A). A significant reduction of BCL11A mRNA after transfected with si-BCL11A was observed across all NKTL cells. (B) Whole-cell lysates were prepared and processed for immunoblotting, probed with anti-BCL11A antibody. ß-Actin was used as a loading control. BCL11A protein expression was efficiently silenced after transfection with siBCL11A. (C) Transfected NKTL cells were stained with Annexin-V and propidium iodide and analyzed for the apoptosis rate by flow cytometry. BCL11A silenced NKTL cells showed an induction of apoptosis compared to cells transfected with control siRNA (siControl) and lipo2000. (D) Transfected NKTL cells were stained with BrdU and analyzed for the effects of si-BCL11A on the cell proliferation rate. The results show that cell proliferation was disrupted in BCL11A silenced NKTL cells (si-BCL11A).
Fig 2: Endogenous BCL11A expression in natural killer/T-cell lymphoma (NKTL) cells (SNK-1, NK-YS, HANK-1, and KHYG-1), NKTL patient samples and normal NK cells (NK01-NK02). (A) messenger RNA (mRNA) expression profiles of BCL11A in NKTL cells, normal NK cells, and NKTL patient samples. cDNA was converted from total RNA of normal NK, NKTL cells, and NKTL patient samples, subsequently assayed by quantitative real-time PCR (RT-PCR). BCL11A mRNA was upregulated in NKTL cells and NKTL patient samples compared to normal NK cells. (B) Protein profiles of BCL11A in NKTL cells, NKTL patient samples and normal NK cells. Cell lysates were probed with BCL11A (5G4) antibody. There was overexpression of BCL11A protein in NKTL cells and NKTL patient samples compared to normal NK cells.
Fig 3: Expression of RUNX3 and BCL11A protein in 16 NKTL patient samples were examined using immunohistochemistry. (A) According to percentages of cells with RUNX3 positivity, cases were divided into two groups: RUNX3 < 10% and ??10%. The scatter plot showed that cases with high RUNX3 protein expression (RUNX3??10%) showed a significantly higher median expression of BCL11A using Student’s t-test (P=0.0022). (B) Spearman correlation analysis suggest moderate correlation between RUNX3 and BCL11A protein expression levels (R=0.57, P =0.0007). (C) Representative images of H&E-staining, immunochemistry-staining of BCL11A and RUNX3 protein in samples. BCL11A and RUNX3 expression levels were high in case 1; BCL11A and RUNX3 expression levels were low in case 2.
Fig 4: Correlation of BCL11A, RUNX3, c-MYC, and P53 protein expressing levels. (A) Representative images of immunohistochemical expression of BCL11A, RUNX3, c-MYC, and P53 protein in two natural killer/T-cell lymphoma (NKTL) samples. In case 3, BCL11A protein expressing level was high, along with high RUNX3, c-MYC, and P53 protein expressing levels. In contrast, case 4 with low BCL11A protein expressing level showed low RUNX3, c-MYC, and P53 protein expressing levels. (B) Protein expression of BCL11A, RUNX3, c-MYC, and P53 after BCL11A knockdown. After efficiently silenced BCL11A as showed in Figure 2, RUNX3, c-MYC, and P53 expression profiles were analyzed post 96 h after BCL11A knockdown. Silencing of BCL11A sequentially deregulated RUNX3, c-MYC, and P53 expression in NKTL cells.
Fig 5: Survival curves of natural killer/T-cell lymphoma (NKTL) patients with high and low expression level of BCL11A. (A) Overall survival (OS) of test group of NKTL patients with high and low expression level of BCL11A. (B) Progression-free survival (PFS) of test group of NKTL patients with high and low expression level of BCL11A. (C) OS of validation group of NKTL patients with high and low expression level of BCL11A. (D) PFS of validation group of NKTL patients with high and low expression level of BCL11A.
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