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Methylation-associated silencing of BASP1 contributes to leukemogenesis in t(8;21) acute myeloid leukemia

Zhou, Lei, Fu, Lin, Lv, Na, Liu, Jing, Li, Yan, Chen, Xiaosu, Xu, Qingyu, Chen, Guofeng, Pang, Baoxu, Wang, Lili, Li, Yonghui, Zhang, Xiaodong, Yu, Li·2018·Experimental & Molecular Medicine
DOI 10.1038/s12276-018-0067-4PMC PMC5938046
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Fig. 1 BASP1 expression is selectively down-regulated in A/E-positive AML. a Expression of BASP1 is down-regulated in A/E-positive cell lines (Kasumi-1 and SKNO-1) compared to the other A/E-negative AML cell lines (NB4, U937, THP-1, KG-1, MV-4-11, HEL, and HL-60) and three sets of normal bone marrow (NBM). b Expression of BASP1 in different subtypes of AML and hematopoietic stem cells (HSC) analyzed from the GEO dataset (GSE13159). BASP1 expression was down-regulated in t(8;21) AML in contrast to the other subtypes of AML and HSC (***p < 0.001). c The protein level of BASP1 was detected by western blotting in AML cell lines. β-actin was used as a control. d mRNA expression of BASP1 was plotted against that of AML1-ETO in A/E-positive AML (n = 60) (GSE13159). The plot of BASP1 versus AML1-ETO expression showed an inverse correlation (r = -0.38, p = 0.0027). e Upper panel: mRNA expression of BASP1 was measured in two pairs of cell lines: SKNO-1 and SKNO-1-siA/E, and U937 and U937-A/E. GAPDH was used as a control (**p < 0.01, ***p < 0.001). Lower panel: The protein levels of BASP1 were detected by western blotting. β-Actin was used as the control
Fig. 1 BASP1 expression is selectively down-regulated in A/E-positive AML. a Expression of BASP1 is down-regulated in A/E-positive cell lines (Kasumi-1 and SKNO-1) compared to the other A/E-negative AML cell lines (NB4, U937, THP-1, KG-1, MV-4-11, HEL, and HL-60) and three sets of normal bone marrow (NBM). b Expression of BASP1 in different subtypes of AML and hematopoietic stem cells (HSC) analyzed from the GEO dataset (GSE13159). BASP1 expression was down-regulated in t(8;21) AML in contrast to the other subtypes of AML and HSC (***p < 0.001). c The protein level of BASP1 was detected by western blotting in AML cell lines. β-actin was used as a control. d mRNA expression of BASP1 was plotted against that of AML1-ETO in A/E-positive AML (n = 60) (GSE13159). The plot of BASP1 versus AML1-ETO expression showed an inverse correlation (r = -0.38, p = 0.0027). e Upper panel: mRNA expression of BASP1 was measured in two pairs of cell lines: SKNO-1 and SKNO-1-siA/E, and U937 and U937-A/E. GAPDH was used as a control (**p < 0.01, ***p < 0.001). Lower panel: The protein levels of BASP1 were detected by western blotting. β-Actin was used as the controlCC BY-NC-SA · PubMed Central
Fig. 2 The BASP1 promoter is highly methylated in A/E-positive AML. a Schematic diagrams of the CpG island of BASP1 promoter sequences (−2000 to −1 bp). The horizontal line (F1–R1) indicates the location of the primer used in the BSP assays. b Genomic bisulfate sequencing was performed to detect the methylation status of the DNA sequences in the CpG island of the BASP1 promoter from the indicated leukemia cell lines and normal bone marrow. Black dots and white dots indicate methylated and unmethylated CpG cytosine, respectively. c DNA methylation of BASP1 in nine A/E-positive AML cases (#) and three normal bone marrow samples (N) was demonstrated by MSP. M methylated allele, U unmethylated allele. d Upper panel: mRNA expression of BASP1 was up-regulated after continuous treatment with 0.5 or 1.0 µmol/L decitabine (DAC) for 3 days compared to the vehicle in Kasumi-1 and SKNO-1. GAPDH was used as a control. Error bars show the SD from three different assays (*p < 0.05, **p < 0.01). Lower panel: The protein levels of BASP1 were detected by western blotting. β-Actin was used as a control
Fig. 2 The BASP1 promoter is highly methylated in A/E-positive AML. a Schematic diagrams of the CpG island of BASP1 promoter sequences (−2000 to −1 bp). The horizontal line (F1–R1) indicates the location of the primer used in the BSP assays. b Genomic bisulfate sequencing was performed to detect the methylation status of the DNA sequences in the CpG island of the BASP1 promoter from the indicated leukemia cell lines and normal bone marrow. Black dots and white dots indicate methylated and unmethylated CpG cytosine, respectively. c DNA methylation of BASP1 in nine A/E-positive AML cases (#) and three normal bone marrow samples (N) was demonstrated by MSP. M methylated allele, U unmethylated allele. d Upper panel: mRNA expression of BASP1 was up-regulated after continuous treatment with 0.5 or 1.0 µmol/L decitabine (DAC) for 3 days compared to the vehicle in Kasumi-1 and SKNO-1. GAPDH was used as a control. Error bars show the SD from three different assays (*p < 0.05, **p < 0.01). Lower panel: The protein levels of BASP1 were detected by western blotting. β-Actin was used as a controlCC BY-NC-SA · PubMed Central
Fig. 3 A/E inactivates BASP1 through direct promoter binding. a The left diagram shows a luciferase reporter containing various lengths of the BASP1 promoter region with wild-type A/E-binding sites1–4 or mutated sequence (mut). Luciferase reporter assays showed that A/E repressed the transcriptional activity of the BASP1 promoter. b ChIP was performed in the SKNO-1 and SKNO-1-siA/E cell lines using anti-AML1, anti-ETO, anti-DNMT1, anti-DNMT3a, and anti-DNMT3b antibodies or a non-specific antibody (IgG control). Quantitative RT-PCR was performed with primers specific for the BASP1 promoter region surrounding the predicted −546/−556 binding site and expression was quantified as 2−ΔCT relative to input. ChIP-PCR showed that A/E and DNMT3a bound the BASP1 promoter (*p < 0.05, **p < 0.01)
Fig. 3 A/E inactivates BASP1 through direct promoter binding. a The left diagram shows a luciferase reporter containing various lengths of the BASP1 promoter region with wild-type A/E-binding sites1–4 or mutated sequence (mut). Luciferase reporter assays showed that A/E repressed the transcriptional activity of the BASP1 promoter. b ChIP was performed in the SKNO-1 and SKNO-1-siA/E cell lines using anti-AML1, anti-ETO, anti-DNMT1, anti-DNMT3a, and anti-DNMT3b antibodies or a non-specific antibody (IgG control). Quantitative RT-PCR was performed with primers specific for the BASP1 promoter region surrounding the predicted −546/−556 binding site and expression was quantified as 2−ΔCT relative to input. ChIP-PCR showed that A/E and DNMT3a bound the BASP1 promoter (*p < 0.05, **p < 0.01)CC BY-NC-SA · PubMed Central
Fig. 4 Ectopic expression of BASP1 in SKNO-1 cells inhibits proliferation, suppresses colony formation, and increases apoptosis and cell cycle arrest. a The CCK-8 assay was performed on SKNO-1 cells transduced with the GFP-tagged BASP1 lentiviral or GFP control plasmids at the indicated time points. b A colony formation assay was performed on SKNO-1 cells transduced with the GFP-tagged BASP1 lentiviral or GFP control plasmids and grown for 7 days. c Cell cycle analyses in SKNO-1 cells by flow cytometry showed that BASP1 overexpression induced the G1 phase arrest and blocked S-phase entry. d The induction of apoptosis in BASP1 overexpressing cells was measured using Annexin V-7AAD staining via flow cytometry. Error bars indicates the SD from three different assays (*p < 0.05)
Fig. 4 Ectopic expression of BASP1 in SKNO-1 cells inhibits proliferation, suppresses colony formation, and increases apoptosis and cell cycle arrest. a The CCK-8 assay was performed on SKNO-1 cells transduced with the GFP-tagged BASP1 lentiviral or GFP control plasmids at the indicated time points. b A colony formation assay was performed on SKNO-1 cells transduced with the GFP-tagged BASP1 lentiviral or GFP control plasmids and grown for 7 days. c Cell cycle analyses in SKNO-1 cells by flow cytometry showed that BASP1 overexpression induced the G1 phase arrest and blocked S-phase entry. d The induction of apoptosis in BASP1 overexpressing cells was measured using Annexin V-7AAD staining via flow cytometry. Error bars indicates the SD from three different assays (*p < 0.05)CC BY-NC-SA · PubMed Central

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Cited by

Metadata

Authors
Zhou, L., Fu, L., Lv, N., Liu, J., Li, Y., Chen, X., Xu, Q., Chen, G., Pang, B., Wang, L., Li, Y., Zhang, X., & Yu, L.
Venue
Experimental & Molecular Medicine
Publisher
Springer Science and Business Media LLC
Published
2018-04
Volume
50
Issue
4
Pages
1-8
ISSN
  • 1226-3613
  • 2092-6413
DOI
10.1038/s12276-018-0067-4
PMC
PMC5938046
Cited by
24
References
0
Language
en
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