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YM155 Chemical Structure
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Biological Activity
| Information | YM155 is a potent IAP (inhibitor of apoptosis proteins) inhibitor of survivin with IC50 of 0.54 nM. | |||||
|---|---|---|---|---|---|---|
| Targets | survivin | |||||
| IC50 | 0.54 nM [1] | |||||
| In vitro | YM155 is not sensitive to survivn gene promoter-driven luciferase reporter activity even at 30 μM. YM155 significantly inhibits endogenous survivin expression in PC-3 and PPC-1 human HRPC cells with deficient p53 through transcriptional inhibition of the survivin gene promoter. On the contrary YM155 shows no sufficient effect on protein expression of c-IAP2, XIAP, Bcl-2, Bcl-xL, Bad, α-actin, and β-tubulin at 100 nM. YM155 indicates great apoptosis in human cancer cell lines including PC-3 and PPC-1 with a concomitant increase in caspase-3 activity. YM155 potently inhibits human cancer cell lines (mutated or truncated p53) including PC-3, PPC-1, DU145, TSU-Pr1, 22Rv1, SK-MEL-5 and A375 with IC50 from 2.3 to 11 nM, respectively. [1] YM155 increases the sensitivity of NSCLC cells to γ-radiation. The combination of YM155 and γ-radiation increases both the number of apoptotic cells and the activity of caspase-3. YM155 delays the repair of radiation-induced double-strand breaks in nuclear DNA. [2] | |||||
| In vivo | YM155 completely inhibits the tumor growth of PC-3 s.c. xenografted prostate tumors at doses of 3 and 10 mg/kg, without body weight loss and blood cell count decrease. Pharmacokinetic analysis shows that YM155 is highly distributed to tumor tissue. Moreover, YM155 shows 80% TGI at a dose of 5 mg/kg in PC-3 orthotopic xenografts. [1] The combination therapy with YM155 and γ-radiation shows great antitumor activity against H460 or Calu6 xenografts in nude mice. [2] | |||||
| Clinical Trials | YM155 is currently in Phase II clinical trial in advanced non-small cell lung carcinoma. | |||||
| Features | ||||||
Protocol
Kinase Assay: [1]
| Promoter-luciferase reporter assay | A 2,767-bp sequence of human survivin gene promoter is isolated from human genomic DNA by PCR using Pyrobest polymerase and the following primers: 5’-GCGCGCTCGAGTCTAGACATGCGGATATATTC-3’ and 5’-GCGCGAA-GCTTTGGCGGTTAATGGCGCGC-3’. The resulting PCR fragment is digested with XhoI/HindIII and ligated into the XhoI/HindIII cleavage site of the pGL3-Basic vector. The resulting plasmid is named pSUR-luc. DNA sequencing is done on all amplified sequences by a DNA sequencer. The activity of pSUR-luc is confirmed by luciferase assay with transiently transfected HeLa-S3 cells. Luciferase assay is done. The pGL3 control vector, which contains the SV40 promoter and enhancer sequences, is used. HeLa cells are stably transfected with pSUR-luc and pSV2bsr by Lipofect-AMINE 2000. After blasticidin selection at 10 μg/mL, a single colony is chosen based on appropriate luciferase signals and genetic stability over time and named HeLa-SURP-luc. CHO cells are stably transfected with pGL3-control and pSV2bsr. After blasticidin selection at 10 μg/mL, a single colony is chosen based on appropriate luciferase signals and genetic stability over time and named CHO-SV40-luc. Stocked cells from the HeLa-SURP-luc and CHO-SV40-luc clones are used for chemical screening and characterization of YM155. YM155 in DMSO are added to the cells, which had been seeded the previous day on 96-well plastic plates at 5 × 103 per well. Luciferase activity is measured 24 hours later. IC50 is calculated by logistic analysis. |
|---|
Cell Assay: [1]
| Cell lines: | Hormone refractory prostate cancer cell lines (PC-3, PPC-1, DU145, TSU-Pr1 and 22Rv1) and malignant melanoma cell lines (SK-MEL-5 and A375) |
|---|---|
| Concentrations: | ~ 100 nM |
| Incubation Time: | 48 hours |
| Method: | Cells are seeded in 96-well plates at a density of 5-40 × 103. YM155 is dissolved in DMSO and added to cells for 48 hours. Then the cell count is determined by sulforhodamine B assay. |
Animal Study:[1]
Chemical Information
| Molecular Weight (WM): | 443.29 |
|---|---|
| Formula: | C20H19BrN4O3 |
| CAS No.: | 781661-94-7 |
| Synonyms: |
N/A
|
| Dissolve in (25°C): | DMSO ≥89mg/mL |
| Water ≥89mg/mL | |
| Ethanol ≥24mg/mL | |
| Storage: | 2 years-20°CPowder |
| 1 week-4°Cin DMSO | |
| 1 month-80°in DMSO |
Quality Control & MSDS
Research Area
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Selleck's high quality products have been used in several published research findings, including the following:
Survivin Inhibition Is Critical for Bcl-2 Inhibitor-Induced Apoptosis in Hepatocellular Carcinoma Cells
Burn-induced apoptosis of cardiomyocytes is survivin dependent and regulated by PI3K/Akt, p38 MAPK and ERK pathways
Targeting survivin and p53 in pediatric acute lymphoblastic leukemia
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YM-155 sensitizes ABT-263-induced apoptosis in HCC cells. A. LH86 and B. Huh7 cells were untreated or treated with ABT-263(1 mM), YM-155(1 mM) or combination of ABT-263(1 mM) and YM-155(1 mM) for up to 6 h. Then apoptotic cells were assessed as in Figure 2A and2B (representative apoptotic cells were marked with white arrows). C. LH86 and D. Huh7 cells were untreated or treated with ABT-263(1 mM), YM-155(1 mM) or combination of ABT-263(1 mM) and YM-155(1 mM) for 6 h. Cells with apoptotic nuclei were counted to determine cell death ratio (*p,0.05, **p,0.05). E. LH86 cells and F. Huh7 cells were treated as indicated and cell lysates were prepared and subjected to Western blotting.Apoptosis was evaluated through caspase 3 activation. b-actin was used as an equal protein loading control. G. LH86 cells grown in six-well plate were untreated (control) or treated with different conditions as indicated for 48 h. After rinsed with fresh culture medium for 3 times, cells were cultured for another two weeks. Cell colony formation assays were performed with crystal violet staining. H. colony number were counted to show combination treatment with ABT-263 and YM-155 resulted in reduction of clonogenesis (#p<0.05). - YM-155 sensitizes ABT-263-induced apoptosis in HCC cells. A. LH86 and B. Huh7 cells were untreated or treated with ABT-263(1 mM), YM-155(1 mM) or combination of ABT-263(1 mM) and YM-155(1 mM) for up to 6 h. Then apoptotic cells were assessed as in Figure 2A and2B (representative apoptotic cells were marked with white arrows). C. LH86 and D. Huh7 cells were untreated or treated with ABT-263(1 mM), YM-155(1 mM) or combination of ABT-263(1 mM) and YM-155(1 mM) for 6 h. Cells with apoptotic nuclei were counted to determine cell death ratio (*p,0.05, **p,0.05). E. LH86 cells and F. Huh7 cells were treated as indicated and cell lysates were prepared and subjected to Western blotting.Apoptosis was evaluated through caspase 3 activation. b-actin was used as an equal protein loading control. G. LH86 cells grown in six-well plate were untreated (control) or treated with different conditions as indicated for 48 h. After rinsed with fresh culture medium for 3 times, cells were cultured for another two weeks. Cell colony formation assays were performed with crystal violet staining. H. colony number were counted to show combination treatment with ABT-263 and YM-155 resulted in reduction of clonogenesis (#p<0.05).
Data from [PLoS ONE 2011 August;6: e21980] YM155 purchased from Selleck
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Survivin down-regulation sensitizes ABT-263-induced apoptosis in HCC cells. A. LH86 cells were treated as indicated and cell lysates were prepared for Western blotting. Pro-apoptotic proteins: Bax, Bad, and Bak and anti-apoptotic proteins Bcl-xL and Mcl-1 were assessed with specific antibodies respectively. b-actin was detected and served as an equal protein loading control. B. LH86 cells were untreated or treated with ABT-263 (1 mM), YM-155 (1 mM) or combination of ABT-263 (1 mM) and YM155 (1 mM) for up to 6 h as indicated. Then cells were harvested and cell lysates were prepared for Western blotting. Anti-survivin and anti-Bcl-xL polyclonal antibodies were used to assess protein levels for survivin and Bcl-xL respectively. b-actin was used as an equal protein loading control. The band intensities of survivin, Bcl-xL, and b-actin was qualified with Image J software. C. LH86 cells were transiently transfected with synthesized random siRNA (control) or survivin specific siRNA duplexes, and 48 h posttransfection, cells were subjected to Western blotting analysis with anti-survivin polyclonal antibody. b-actin was used as an equal protein loading control. D. LH86 cells were transfected with synthesized random control siRNA or survivin specific siRNA, and 48 h post-transfection, cells were untreated or treated with ABT-263 (1 mM) for 24 h and then subjected to Hoechst staining to show apoptotic cells with condensed nuclei (representative apoptotic cells were marked with white arrows). E. LH86 cells were treated as in Figure 4D and apoptosis was measured as in Figure 2A. Statistical analysis was performed for apoptosis ratio by counting the number of cells with apoptotic nuclei (*p,0.05). F. LH86 cells treated as in Figure 4D were harvested and cell lysates were prepared and subjected to Western blotting. Apoptosis was determined through caspase 3 activation. b-actin was used as an equal protein loading control. - Survivin down-regulation sensitizes ABT-263-induced apoptosis in HCC cells. A. LH86 cells were treated as indicated and cell lysates were prepared for Western blotting. Pro-apoptotic proteins: Bax, Bad, and Bak and anti-apoptotic proteins Bcl-xL and Mcl-1 were assessed with specific antibodies respectively. b-actin was detected and served as an equal protein loading control. B. LH86 cells were untreated or treated with ABT-263 (1 mM), YM-155 (1 mM) or combination of ABT-263 (1 mM) and YM155 (1 mM) for up to 6 h as indicated. Then cells were harvested and cell lysates were prepared for Western blotting. Anti-survivin and anti-Bcl-xL polyclonal antibodies were used to assess protein levels for survivin and Bcl-xL respectively. b-actin was used as an equal protein loading control. The band intensities of survivin, Bcl-xL, and b-actin was qualified with Image J software. C. LH86 cells were transiently transfected with synthesized random siRNA (control) or survivin specific siRNA duplexes, and 48 h posttransfection, cells were subjected to Western blotting analysis with anti-survivin polyclonal antibody. b-actin was used as an equal protein loading control. D. LH86 cells were transfected with synthesized random control siRNA or survivin specific siRNA, and 48 h post-transfection, cells were untreated or treated with ABT-263 (1 mM) for 24 h and then subjected to Hoechst staining to show apoptotic cells with condensed nuclei (representative apoptotic cells were marked with white arrows). E. LH86 cells were treated as in Figure 4D and apoptosis was measured as in Figure 2A. Statistical analysis was performed for apoptosis ratio by counting the number of cells with apoptotic nuclei (*p,0.05). F. LH86 cells treated as in Figure 4D were harvested and cell lysates were prepared and subjected to Western blotting. Apoptosis was determined through caspase 3 activation. b-actin was used as an equal protein loading control.
Data from [PLoS ONE 2011 August;6: e21980] YM155 purchased from Selleck
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Survivin inhibitor increased apoptosis in burn serum-stimulated cardiomyocytes. a YM155 increased apoptosis in burn serumstimulated cardiomyocytes in a concentration-dependent manner. Neonatal rat cardiomyocytes were treated with YM155 (3–300 nM at the indicated) for 2 h prior to stimulation burn serum for 12 h. The extent of DNA fragmentation was quantified using the Cell Death Detection ELISA. versus 0 nM YM155 plus stimulation with burn serum. b YM155 (100 nM) pretreatment increased the apoptosis production at 2 or 12 h after burn serum stimulation. c Representative blots of survivin and cleaved caspase-3 in YM155 (100 nM) pretreated cardiomyocytes at 2 and 12 h after burn serum stimulation. d Bar graphs show the relative proteins. - Survivin inhibitor increased apoptosis in burn serum-stimulated cardiomyocytes. a YM155 increased apoptosis in burn serumstimulated cardiomyocytes in a concentration-dependent manner. Neonatal rat cardiomyocytes were treated with YM155 (3–300 nM at the indicated) for 2 h prior to stimulation burn serum for 12 h. The extent of DNA fragmentation was quantified using the Cell Death Detection ELISA. versus 0 nM YM155 plus stimulation with burn serum. b YM155 (100 nM) pretreatment increased the apoptosis production at 2 or 12 h after burn serum stimulation. c Representative blots of survivin and cleaved caspase-3 in YM155 (100 nM) pretreated cardiomyocytes at 2 and 12 h after burn serum stimulation. d Bar graphs show the relative proteins.
Data from [Basic Res Cardiol 2011 June;ahead of print] YM155 purchased from Selleck
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Induction of cardiomyocytes apoptosis by survivin inhibitor in vivo. After YM155 was administered (5 mg/kg/day) for 5 days, the rats were exposed to a 40% TBSA burn (burn injury) or 25C water (sham) and killed 6 h after burn injury. The frozen sections of the ventricular tissues or whole cell lysates were prepared. Apoptotic staining was performed using the TUNEL method and immunostained using a-sarcomeric actin. The survivin and cleaved caspase-3 levels were measured by Western blot analysis. a Representative blots of survivin and cleaved caspase-3. b The statistical analysis of the relative proteins .c Figures are representative of two independent TUNEL experiments. Green fluorescence represents apoptotic cells, whereas red stain indicates staining for a-sarcomeric actin specific for cardiac myocytes. d Bar graph summarizes the counted apoptotic cells.
Induction of cardiomyocytes apoptosis by survivin inhibitor in vivo. After YM155 was administered (5 mg/kg/day) for 5 days, the rats were exposed to a 40% TBSA burn (burn injury) or 25C water (sham) and killed 6 h after burn injury. The frozen sections of the ventricular tissues or whole cell lysates were prepared. Apoptotic staining was performed using the TUNEL method and immunostained using a-sarcomeric actin. The survivin and cleaved caspase-3 levels were measured by Western blot analysis. a Representative blots of survivin and cleaved caspase-3. b The statistical analysis of the relative proteins .c Figures are representative of two independent TUNEL experiments. Green fluorescence represents apoptotic cells, whereas red stain indicates staining for a-sarcomeric actin specific for cardiac myocytes. d Bar graph summarizes the counted apoptotic cells.
Data from [Basic Res Cardiol 2011 June;ahead of print] YM155 purchased from Selleck
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Dose response of ALL cell lines to YM155. Asynchronous populations of cells were treated with increasing doses of YM155 for 72 h. Then, viability was measured by MTS and normalized to no drug control. S.e.m. bars are inserted. Dotted line represents 50% viability.
Dose response of ALL cell lines to YM155. Asynchronous populations of cells were treated with increasing doses of YM155 for 72 h. Then, viability was measured by MTS and normalized to no drug control. S.e.m. bars are inserted. Dotted line represents 50% viability.
Data from [Leukemia 2011 September;ahead of print] YM155 purchased from Selleck
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Treatment of SUPB15 cells with imatinib or YM155. Top panel shows cells treated with siRNA in the presence of 500 nM imatinib. Cells were treated with siRNA, and then subsequently incubated in 500 nM imatinib for 96 h. Bottom panel shows the partial rescue of SUPB15 cells treated with 100 nM YM155 for 96 h. S.e.m. bars are inserted into each graph.
Treatment of SUPB15 cells with imatinib or YM155. Top panel shows cells treated with siRNA in the presence of 500 nM imatinib. Cells were treated with siRNA, and then subsequently incubated in 500 nM imatinib for 96 h. Bottom panel shows the partial rescue of SUPB15 cells treated with 100 nM YM155 for 96 h. S.e.m. bars are inserted into each graph.
Data from [Leukemia 2011 September;ahead of print] YM155 purchased from Selleck
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Total RNA from livers of these mice were isolated from tissues using TRIZOL (Invitrogen). cDNA synthesis was performed with the M-MLV RTase cDNA Synthesis Kit (Promega). qRT-PCR reactions were performed using SYBR Green (Takara) on ABI 7500 Fast system. Expression levels of Survivin gene were measured by qRT-PCR in livers injected with 0.9% Nacl (91#,92#) or YM155 48 hours after DEN treatment.
Total RNA from livers of these mice were isolated from tissues using TRIZOL (Invitrogen). cDNA synthesis was performed with the M-MLV RTase cDNA Synthesis Kit (Promega). qRT-PCR reactions were performed using SYBR Green (Takara) on ABI 7500 Fast system. Expression levels of Survivin gene were measured by qRT-PCR in livers injected with 0.9% Nacl (91#,92#) or YM155 48 hours after DEN treatment.
Data independently produced by Lihua Min of Chinese Academy of Sciences YM155 purchased from Selleck
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Western blot analysis of Survivin. U-251 and PC-3 cell line was treated with 0-100nM YM-155.
Western blot analysis of Survivin. U-251 and PC-3 cell line was treated with 0-100nM YM-155.
Data independently produced by Dr Chunrong Yu of RoswelI Park Cancer Institute YM155 purchased from Selleck
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| YM-155 sensitizes ABT-263-induced apoptosis in HCC cells. A. LH86 and B. Huh7 cells were untreated or treated with ABT-263(1 mM), YM-155(1 mM) or combination of ABT-263(1 mM) and YM-155(1 mM) for up to 6 h. Then apoptotic cells were assessed as in Figure 2A and2B (representative apoptotic cells were marked with white arrows). C. LH86 and D. Huh7 cells were untreated or treated with ABT-263(1 mM), YM-155(1 mM) or combination of ABT-263(1 mM) and YM-155(1 mM) for 6 h. Cells with apoptotic nuclei were counted to determine cell death ratio (*p,0.05, **p,0.05). E. LH86 cells and F. Huh7 cells were treated as indicated and cell lysates were prepared and subjected to Western blotting.Apoptosis was evaluated through caspase 3 activation. b-actin was used as an equal protein loading control. G. LH86 cells grown in six-well plate were untreated (control) or treated with different conditions as indicated for 48 h. After rinsed with fresh culture medium for 3 times, cells were cultured for another two weeks. Cell colony formation assays were performed with crystal violet staining. H. colony number were counted to show combination treatment with ABT-263 and YM-155 resulted in reduction of clonogenesis (#p<0.05). |
Data from [PLoS ONE 2011 August;6: e21980]
| Survivin down-regulation sensitizes ABT-263-induced apoptosis in HCC cells. A. LH86 cells were treated as indicated and cell lysates were prepared for Western blotting. Pro-apoptotic proteins: Bax, Bad, and Bak and anti-apoptotic proteins Bcl-xL and Mcl-1 were assessed with specific antibodies respectively. b-actin was detected and served as an equal protein loading control. B. LH86 cells were untreated or treated with ABT-263 (1 mM), YM-155 (1 mM) or combination of ABT-263 (1 mM) and YM155 (1 mM) for up to 6 h as indicated. Then cells were harvested and cell lysates were prepared for Western blotting. Anti-survivin and anti-Bcl-xL polyclonal antibodies were used to assess protein levels for survivin and Bcl-xL respectively. b-actin was used as an equal protein loading control. The band intensities of survivin, Bcl-xL, and b-actin was qualified with Image J software. C. LH86 cells were transiently transfected with synthesized random siRNA (control) or survivin specific siRNA duplexes, and 48 h posttransfection, cells were subjected to Western blotting analysis with anti-survivin polyclonal antibody. b-actin was used as an equal protein loading control. D. LH86 cells were transfected with synthesized random control siRNA or survivin specific siRNA, and 48 h post-transfection, cells were untreated or treated with ABT-263 (1 mM) for 24 h and then subjected to Hoechst staining to show apoptotic cells with condensed nuclei (representative apoptotic cells were marked with white arrows). E. LH86 cells were treated as in Figure 4D and apoptosis was measured as in Figure 2A. Statistical analysis was performed for apoptosis ratio by counting the number of cells with apoptotic nuclei (*p,0.05). F. LH86 cells treated as in Figure 4D were harvested and cell lysates were prepared and subjected to Western blotting. Apoptosis was determined through caspase 3 activation. b-actin was used as an equal protein loading control. |
Data from [PLoS ONE 2011 August;6: e21980]
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